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Chapter 7 : Modulatory Role of Modified Nucleotides in RNA Loop-Loop Interaction

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Abstract:

The anticodon stem loop of tRNA is one of the most remarkable hairpins in RNAs that present several modified nucleotides arising by posttranscriptional processes. Many different modifications have been identified at position 34. These modifications are considered to be important for the specificity, fidelity, and efficiency of the tRNA functions, mainly in decoding the genetic message during translation on the ribosome. This chapter summarizes the information available about the role of modified nucleotides present at positions 34 and 37 in modulating tRNA anticodon-anticodon interaction. Implications for codon-anticodon interaction and comparison with other types of RNA-RNA interacting systems are also discussed in this chapter. One way to evaluate the effect of modified nucleotides on the stability and dynamic properties of anticodon-anticodon complexes is the temperature-jump relaxation technique. The chapter describes two RNA loop-loop interacting systems that do not involve modified nucleotides. Their comparison with the loop-loop interacting systems involving hairpins of tRNA molecules described in this chapter are interesting to better understand how modified nucleotides can restrict the interaction to only a few selected nucleotides within the interacting RNA loops. Comparison to other types of loop-loop complexes involving RNAs other than tRNAs, the so-called "kissing" complexes, is also made. The main difference between these different types of loop-loop complexes is the extent of base pairing between the nucleotides of the interacting loops.

Citation: Grosjean H, Houssier C, Romby P, Marquet R. 1998. Modulatory Role of Modified Nucleotides in RNA Loop-Loop Interaction, p 113-133. In Grosjean H, Benne R (ed), Modification and Editing of RNA. ASM Press, Washington, DC. doi: 10.1128/9781555818296.ch7

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Figures

Image of Figure 1
Figure 1

Type and location of modified nucleotides in the anticodon stem and loop of tRNAs. The upper part is a schematic representation of the three-dimensional architecture of tRNA. Numbering of nucleotide positions are those universally adopted (see Appendix 5 by Auffinger and Westhof). The anticodon nucleotides corresponding to positions 34, 35, and 36 are shown as square boxes in the anticodon hairpin representation (lower part of the figure). Symbols for modified nucleotides are those defined in Appendix 1 by Motorin and Grosjean. The information is derived from the tRNA data bank of Sprinzl et al. (1996). Frequency of modified nucleotides at specific positions can be obtained from the compilation of and from the data in Appendix 5 by Auffinger and Westhof. Almost all of the hyper-modified nucleotides characterized so far occur exclusively in position 34 (the so-called wobble base) or in position 37 (3′-adjacent to the anticodon); see also Appendix 6 by Björk. Notice also that all positions of the anticodon hairpin (except positions 33, 42, and 43) are potential sites for modification, especially for pseudouridylation (Ψ).

Citation: Grosjean H, Houssier C, Romby P, Marquet R. 1998. Modulatory Role of Modified Nucleotides in RNA Loop-Loop Interaction, p 113-133. In Grosjean H, Benne R (ed), Modification and Editing of RNA. ASM Press, Washington, DC. doi: 10.1128/9781555818296.ch7
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Image of Figure 2
Figure 2

Schematic representation of complexes formed between two tRNAs having complementary anticodons. Only the nucleotides present in the 7-member anticodon loops are indicated. However, the invariant uridine-33, 5′-adjacent to the wobble base, is omitted for better clarity of the figure. Out of the 60 anticodon-anticodon complexes we have studied, only those having their 3 anticodon nucleotides engaged in canonical A•U, G•C or l•C Watson-Crick base pairs are represented (no mismatch base pairs). Symbols for modified nucleotides are defined in Appendix 1 by Motorin and Grosjean. U* at position 34 of tRNA designates a yet unidentified modified uridine (possibly a derivative of nmU or mnmU). Sequence information originates from the tRNA data bank of Sprinzl et al., 1998.

Citation: Grosjean H, Houssier C, Romby P, Marquet R. 1998. Modulatory Role of Modified Nucleotides in RNA Loop-Loop Interaction, p 113-133. In Grosjean H, Benne R (ed), Modification and Editing of RNA. ASM Press, Washington, DC. doi: 10.1128/9781555818296.ch7
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Image of Figure 3
Figure 3

Comparison of complexes formed between complementary sequences in various polynucleotides, (a) Two triplets mimicking the anticodons of tRNA and tRNA. (b) Anticodon triplet corresponding to tRNA and its complementary sequence within an anticodon hairpin of yeast tRNA (harboring naturally occurring modified nucleotides). Only the anticodon loop and the proximal anticodon stem are represented, despite the fact that the experiments described in the text concern the entire yeast tRNAPhe, (c) The complementary sequences are both part of the anticodon loop of the entire tRNAs ( tRNA and yeast tRNA) (again only the anticodon loop and proximal anticodon stem are presented), (d) The interaction between a fragment of tRNA (10-mer) and fragment of yeast tRNA (12-mer) is shown, both fragments bearing their respective anticodon sequence. These fragments were obtained after purification of the RNase T hydrolysate of the corresponding tRNAs. Association constants were determined at ionic strength 0.1, 10 mM Mg at pH 6.8, by the T-jump relaxation technique. Symbols for modified nucleotides are those of Appendix 1 by Motorin and Grosjean. For more details see and .

Citation: Grosjean H, Houssier C, Romby P, Marquet R. 1998. Modulatory Role of Modified Nucleotides in RNA Loop-Loop Interaction, p 113-133. In Grosjean H, Benne R (ed), Modification and Editing of RNA. ASM Press, Washington, DC. doi: 10.1128/9781555818296.ch7
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Image of Figure 4
Figure 4

Comparison of relaxation time constants (lifetimes) of different types of nucleic acid associations at 20°C. The left part of the figure shows data concerning duplex formation using synthetic oligoribonucleotides. They were kindly provided by D. Pörschke(MPI of Göttingen, Germany ). On the right part of the figure are the data concerning tRNA anticodon-anticodon complexes. Only a few selected examples are illustrated on this figure: the complete set of tRNA pairs are given in Fig. 2 ; see also Grosjean et al., 1978; Vacher et al., 1984; Houssier and Grosjean, 1985; and Romby et al., 1985). The time scale is logarithmic. Relaxation time constants of the bimolecular reactions are given at zero concentration and correspond to the reverse of the kinetic rate constants of the dissociation of the complexes.

Citation: Grosjean H, Houssier C, Romby P, Marquet R. 1998. Modulatory Role of Modified Nucleotides in RNA Loop-Loop Interaction, p 113-133. In Grosjean H, Benne R (ed), Modification and Editing of RNA. ASM Press, Washington, DC. doi: 10.1128/9781555818296.ch7
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Image of Figure 5
Figure 5

Schematic representation of complexes formed between two tRNAs having complementary anticodons. In boxes are the nucleotides for which the effect of alteration of the chemical structure or substitution by another nucleotide have been measured (see Table 1 ). Only the nucleotides present in positions 34–38 of the anticodon loops are indicated. W* stands for wobble base-34; R* stands for purine 37; all other symbols for modified nucleotides are as in Appendix 1 by Motorin and Grosjean. The different tRNA pairs are as follows, (a) tRNA (wild type or chemically treated to oxidize the thiol group in mnmsU, ) and yeast tRNA (wild type or chemically treated under acidic conditions to remove the Wye base; ). (b) tRNA (wild type) and tRNA or tRNA (both wild type; ). (c) tRNA (wild type) and tRNA (wild type or the mutant lacking the msi group on A; ). (d) tRNA (wild type) and tRNA or yeast tRNA (both wild type; ). (e) tRNA (wild type) and yeast tRNA (species I and II). Both species were purified from the same yeast strain; species II was shown to lack the t group on A ( ). Notice that in this example, a G•U wobble occurs within the anticodon-anticodon complex, (f) tRNA (wild type) and tRNA or yeast tRNA (both wild type; ). Here, two parameters vary (G and mG in the yeast tRNA versus Q and mA in the tRNA). Therefore, the data obtained with this tRNA pair cannot be interpreted solely on the basis of one nucleotide difference, as in all of the other cases above. The T-jump relaxation technique was used to compare the relative stability of the different tRNA pairs (wild types and mutants; see Table 1 ).

Citation: Grosjean H, Houssier C, Romby P, Marquet R. 1998. Modulatory Role of Modified Nucleotides in RNA Loop-Loop Interaction, p 113-133. In Grosjean H, Benne R (ed), Modification and Editing of RNA. ASM Press, Washington, DC. doi: 10.1128/9781555818296.ch7
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Image of Figure 6
Figure 6

Correlation between the relative order of the stacking energy of base pairs (a) and the presence of modified bases located at position 37 of the anticodon loop of tRNA (b). (a) Classification of the 10 possible Watson-Crick base paired nearest-neighbor sequences (notice that GG•CC and CC•GG as well as UU•AA and AA•UU are identical) according to measured thermodynamic parameters taken from Borer et al., 1974, and largely confirmed later ( ). (b) Correlation between the nucleotide at position 36 of anticodon in tRNA (cardinal nucleotide; ) and the type of modified nucleotide found at position 37 of tRNA from different origins. Î’, E, and A in parentheses stand for eubacteria, eukaryotes, and archaea, respectively; , mitochondria, and chloroplasts have been excluded from the compilation. Symbols for modified nucleotides are those defined in Appendix 1 by Motorin and Grosjean. The most frequent modified nucleotides are doubly underlined. Ν stands for any nucleotide. For more detailed information see Appendix 6 by Björk or Sprinzl et al., 1998.

Citation: Grosjean H, Houssier C, Romby P, Marquet R. 1998. Modulatory Role of Modified Nucleotides in RNA Loop-Loop Interaction, p 113-133. In Grosjean H, Benne R (ed), Modification and Editing of RNA. ASM Press, Washington, DC. doi: 10.1128/9781555818296.ch7
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Figure 7

Structural model for the tRNA anticodon-anticodon interaction. The case of duplex formation with yeast tRNA is illustrated because the crystal structure of this duplex at a 3-Å resolution is known ( ). (A) Nucleotide sequences of the interacting anticodon hairpins; (B) stereo view of the interacting anticodon loops of yeast tRNA (only the segment from Ψ to A is shown). In this complex, the three bases of the anticodon stack in a helical conformation (Α-form) with the purine 37 and the pyrimidine 38 on their 3′ side. The two pyrimidines on the 5′ side of the loop are stacked together but separated from the other stacked bases by a short bend. The two-fold rotational axis is perpendicular to this paper, through the bond joining the two middle bases of the anticodon (here a U•U mismatch). The double helix composed of the three anticodon base pairs is sandwiched (coaxially stacked) into an almost continuous double helix (Α-form) which includes the anticodon stems of both tRNAs. The extensive stacking interactions generated in this structure explain the stabilizing effects of the anticodon stems and of the modified purine (often hypermodified residues) 3′-adjacent to the anticodon ending with A or U (see Fig. 6 ). The crystal structure (as discussed in ) fully confirmed the earlier model proposed by .

Citation: Grosjean H, Houssier C, Romby P, Marquet R. 1998. Modulatory Role of Modified Nucleotides in RNA Loop-Loop Interaction, p 113-133. In Grosjean H, Benne R (ed), Modification and Editing of RNA. ASM Press, Washington, DC. doi: 10.1128/9781555818296.ch7
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Image of Figure 9
Figure 9

Structural model for the loop-loop interaction formed by two complementary hairpin loops (in fact, an “inverted” loop) found in the antisense RNA-I transcript and its target site (mRNA-II) in the ColE1 plasmid. (A) Nucleotide sequences of the interacting hairpins. (B) Corresponding schematic model as proposed by . The phosphodiester backbone of the RNA-RNA complex is shown as a shaded ribbon (Α-form RNA helix). The seven base pairs of the loop and of the proximal stems are indicated by crossed rods. This complex has also a dyad axis of symmetry located perpendicular to the paper, through the bond joining the pairing central bases of the seven-member loop (here a C•G). Determinants of the instability of such RNA hairpin loop-loop complexes have been extensively studied by and . More detailed model building shows that the helix bends to accommodate the full complementarity of the seven base pairs within the loop ( ). Such bending is further stabilized by protein (see text). (C) Secondary structure of the anticodon domain of tRNA (isoacceptors 1 and 3). The chemical structure of the modified nucleotide (A*) at position 37 of tRNA is not known but could be a derivative of tA.

Citation: Grosjean H, Houssier C, Romby P, Marquet R. 1998. Modulatory Role of Modified Nucleotides in RNA Loop-Loop Interaction, p 113-133. In Grosjean H, Benne R (ed), Modification and Editing of RNA. ASM Press, Washington, DC. doi: 10.1128/9781555818296.ch7
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Image of Figure 8
Figure 8

Modulation of codon-anticodon binding. The anticodon hairpin in tRNAs is schematically represented. Ζ stands for any nucleotide in the anticodon loop or in the proximal anticodon stem, R stands for purine 37 located 3′-adjacent to the anticodon, and W stands for the anticodon wobble base 34. Asterisks show positions where the bases or the ribose are most frequently modified (see Fig. 1 ). (a and b) Modulation of the strength of binding occurs by the loop constraint. Here the nature of the bases (Z) in the proximal anticodon stem and loop plays a role in the flexibility and hence the preferential conformation adopted by the anticodon when it binds to a complementary codon (conformational switches). The 3′-stacked conformation is schematically represented in panel b because it is the predominant conformation in solution ( ; and ) and the only conformation in the crystal (discussed in ). However, major contributions of the “ribosomal milieu” as well as of divalent cations have also to be taken into account, (c) Modulation occurs by the immediate context of the codon-anticodon pairing. Here the purine (R) 3′-adjacent to the anticodon (and possibly the base 3′-adjacent to the codon) plays a role in the stabilization of the base pair between the third anticodon base and the first codon base ( ). Certain modified bases such as tA, msiA and Y base (designated by the symbol R*) are particularly important because of their stacking potential (this chapter), (d) Modulation occurs by the so-called wobble base (W). Here the strength of the binding depends on the possibility of forming a stable Watson-Crick type base pair rather than a less stable “mismatched” pair (modulation by third codon choice). It also depends on the stabilizing effect (stacking) of the wobble base (modified or not) on the strength of pairing in the middle position of the codon-anticodon complex.

Citation: Grosjean H, Houssier C, Romby P, Marquet R. 1998. Modulatory Role of Modified Nucleotides in RNA Loop-Loop Interaction, p 113-133. In Grosjean H, Benne R (ed), Modification and Editing of RNA. ASM Press, Washington, DC. doi: 10.1128/9781555818296.ch7
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References

/content/book/10.1128/9781555818296.chap7
1. Amano, M.,, and Y. Kyogoku. 1993. Nuclear magnetic resonance study of the codon-anticodon interaction in Bombix mori tRNAGly (GCC). Eur. J. Biochem. 217:131136.
2. Auffinger, P.,, and E. Westhof. 1997. RNA hydration: three non-aseconds of multiple molecular dynamics simulations of the solvated tRNAAspanticodon hairpin. J. Mol. Biol. 269:326341.
3. Becker, H. F.,, Y. Motorin,, M. Sissler,, C. Florentz,, and H. Grosjean. 1997. Major identity determinants for enzymatic formation of ribothymidine and pseudouridine in the TΨ-loop of yeast tRNAs.J. Mol. Biol. 274:505518.
4. Berkhout, B.,, and J. L. B. van Wamel. 1996. Role of the DIS hairpin in replication of human immunodeficiency virus type 1. J. Virol. 70:67236732.
5. Bernasconi, C. F. 1976. Relaxation Kinetics. Academic Press, New York, N.Y..
6. Björk, G. R., 1995a. Biosynthesis and function of modified nucleosides, p. 165Æ206. In D. Soil, and U. RajBhandary (ed.), tRNA: Structure, Biosynthesis, and Function. ASM Press, Washington, D.C..
7. Björk, G. R. 1995b. Genetic dissection of synthesis and function of modified nucleosides in bacterial tRNA. Prog. Nucleic Acid Res. Mol. Biol. 50:263338.
8. Björk, G. R.,, P. Wikstrom,, and A. S. Bystrom. 1989. Prevention of translational frameshifting by the modified nucleoside 1-methylguanosine. Science 244:986989.
9. Borer, P. N.,, B. Dengler, Jr.,, I. Tinoco,, and O. C. Uhlenbeck. 1974. Stability of ribonucleic acid double-stranded helices. J. Mol. Biol. 86:843853.
10. Brion, P.,, and E. Westhof. 1997. Hierarchy and dynamics of RNA folding. Annu. Rev. Biophys. Biomol. Struct. 26:113137.
11. Bubienko, E.,, P. Cruz,, J. F. Thomason,, and P. N. Borer. 1983. Nearest neighbour effects in the structure and function of nucleic acids. Prog. Nucleic Acid Res. Mol. Biol. 30:4190.
12. Buckingham, R. H. 1976. Anticodon conformation and accessibility in wild-type and suppressor tryptophan tRNA from E. coli. Nucl. Acids Res. 3:965975.
13. Buckingham, R. H.,, and H. Grosjean,. 1986. The accuracy of mRNA-tRNA recognition, p. 83126. In T. B. L. Kirkwood,, R. F. Rosenberger,, and D. J. Galas (ed.), Accuracy in Molecular Processes: Its Control and Relevance to Living Systems. Chapman and Hall, London, United Kingdom.
14. Bujalowski, W.,, M. Jung,, L. W. McLaughlin,, and D. Porschke. 1986a. Codon-induced association of the isolated anticodon loop of tRNAphe. Biochemistry 25:63726378.
15. Bujalowski, W.,, E. Graeser,, L. W. McLaughlin,, and D. Porschke. 1986b. Anticodon loop of tRNAPhe: structure, dynamics and Mg2+ binding. Biochemistry 25:63656371.
16. Carter, R. J.,, K. J. Baeyens,, J. SantaLucia,, D. H. Turner,, and S. R. Holbrook. 1997. The crystal structure of an RNA oligomer incorporating tandem adenosine-inosine mismatches. Nucleic Acids Res. 25:41174122.
17. Cedergren, R. J.,, D. Sankoff,, B. LaRue,, and H. Grosjean. 1981. The evolving tRNA molecule. Crit. Rev. Biochem. 11:35104.
18. Cedergren, R. J.,, H. Grosjean,, and B. LaRue. 1986. Primordial reading of genetic information. BioSystems 19:259266.
19. Chang, K.-Y.,, and I. Tinoco, Jr. 1994. Characterization of a "kissing" hairpin complex derived from the human immunodeficiency virus genome. Proc. Natl. Acad. Sci. USA 91:87058709.
20. Clore, G. M.,, A. M. Gronenborn,, and L. W. McLaughlin. 1984a. Structure of the ribonucleoside diphosphate codon UpUpC bound to tRNAphc from yeast: a time dependent transferred nuclear overhauser enhancement study.J. Mol. Biol. 174:163174.
21. Clore, G. M.,, A. M. Gronenborn,, E. A. Piper,, L. W. McLaughlin,, E. Graeser,, and J. H. Van Boom. 1984b. The solution structure of a RNA pentadecamer comprising the anticodon loop and stem of yeast tRNAPhe. Biochem. J. 221:737751.
22. Condon, C.,, H. Putzer,, and M. Grunberg-Manago. 1996. Processing of the leader mRNA plays a major role in the induction of thrS expression following threonine starvation in B. subtilis. Proc. Natl. Acad. Sci. USA 93:69926997.
23. Condon, C.,, H. Putzer,, D. Luo,, and M. Grunberg-Manago. 1997. Processing of the Bacillus subtilis thrS leader mRNA is RNase-dependent in E. coli. J. Mol. Biol. 268:235242.
24. Craig, M. E.,, D. M. Crothers,, and P. Doty. 1971. Relaxation kinetics of dimer formation by self complementary oligonucleotides. J. Mol. Biol. 62:383401.
25. Crick, F. H. C. 1966. Codon-anticodon pairing: the wobble hypothesis.J. Mol. Biol. 19:548555.
26. Crothers, D. M., 1971. Temperature-jump methods, p. 369388. In G. L. Cantoni, and D. R. Davies (ed.), Procedures in Nucleic Acid Research, vol. 2. Harper and Row, New York, N.Y..
27. Curran, J. F. 1995. Decoding with the A:I wobble pair is inefficient. Nucleic Acids Res. 23:683688.
28. Davanloo, P.,, M. Sprinzl,, K. Watanabe,, M. Albani, and H. Kersten. 1979. Role of ribothymidine in the thermal stability of tRNA as monitored by proton magnetic resonance. Nucleic Acids Res. 6:15711581.
29. Davis, D. R. 1995 Stabilization of RNA stacking by pseudouridine. Nucleic Acids Res. 23:50205026.
30. Derrick, W. B.,, and J. Horowitz. 1993. Probing structural differences between native and in vitro transcribed E. coli valine transfer RNA: evidence for stable base modification dependent con-formers. Nucleic Acids Res. 21:49484953.
31. Dirheimer, G.,, G. Keith,, P. Dumas,, and E. Westhof,. 1995. Primary, secondary and tertiary structures of tRNAs, p. 93140. In D. Soil, and U. RajBhandary (ed.), tRNA: Structure, Biosynthesis, and Function. ASM Press, Washington, D.C..
32. Eguchi, Y.,, and J. Tomizawa. 1990. Complex formed by complementary RNA stem-loops and its stabilization by a protein: function of ColE1 Rom protein. Cell 60:199209.
33. Eguchi, Y.,, and J. Tomizawa. 1991. Complexes formed by complementary RNA stem-loops: their formations, structures, and interaction with ColE1 Rom protein.J. Mol. Biol. 220:831842.
34. Eguchi, Y.,, T. Itoh,, and J. Tomizawa. 1991. Antisense RNA. Annu. Rev. Biochem. 60:631652.
35. Eigen, M., 1954. Methods for investigation of ionic reactions in aqueous solutions with half-times as short as 10-9 sec: application to neutralization and hydrolysis reactions. Discuss. Faraday Soc. 17:194205.
36. Eigen, M.,, and L. DeMaeyer,. 1963. Relaxation methods, p. 8951054. In S. L. Friess,, E. S. Lewis,, and A. Weissberger (ed.), Technique of Organic Chemistry, vol. VIII, part 2. Wiley (Inter-science), New York, N.Y..
37. Eisinger, J. 1971a. Complex formation between transfer RNA's with complementary anticodons. Biochem. Biophys. Res. Commun. 43:854861.
38. Eisinger, J. 1971b. Visible gel electrophoresis and the determination of association constant. Biochem. Biophys. Res. Commun. 44:11351142.
39. Eisinger, J.,, B. Feuer,, and T. Yamane. 1971. Codon-anticodon binding in yeast tRNAPhe. Nature 231:126128.
40. Eisinger, J.,, and W. E. Blumberg. 1973. Binding constants from zone transport of interacting molecules. Biochemistry 12: 36483660.
41. Eisinger, J.,, and N. Gross. 1974. The anticodon-anticodon complex.J. Mol. Biol. 88:165174.
42. Eisinger, J.,, and N. Gross. 1975. Conformers, dimers and anticodons complexes of tRNAPhe of E. coli. Biochemistry 14: 40314041.
43. Garriti, D. B.,, and S. A. Zahler. 1994. Mutations in the gene for a tRNA that functions as a regulator of a transcriptional attenuator in B. subtilis. Genetics 137:627636.
44. Geerdes, H. A. M.,, J. H. Van Boom,, and C. W. Hilbers. 1980. Codon-anticodon interactions in tRNAPhc: II. A NMR study of the binding of the codon UUC. J. Mol. Biol. 142:219230.
45. Gregorian, R. S.,, and D. M. Crothers. 1995. Determinants of RNA hairpin loop-loop complex stability.J. Mol. Biol. 248:968984.
46. Grosjean, H.,, C. Takada,, and J. Petre. 1973. Complex formation between tRNAs with complementary anticodons: use of matrix bound tRNA. Biochem. Biophys. Res. Commun. 53:882893.
47. Grosjean, H.,, D. G. Soil,, and D. M. Crothers. 1976. Studies of the complex between tRNAs with complementary anticodons: I. Origins of enhanced affinity between complementary triplets. J. Mol. Biol. 103:499519.
48. Grosjean, H.,, S. de Henau,, and D. M. Crothers. 1978. On the physical basis for ambiguity in genetic coding interactions. Proc. Natl. Acad. Sci. USA 75:610614.
49. Grosjean, H.,, and H. Chantrenne,. 1980. On codon-anticodon interactions, p. 347367. In F. Chapeville, and A.-L. Haenni (ed.), Molecular Biology Biochemistry and Biophysics, vol. 32. Chemical Recognition in Biology. Springer-Verlag, Berlin, Germany.
50. Grosjean, H.,, and W. Fiers. 1982. Preferential codon usage in prokaryotic genes: the optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes. Gene 18:199209.
51. Grosjean, H.,, K. Nicoghosian,, E. Haumont,, D. Soil,, and R. J. Cedergren. 1985. Nucleotide sequences of two serine tRNAs with a GGA anticodon: the structure-function relationships in the serine family of E. coli tRNAs. Nucleic Acids Res. 13: 56975706.
52. Grosjean, H.,, and C. Houssier,. 1990. Codon recognition: evaluation of the effects of modified bases in the anticodon loop of tRNA using temperature-jump relaxation method, p. A255A295. In C. W. Gehrke, and K. C. Kuo (ed.), Chromatography and Modification of Nucleosides, part A. Analytical Methods for Major and Modified Nucleosides. J. Chrom. Library, vol. 45A. Elsevier Science Publishing, Amsterdam, The Netherlands.
53. Grosjean, H.,, M. Sprinzl,, and S. Steinberg. 1995. Posttranscriptionnally modified nucleotides in tRNA: their locations and frequencies. Biochimie 77:139141.
54. Grundy, F. J.,, and T. M. Henkin. 1993. tRNA as a positive regulator of transcription in B. subtilis. Cell 74:475482.
55. Grundy, F. J.,, and T. M. Henkin. 1994. Conservation of a transcription antitermination mechanism in aminoacyl-tRNA synthetase and amino acid biosynthesis genes in gram-positive bacteria. J. Mol. Biol. 235:798804.
56. Grundy, F. J.,, S. E. Hodil,, S. M. Rollins, and T. M. Henkin. 1997. Specificity of tRNA-mRNA interactions in Bacillus subtilis tyrS antitermination.J. Bacteriol. 179:25872594.
57. Haddrick, M.,, A. L. Lear,, A. J. Cann,, and S. Heaphy. 1996. Evidence that a kissing loop structure facilitates genomic RNA dimerisation in HIV-1.J. Mol. Biol. 259:5868.
58. Hagervall, T. G.,, T. M. F. Tuohy,, J. F. Atkins,, and G. R. Björk. 1993. Deficiency of 1-methylguanosine in tRNA from Salmonella typhimurium induces frameshifting by quadruplet translocation.J. Mol. Biol. 232:756765.
59. Hall, K. B.,, J. R. Sampson,, O. C. Uhlenbeck,, and A. G. Redfield. 1989. Structure of an unmodified tRNA molecule. Biochemistry 28:57945801.
60. Hammes, G. G. 1968. Relaxation spectrometry of biological systems. Adv. Prot. Chem. 23:157.
61. Hara-Yokoyama, M.,, S. Yokoyama,, T. Watanabe,, K. Watanabe,, K. Kitazume,, Y. Mitamura,, T. Morii,, S. Takahashi,, Y. Kuchino,, S. Nishimura,, and T. Miyazawa. 1986. Characteristic anticodon sequences of major tRNA species from an extreme thermophile, T. thermophilus HB8. FEBS Lett. 202:149152.
62. He, L.,, R. Kierzek,, J. SantaLucia,, A. E. Walter, and D. H. Turner. 1991. Nearest-neighbour parameters for G.U mismatches: GU/ UG is destabilizing in the contexts CGUG/GUGC, UGUA/ AUGU, and AGUU/UUGA but stabilizing in GGUC/CUGG. Biochemistry 30:1112411132.
63. Helm, M.,, H. Brule,, F. Degoul,, C. Cepanec,, J. P. Leroux,, R. Giege, and C. Florentz. 1997. The presence of a modified nucleotide is required for the cloverleaf folding of a human mitochondrial tRNA, abstr. 3-13. 17th International tRNA Workshop, May 10-15, Kazusa Akademia Center, Chiba, Japan.
64. Henkin, T. M. 1994. tRNA-directed transcription antitermination. Mol. Microbiol. 13:381387.
65. Horie, N.,, M. Hara-Yokoyama,, S. Yokoyama,, K. Watanabe,, Y. Kuchino,, S. Nishimura, and T. Miyazawa. 1985. Two tRNA1Ile from an extreme thermophile, Thermus thermophilus HB8: effect of 2-thiolation of ribothymidine on the thermostability of tRNA. Biochemistry 24:57115715.
66. Houssier, C.,, and H. Grosjean. 1985. Temperature jump relaxation studies on the interactions between tRNAs with complementary anticodons: the effect of modified bases adjacent to the anticodon triplet.J. Biomol. Struct. Dyn. 3:387408.
67. Houssier, C.,, P. Degee,, K. Nicoghosian,, and H. Grosjean. 1988. Effect of uridine dethiolation in the anticodon triplet of tRNA2Glu on its association with tRNAPhe J. Biomol. Struct. Dyn. 5:12591266.
68. Isel, C.,, C. Ehresmann,, G. Keith,, B. Ehresmann,, and R. Marquet. 1995. Initiation of reverse transcription of HIV-1: secondary structure of the HIV-1 RNA/tRNA3Lys (template/primer) complex.J. Mol. Biol. 247:236250.
69. Isel, C.,, J. M. Lanchy,, S. F. J. Le Grice,, C. Ehresmann,, B. Ehresmann,, and R. Marquet. 1996. Specific initiation and switch to elongation of human immunodeficiency virus type 1 reverse transcription require the post-transcriptional modifications of primer tRNA3Lys EMBO J. 15:917924.
70. Isel, C.,, R. Marquet,, G. Keith,, C. Ehresmann,, and B. Ehresmann. 1993. Modified nucleotides of transfer-RNA3Lys modulate primer/template loop-loop interaction in the initiation complex of HIV-1 reverse transcription. J. Biol. Chem. 268: 2526925272.
71. Kawai, G.,, Y. Yamamoto,, T. Kamimura,, T. Masegi,, M. Sekine,, T. Hata,, T. Iimori,, T. Watanabe,, T. Miyazawa,, and S. Yokoyama. 1992. Conformational rigidity of specific pyrimidine residues in tRNA arises from post-transcriptional modifications that enhance steric interaction between the base and the 2'-hydroxyl group. Biochemistry 31:10401046.
72. Kowalak, J. A.,, J. J. Dalluge,, J. A. McCloskey,, and K. O. Stetter. 1994. The role of post-transcriptional modification in stabilization of tRNA from hyperthermophiles. Biochemistry 33: 78697876.
73. Kim, J.,, A. E. Walter,, and D. H. Turner. 1996. Thermodynamics of coaxially stacked helixes with GA and CC mismatches. Biochemistry 35:1375313781.
74. Labuda, D.,, H. Grosjean,, G. Striker,, and D. Porschke. 1982. Codomanticodon and anticodomanticodon interaction. Evaluation of equilibrium and kinetic parameters of complexes involving a G:U wobble. Biochim. Biophys. Acta 698:230236.
75. Labuda, D.,, G. Striker,, and D. Porschke. 1984. Mechanism of codon recognition by tRNA and codon-induced tRNA association.J. Mol. Biol. 174:587604.
76. Labuda, D.,, G. Striker,, H. Grosjean,, and D. Porschke. 1985. Mechanism of codon recognition by tRNA studied with oligonucleotides larger than triplets. Nucleic Acids Res. 13:36673683.
77. Lagerkvist, U. 1978. "Two-out-of-three": an alternative method of codon reading. Proc. Natl. Acad. Sci. USA 75:17591762.
78. Laughrea, M.,, and L. Jette. 1994. A 19-nucleotide sequence upstream of the 5' major splice donor is part of the dimerization domain of human immunodeficiency virus 1 genomic RNA. Biochemistry 33:1346413474.
79. Laughrea, M.,, and L. Jette. 1996. Kissing-loop model of HIV-1 genome dimerization: HIV-1 RNA can assume alternative dimeric forms, and all sequences upstream or downstream of hairpin 248-271 are dispensable for dimer formation. Biochemistry 35:15891598.
80. Le, S. Y.,, and M. Zuker. 1991. Predicting common foldings of homologous RNA.J. Biomol. Struct. Dyn. 8:10271044.
81. Levin, H. L. 1997. It's prime time for reverse transcriptase. Cell 88:58.
82. Luo, D.,, J. Leautey,, M. Grunberg-Manago,, and H. Putzer. 1997. Structure and regulation of expression of the Bacillus subtilis valyl-tRNA synthetase gene.J. Bacteriol. 179:24722478.
83. Mandal, N.,, D. Mangroo,, J. J. Dalluge,, J. A. McCloskey, and U. L. RajBandary. 1996. Role of the three consecutive G:C base pairs conserved in the anticodon stem of initiator tRNAs in initiation of protein synthesis in E. coli. RNA 2:473482.
84. Marino, J. P.,, R. S. Gregorian,, G. Csankovvszki,, and D. M. Crothers. 1995. Bent helix formation between RNA hairpins with complementary loops. Science 268:14481454.
85. Marquet, R.,, C. Isel,, C. Ehresmann,, and B. Ehresmann. 1995. tRNAs as primer of reverse transcriptase. Biochimie 77: 113124.
86. Masukata, H.,, and J. Tomizawa. 1986. Control of primer formation for ColE1 plasmid replication: conformational change of the primer transcript. Cell 44:125136.
87. McBride, M. S.,, and A. T. Panganiban. 1996. The human immunodeficiency virus type 1 encapsidation site is a multipartite RNA element composed of functional hairpin structures.J. Virol. 70:29632973.
88. Meier, F.,, B. Suter,, H. Grosjean,, G. Keith,, and E. Kubli. 1985. Queuosine modification of the wobble base in tRNAHis influences in vivo decoding properties. EMBO J. 4:823827.
89. Michel, F.,, and E. Westhof. 1990. Modelling of the three-dimensional architecture of group I catalytic introns based on comparative sequence analysis.J. Mol. Biol. 216:585610.
90. Moras, D.,, M. B. Comarmond,, J. Fisher,, R. Weiss,, J. C. Thierry,, J. P. Ebel,, and R. Giege. 1980. Crystal structure of yeast tRNAAsp. Nature 288:669674.
91. Moras, D.,, A. C. Dock,, P. Dumas,, E. Westhof,, P. Romby,, J. P. Ebel,, and R. Giege. 1986. Anticodon-anticodon interaction induces conformational changes in yeast tRNAAsp, a model for tRNA-mRNA recognition. Proc. Natl. Acad. Sci. USA 83: 932936.
92. Motorin, Y.,, G. Bee,, R. Tewari,, and H. Grosjean. 1997. Transfer RNA recognition by E. coli isopentenyl-pyrophosphate:tRNA-isopentenyl transferase: dependence on the anticodon arm structure. RNA 3:721733.
93. Muriaux, D.,, P.-M. Girard,, B. Bonnet-Mathoniere,, and J. Paoletti. 1995. Dimerization of HIV-lLai RNA at low ionic strength. An autocomplementary sequence in the 5' leader region is evidenced by an antisense oligonucleotide. J. Biol. Chem. 270: 82098216.
94. Muriaux, D.,, P. Fosse,, and J. Paoletti. 1996a. A kissing complex together with a stable dimer is involved in the HIV-1Lai RNA dimerization process in vitro. Biochemistry 35:50755082.
95. Muriaux, D.,, H. DeRocquigny,, B. P. Roques,, and J. Paoletti. 1996b. NCp7 activates HIV-l(Lai) RNA dimerization by converting a transient loop-loop complex into a stable dimer.J. Biol. Chem. 271:3368633692.
96. Nakamura, Y.,, K.-N. Wada,, Y. Wada,, H. Doi,, S. Kanaya,, T. Gojobori,, and T. Ikemura. 1996. Codon usage tabulated from the international DNA sequence databases. Nucleic Acids Res. 24: 214215.
97. Nelson, J. W.,, and I. Tinoco, Jr. 1982. Comparison of the kinetics of ribooligonucleotide, deoxyribonucleotide and hybrid oligonucleotide double-strand formation by T-jump kinetics. Biochemistry 21:52895295.
98. Nilson, L.,, R. Rigler,, and P. Laggner. 1982. Structural variability of small-angle x-ray scattering of the yeast tRNApw-E. coli tRNAGlu2 complex. Proc. Natl. Acad. Sci. USA 79:58915895.
99. Paillart, J. C.,, R. Marquet,, E. Skripkin,, B. Ehresmann,, and C. Ehresmann. 1994. Mutational analysis of the bipartite dimer linkage structure of HIV-1 genomic RNA. J. Biol. Chem. 269: 2748627493.
100. Paillart, J. C.,, R. Marquet,, E. Skripkin,, C. Ehresmann,, and B. Ehresmann. 1996a. Dimerization of retroviral genomic RNAs: structural and functional implications. Biochimie 78:639653.
101. Paillart, J.-C.,, L. Berthoux,, M. Ottmann,, J.-L. Darlix,, R. Marquet,, B. Ehresmann,, and C. Ehresmann. 1996b. A dual role of the putative RNA dimerization initiation site of human immunodeficiency virus type 1 in genomic RNA packaging and proviral DNA synthesis. J. Virol. 70:83488354.
102. Paillart, J.-C,, E. Skripkin,, B. Ehresmann,, C. Ehresmann,, and R. Marquet. 1996c. A loop-loop "kissing" complex is the essential part of the dimer linkage of genomic HIV-1 RNA. Proc. Natl. Acad. Sci. USA 93:55725577.
103. Paillart, J. C.,, E. Westhof,, C. Ehresmann,, B. Ehresmann,, and R. Marquet. 1997. Non-canonical interactions in a kissing loop complex: the dimerization initiation site of HIV-1 genomic RNA.J. Mol. Biol. 270:3649.
104. Perret, V.,, A. Garcia,, J. Puglisi,, H. Grosjean,, J. P. Ebel,, C. Florentz,, and R. Giege. 1990. Conformation in solution of yeast tRNAAsp transcripts deprived of modified nucleotides. Biochimie 72:735743.
105. Pleij, C. W. A. 1994. RNA pseudoknots. Curr. Opin. Struct. Biol. 4:337344.
106. Pörschke, D.,, O. C. Uhlenbeck,, and F. H. Martin. 1973. Thermodynamics and kinetics of the helix-coil transition of oligomers containing GC base pairs. Biopolymers 12:13131335.
107. Putzer, H.,, N. Gendron,, and M. Grunberg-Manago. 1992. Co-ordinate expression of the two threonyl-tRNA synthetase genes in Bacillus subtilis: control by transcriptional antitermination involving a conserved regulatory sequence. EMBO J. 11: 31173127.
108. Putzer, H.,, S. Laalami,, A. A. Brakhage,, C. Condon,, and M. Grunberg-Manago. 1995a. Aminoacyl-tRNA synthetase gene regulation in Bacillus subtilis: induction, repression and growth-rate regulation. Mol. Microbiol. 16:709718.
109. Putzer, H.,, M. Grunberg-Manago,, and M. Springer,. 1995b. Bacterial aminoacyl-tRNA synthetases: genes and regulation of expression, p. 293333. In D. Soil, and U. RajBhandary (ed.), tRNA: Structure, Biosynthesis, and Function. ASM Press, Washington, D.C..
110. Pyle, A. M.,, and J. B. Green. 1995. RNA folding. Curr. Opin. Struct. Biol. 5:303310.
111. Qian, Q.,, and G. R. Björk. 1997. Structural alterations far from the anticodon of the tRNAPro(GGG) of Salmonella typhimurium induce +1 frameshifting at the peptidyl-site.J. Mol. Biol. 273: 978992.
112. Ravetch, J.,, J. Gralla,, and D. M. Crothers. 1974. Thermodynamic and kinetic properties of short RNA helices: the oligomers sequences AnGCUn. Nucleic Acids Res. 1:109127.
113. Riesner, D.,, and R. Romer,. 1973. Thermodynamics and kinetics of conformational transitions in oligonucleotides and tRNA, p. 237318. In J. Duchesne (ed.) Physico-chemical Properties of Nucleic Acids, vol. 2. Academic Press, New York, N.Y..
114. Rigler, R.,, C. R. Rabl,, and T. M. Jovin. 1974. A T-jump apparatus for fluorescence measurements. Rev. Sci. Instrum. 45:580588.
115. Romby, P.,, P. Carbon,, E. Westhof,, C. Ehresmann,, J.-P. Ebel,, B. Ehresmann,, and R. Giege. 1987. Importance of conserved residues for the conformation of the T-loop in tRNAs.;. Biomol. Struct. Dyn. 5:669687.
116. Romby, P.,, R. Giege,, C. Houssier,, and H. Grosjean. 1985. Anticodon-anticodon interactions in solution: studies of the self-association of yeast or E. coli tRNAAsp and of their interactions with E. coli tRNAVal. J. Mol. Biol. 184:107118.
117. Romby, P.,, E. Westhof,, D. Moras,, R. Giege,, C. Houssier,, and H. Grosjean. 1986. Studies on anticodon-anticodon interactions. Hemi-protonation of cytosines induces self-pairing through the GCC anticodon of E. coli tRNAUy. J. Biomol. Struct. Dyn. 4: 193203.
118. Sampson, J. R.,, and O. C. Uhlenbeck. 1988. Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro. Proc. Natl. Acad. Sci. USA 85: 10331037.
119. Schweisguth, D. C.,, and P. B. Moore. 1997. On the conformation of the anticodon loops of initiator and elongator methionine tRNAs.J. Mol. Biol. 267:505519.
120. Simons, R. W. 1988. Naturally occurring antisense RNA control- a brief review. Gene 72:3544.
121. Skripkin, E.,, J. C. Paillart,, R. Marquet,, B. Ehresmann,, and C. Ehresmann. 1994. Identification of the primary site of human immunodeficiency virus type 1 RNA dimerization in vitro. Proc. Natl. Acad. Sci. USA 91:49454949.
122. Sprinzl, M.,, C. Horn,, M. Brown,, A. Ioudovitch,, and S. Steinberg. 1998. Compilation of tRNA sequences and sequences of tRNA genes. Nucleic Acids Res. 26:148153.
123. Steinberg, S.,, and R. Cedergren. 1995. A correlation between N2-dimethylguanosine presence and alternate tRNA conformers. RNA 1:886891.
124. Strieker, G.,, D. Labuda, and M. D. C. Vega-Carmen. 1989. The three conformations of the anticodon loop of yeast tRNAPhe J. Biomol. Struct. Dyn. 7:235255.
125. ten Dam, E.,, K. Pleij,, and D. Draper. 1992. Structural and functional aspects of RNA pseudoknots. Biochemistry 31: 1166511676.
126. Thusius, D.,, G. Foucault,, and F. Guillain,. 1973. The analysis of chemical relaxation amplitudes and some applications to reactions involving macromolecules, p. 271284. In C. Sadron (ed.), Dynamics Aspects of Conformation Changes in Biological Macromolecules. D. Reidel Publishing Company, Dordrecht, The Netherlands.
127. Tomizawa, J. 1984. Control of ColE1 plasmid replication: the process of binding of RNA I to the primer transcript. Cell 38: 861870.
128. Tomizawa, J. 1990a. Control of ColE1 plasmid replication: intermediates in the binding of RNA I and RNA II.J. Mol. Biol. 212: 683694.
129. Tomizawa, J. 1990b. Control of ColE1 plasmid replication: interaction of Rom protein with an unstable complex formed by RNA I and RNA II.J. Mol. Biol. 212:695708.
130. Tomizawa, J., 1993. Evolution of functional structures of RNA, p. 419445. In R. F. Gesteland, and J. F. Atkins (ed.), The RNA World. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y..
131. Turner, D. H.,, and P. C. Bevilacqua,. 1993. Thermodynamic considerations for evolution by RNA, p. 447464. In R. F. Gesteland, and J. F. Atkins (ed.), The RNA World. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y..
132. Uhlenbeck, O. C. 1972. Complementary oligonucleotide binding to tRNA.J. Mol. Biol. 65:2541.
133. Vacher, J.,, H. Grosjean,, C. Houssier,, and R. H. Buckingham. 1984. The effect of point mutations affecting E. coli tryptophan-tRNA on anticodon-anticodon interactions and on UGA suppression.J. Mol. Biol. 177:329342.
134. Varani, G. 1995. Exceptionally stable nucleic acid hairpins. Annu. Rev. Biophys. Biomol. Struct. 24:379404.
135. Vogeli, G.,, H. Grosjean,, and D. Soil. 1975. A method for the isolation of specific tRNA precursor. Proc. Natl. Acad. Sci. USA 72:47904794.
136. Wagner, E. G. H.,, and R. W. Simons. 1994. Antisense RNA control in bacteria, phages, and plasmids. Annu. Rev. Microbiol. 48: 713742.
137. Walter, A. E.,, and D. H. Turner. 1994. Sequence dependence of stability for coaxial stacking of RNA helixes with Watson-Crick base paired interfaces. Biochemistry 33:1271512719.
138. Walter, A. E.,, D. H. Turner,, J. Kim,, M. H. Lyttle,, P. Müller,, D. H. Mathews,, and M. Zucker. 1994. Coaxial stacking of helixes enhances binding of oligoribonucleotides and improves predictions of RNA folding. Proc. Natl. Acad. Sci. USA 91: 92189222.
139. Wang, A. C.,, and N. R. Kallenbach. 1971. Helical complexes of polyriboinosinic acid with copolymers of polyribocytidylic acid containing inosine, adenosine and uridine residues. J. Mol. Biol. 62:591611.
140. Wang, S.,, and E. T. Kool. 1995. Origins of the large difference in stability of DNA and RNA helices: C5-methyl and 2'-hydroxyl effects. Biochemistry 34:41254132.
141. Watanabe, K.,, M. Shinma,, and T. Oshima. 1976. Heat-induced stability of tRNA from an extreme thermophile, Thermus thermophilus. Biochem. Biophys. Res. Commun. 72:11371144.
142. Weiss, G. B. 1973. Translational control of protein synthesis by tRNA unrelated to changes in tRNA concentration.J. Mol. Evol. 2:199204.
143. Weissenbach, J.,, and H. Grosjean. 1981. Effect of threonylcarbamoyl modification (t6A) in yeast tRNAArg on codon-anticodon and anticodon-anticodon interactions: a thermodynamic and kinetic evaluation. Eur. J. Biochem. 116:207213.
144. Westhof, E.,, P. Dumas,, and D. Moras. 1983. Loop stereochemistry and dynamics in tRNA.J. Biomol. Struct. Dyn. 1:337355.
145. Westhof, E.,, P. Dumas,, and D. Moras. 1985. Crystallographic refinement of yeast aspartic acid tRNA.J. Mol. Biol. 184:119145.
146. Westhof, E.,, B. Masquida,, and L. Jaeger. 1996. RNA tectonics: towards RNA design. Fold Des. 1:R78R88.
147. Westhof, E.,, and L. Jaeger. 1992. RNA pseudoknots. Curr. Opin. Struct. Biol. 2:327333.
148. Wyatt, J. R.,, and I. Tinoco, Jr., 1993. RNA structural elements and RNA function, p. 465496. In R. F. Gesteland, and J. F. Atkins (ed.), The RNA World. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y..
149. Yao, L. J.,, T. L. James,, J. T. Kealey,, D. V. Santi,, and U. Schmitz. 1997. The dynamic NMR structure of the TYC-loop: implications for the specificity of tRNA methylation. J. Biomol. NMR 9:229244.
150. Yarus, M. 1982. Translational efficiency of tRNA's: uses of an extended anticodon. Science 218:646652.
151. Yarus, M.,, and D. Smith,. 1995. tRNA on the ribosome: a waggle theory, p. 443469. In D. Soil, and U. RajBhandary (ed.), tRNA: Structure, Biosynthesis, and Function. ASM Press, Washington, D.C..
152. Yaskunas, S. R.,, C. R. Cantor,, and I. Tinoco, Jr. 1968. Association of complementary oligonucleotides in aqueous solution. Biochemistry 7:31643178.
153. Yokoyama, S.,, T. Watanabe,, K. Murao,, H. Ishikura,, Z. Yamaizumi,, S. Nishimura,, and T. Miyazawa. 1985. Molecular mechanism of codon recognition by tRNA species with modified uridine in the first position of the anticodon. Proc. Natl. Acad. Sci. USA 82:49054909.
154. Yokoyama, S.,, Z. Yamaizumi,, S. Nishimura,, and T. Miyazawa. 1979. 1H-NMR studies on the conformational characteristics of 2-thiopyrimidine nucleotides found in tRNA. Nucleic Acids Res. 6:26112626.
155. Yokoyama, S.,, and S. Nishimura,. 1995. Modified nucleosides and codon recognition, p. 207223. In D. Soil, and U. RajBhandary (ed.), tRNA: Structure, Biosynthesis, and Function. ASM Press, Washington, D.C..

Tables

Generic image for table
Table 1

Thermodynamic and kinetic parameters of selected tRNA anticodon-anticodon complexes, as determined by the temperature-jump relaxation technique

Citation: Grosjean H, Houssier C, Romby P, Marquet R. 1998. Modulatory Role of Modified Nucleotides in RNA Loop-Loop Interaction, p 113-133. In Grosjean H, Benne R (ed), Modification and Editing of RNA. ASM Press, Washington, DC. doi: 10.1128/9781555818296.ch7

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