Recognition of Aminoacyl-tRNAs by Protein Elongation Factors

Brian F. C. Clark; Morten Kjeldgaard; Jan Barciszewski; Mathias Sprinzl

doi:10.1128/9781555818333.ch21

Chapter 21 : Recognition of Aminoacyl-tRNAs by Protein Elongation Factors

Authors: Brian F. C. Clark¹, Morten Kjeldgaard¹, Jan Barciszewski², Mathias Sprinzl³

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Affiliations: 1: Institute of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C, Denmark; 2: Institute of Bioorganic Chemistry of the Polish Academy of Sciences, Noskowskiego 12, 61704 Poznan, Poland; 3: Laboratorium für Biochemie, Universität Bayreuth, Postfach 101251, 8580 Bayreuth, Germany

Content Type: Monograph

Publication Year: 1995

Category: Microbial Genetics and Molecular Biology

Book DOI: 10.1128/9781555818333

Chapter DOI: 10.1128/9781555818333.ch21

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Abstract:

The interactive recognition of nucleic acids by proteins is a central process in the regulation of gene expression. To gain insight into such interactions requires a knowledge of appropriate three-dimensional structures and information on biochemical function. Only a few native biological supramacromolecular protein-nucleic acid complexes are currently accessible for such detailed investigations. One convenient object for such study is the ternary complex composed of aminoacyl-tRNA (aa-tRNA) and elongation factor (EF-Tu) bound to GTR. This chapter brings up to date two earlier reviews addressing the problem of aa-tRNA and EF-Tu:GTP interaction. It summarizes the most recent published studies that contribute to an understanding of the recognitory interactions between tRNA and the protein elongation factor, and the chapter puts these studies in perspective. Finally, it proposes a new model for the three-dimensional structure of the ternary complex (TC). This model accommodates all existing structural experimental data obtained during the studies of the TC.

Citation: Clark B, Kjeldgaard M, Barciszewski J, Sprinzl M. 1995. Recognition of Aminoacyl-tRNAs by Protein Elongation Factors, p 423-442. In tRNA. ASM Press, Washington, DC. doi: 10.1128/9781555818333.ch21

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Recognition of Aminoacyl-tRNAs by Protein Elongation Factors

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/content/10.1128/9781555818333.chap21.fig21-1

Figure 1.

Hydrogen bonding interactions between GDP and E. coli EF-Tu.

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10.1128/9781555818333/fig21-1.gif

Figure 1.

Hydrogen bonding interactions between GDP and E. coli EF-Tu.

/content/10.1128/9781555818333.chap21.fig21-2

Figure 2.

Secondary structure model of tRNA ( 94 ) with marked nucleotides whose reactivity is reduced in the presence of elongation factor Tu ( 24 , 110 ) or cross-linked to the EF-Tu ( 67 , 109 ). Large filled arrows mean protected nucleotides, large empty arrows mean exposed nucleotides, and small filled arrows mean neutral cuts.

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10.1128/9781555818333/fig21-2.gif

Figure 2.

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Figure 3.

Cartoon model of conformational changes of elongation factor from GDP to GTP form. Domain 2 moves 35-40 Å to form a cleft with domain 1, which contains the amino acid binding site of aa-tRNA. The effector region comprises the amino acid residues 40–60 in the case of EF-Tu of T. thermophilus.

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Figure 3.

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Figure 4a.

Panels A and B show two views of a tertiary structural model of the ternary complex of EF-Tu:GTP-aa-tRNA. The stretched CCA end is assumed to be bent back to the EF-Tu with the amino acid attached (not shown) (compare with reference 47 ).

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Figure 4a.

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Figure 4b.

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10.1128/9781555818333/fig21-4b.gif

Figure 4b.

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