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Chapter 7 : The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles

Authors: Helena Santos1, Pedro Lamosa2, Tiago Q. Faria3, Nuno Borges4, ClÉlia Neves5
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Affiliations: 1: Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, Apartado 127, 2780-156 Oeiras, Portugal; 2: Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, Apartado 127, 2780-156 Oeiras, Portugal; 3: Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, Apartado 127, 2780-156 Oeiras, Portugal; 4: Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, Apartado 127, 2780-156 Oeiras, Portugal; 5: Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, Apartado 127, 2780-156 Oeiras, Portugal
Content Type: Monograph
Publication Year: 2007

Category: Applied and Industrial Microbiology; Environmental Microbiology

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Abstract:

Many thermophiles and hyperthermophiles (from now on designated (hyper)thermophiles) have been isolated from both fresh water and seawater sources. Compatible solutes must be highly soluble and they usually belong to one of the following groups of compounds: amino acids, sugars, polyols, betaines, and ectoines. In general, compatible solutes accumulate to high levels in the cytoplasm. The relative abundance combined with the low molecular mass of these compounds greatly facilitates the task of their molecular identification by resorting to two powerful analytical techniques: nuclear magnetic resonance (NMR) and mass spectrometry. The mannosyl-3-phosphoglycerate synthase (MPGS) characterized to date produce mannosyl-3-phosphoglycerate with the same anomeric configuration of the substrate and accordingly have been classified as members of glycosyltransferases family GT55, which comprises GDP-mannose: α-mannosyltransferases that retain the anomeric configuration of the substrate. The evolution of MG biosynthesis is a fascinating topic but a meaningful discussion would demand more ample data sets and reliable tools for genome analysis. Diglycerol phosphate (DGP) biosynthesis was investigated by the author and his team on . In the case of solutes from hyperthermophiles, it was shown that the protecting effect was clearly dependent on the solute charge. The melting temperature of bovine ribonuclease A (RNase A) in the presence and absence of 2-a-O-mannosylglycerate (MG) depends on the ionization state of the solute. Due to the enhanced ability to stabilize biological materials, the application of hypersolutes in industrial applications was soon envisioned, and several industrial patents on their uses have been filed.

Citation: Santos H, Lamosa P, Faria T, Borges N, Neves C. 2007. The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles, p 86-103. In Gerday C, Glansdorff N (ed), Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC. doi: 10.1128/9781555815813.ch7

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The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles
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Citation: Santos H, Lamosa P, Faria T, Borges N, Neves C. 2007. The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles, p 86-103. In Gerday C, Glansdorff N (ed), Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC. doi: 10.1128/9781555815813.ch7
/content/10.1128/9781555815813.ch07.ch07fig01
Figure 1.
Compatible solutes primarily restricted to hyperthermophiles.
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Image of Figure 1.
Figure 1.

Compatible solutes primarily restricted to hyperthermophiles.

Citation: Santos H, Lamosa P, Faria T, Borges N, Neves C. 2007. The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles, p 86-103. In Gerday C, Glansdorff N (ed), Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC. doi: 10.1128/9781555815813.ch7
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Figure 2.
Distribution of trehalose (circles), mannosylglycerate (diamonds) and di--inositol-1,1′-phosphate (stars) among (hyper)thermophiles. Tree of Life adapted from . The question marks indicate unknown positions of the branching points between the three domains.
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Image of Figure 2.
Figure 2.

Distribution of trehalose (circles), mannosylglycerate (diamonds) and di--inositol-1,1′-phosphate (stars) among (hyper)thermophiles. Tree of Life adapted from . The question marks indicate unknown positions of the branching points between the three domains.

Citation: Santos H, Lamosa P, Faria T, Borges N, Neves C. 2007. The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles, p 86-103. In Gerday C, Glansdorff N (ed), Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC. doi: 10.1128/9781555815813.ch7
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Figure 3.
The two pathways for the synthesis of mannosylglycerate in . Single-step pathway uses mannosylglycerate synthase (MGS), while the two-step pathway involves the actions of mannosyl-3-phosphoglycerate synthase (MPGS) and mannosyl-3-phosphoglycerate phosphatase (MPGP).
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Image of Figure 3.
Figure 3.

The two pathways for the synthesis of mannosylglycerate in . Single-step pathway uses mannosylglycerate synthase (MGS), while the two-step pathway involves the actions of mannosyl-3-phosphoglycerate synthase (MPGS) and mannosyl-3-phosphoglycerate phosphatase (MPGP).

Citation: Santos H, Lamosa P, Faria T, Borges N, Neves C. 2007. The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles, p 86-103. In Gerday C, Glansdorff N (ed), Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC. doi: 10.1128/9781555815813.ch7
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Figure 4.
Unrooted phylogenetic tree based on known or putative sequences of mannosyl-3-phosphoglycerate synthase genes. The ClustalX and TreeView programs 5,7 were used for sequence alignment and to generate the phylogenetic tree. The significance of the branching order was evaluated by bootstrap analysis of 1000 computer-generated trees. Bar, 0.1 change per site. Abbreviations: Aper, ; Apro, ; Aven, ; Deth, ; Mgri, ; Ncra, ; Pfer, ; Paby, ; Pfur, ; Phor, ; Rmar, ; Tthe, ; Tlit, .
10.1128/9781555815813/f0094-01_thmb.gif
10.1128/9781555815813/f0094-01.gif
Image of Figure 4.
Figure 4.

Unrooted phylogenetic tree based on known or putative sequences of mannosyl-3-phosphoglycerate synthase genes. The ClustalX and TreeView programs 5,7 were used for sequence alignment and to generate the phylogenetic tree. The significance of the branching order was evaluated by bootstrap analysis of 1000 computer-generated trees. Bar, 0.1 change per site. Abbreviations: Aper, ; Apro, ; Aven, ; Deth, ; Mgri, ; Ncra, ; Pfer, ; Paby, ; Pfur, ; Phor, ; Rmar, ; Tthe, ; Tlit, .

Citation: Santos H, Lamosa P, Faria T, Borges N, Neves C. 2007. The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles, p 86-103. In Gerday C, Glansdorff N (ed), Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC. doi: 10.1128/9781555815813.ch7
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Figure 5.
Genomic organization of mannosylglycerate biosynthesis via the two-step pathway. Black arrows indicate genes; dark grey arrows indicate the genes; light grey arrow represents the phosphomannose isomerase/mannose-1-phosphate guanylyltransferase; the white arrow indicates phosphomannomutase.
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Image of Figure 5.
Figure 5.

Genomic organization of mannosylglycerate biosynthesis via the two-step pathway. Black arrows indicate genes; dark grey arrows indicate the genes; light grey arrow represents the phosphomannose isomerase/mannose-1-phosphate guanylyltransferase; the white arrow indicates phosphomannomutase.

Citation: Santos H, Lamosa P, Faria T, Borges N, Neves C. 2007. The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles, p 86-103. In Gerday C, Glansdorff N (ed), Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC. doi: 10.1128/9781555815813.ch7
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Figure 6.
Dependence of the melting temperature of RNase A on pH in the absence of solutes (squares and thin line) and with 0.5 M mannosylglycerate (circles and thick line).
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Image of Figure 6.
Figure 6.

Dependence of the melting temperature of RNase A on pH in the absence of solutes (squares and thin line) and with 0.5 M mannosylglycerate (circles and thick line).

Citation: Santos H, Lamosa P, Faria T, Borges N, Neves C. 2007. The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles, p 86-103. In Gerday C, Glansdorff N (ed), Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC. doi: 10.1128/9781555815813.ch7
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Figure 7.
Effect of solutes on the melting temperature of staphylococcal nuclease (SNase) and pig heart malate dehydrogenase (MDH). Abbreviations: Tre, trehalose; MG, α-mannosylglycerate; MGA, α-mannosylglyceramide; DIP, di- -inositol-1,1′-phosphate; DGP, diglycerol phosphate; KCl, potassium chloride; Gly, glycerol; Ect, ectoine; Hect, hydroxyectoine.
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10.1128/9781555815813/f0098-01.gif
Image of Figure 7.
Figure 7.

Effect of solutes on the melting temperature of staphylococcal nuclease (SNase) and pig heart malate dehydrogenase (MDH). Abbreviations: Tre, trehalose; MG, α-mannosylglycerate; MGA, α-mannosylglyceramide; DIP, di- -inositol-1,1′-phosphate; DGP, diglycerol phosphate; KCl, potassium chloride; Gly, glycerol; Ect, ectoine; Hect, hydroxyectoine.

Citation: Santos H, Lamosa P, Faria T, Borges N, Neves C. 2007. The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles, p 86-103. In Gerday C, Glansdorff N (ed), Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC. doi: 10.1128/9781555815813.ch7
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Figure 8.
Schematic representation of the preferential exclusion of solutes from the protein surface in the native and unfolded states. Upon denaturation, the zone of exclusion increases and, although the same amount of solute molecules is depicted, these become locally more concentrated, i.e., their chemical potential has increased. As a consequence, to achieve thermodynamic equilibrium, the unfolding reaction is displaced to the native state, hence the solute acts as a stabilizer.
10.1128/9781555815813/f0099-01_thmb.gif
10.1128/9781555815813/f0099-01.gif
Image of Figure 8.
Figure 8.

Schematic representation of the preferential exclusion of solutes from the protein surface in the native and unfolded states. Upon denaturation, the zone of exclusion increases and, although the same amount of solute molecules is depicted, these become locally more concentrated, i.e., their chemical potential has increased. As a consequence, to achieve thermodynamic equilibrium, the unfolding reaction is displaced to the native state, hence the solute acts as a stabilizer.

Citation: Santos H, Lamosa P, Faria T, Borges N, Neves C. 2007. The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles, p 86-103. In Gerday C, Glansdorff N (ed), Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC. doi: 10.1128/9781555815813.ch7
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Figure 9.
Fluorescence decay times of staphylococcal nuclease as a function of temperature in the presence of 0.5 M mannosylglycerate (solid symbols) and in the absence of solutes (open symbols). Native protein: triangles; denatured states of the protein: squares and circles.
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10.1128/9781555815813/f0100-01.gif
Image of Figure 9.
Figure 9.

Fluorescence decay times of staphylococcal nuclease as a function of temperature in the presence of 0.5 M mannosylglycerate (solid symbols) and in the absence of solutes (open symbols). Native protein: triangles; denatured states of the protein: squares and circles.

Citation: Santos H, Lamosa P, Faria T, Borges N, Neves C. 2007. The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles, p 86-103. In Gerday C, Glansdorff N (ed), Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC. doi: 10.1128/9781555815813.ch7
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References

/content/book/10.1128/9781555815813.ch07
1. Adams, M. 1993. Enzymes and proteins from organisms that grow near and above 100°C. Annu. Rev. Microbiol. 47: 627– 658
2. Alarico, S.,, N. Empadinhas,, C. Simões,, Z. Silva,, A. Henne,, A. Mingote,, H. Santos, and, M. S. da Costa. 2005. Distribution of genes for synthesis of trehalose and mannosylglycerate in Thermus spp. and direct correlation of these genes with halotolerance. Appl. Environ. Microbiol. 71: 2460– 2466
3. Arakawa, T.,, and S. N. Timasheff. 1982a. Stabilization of protein structure by sugars. Biochemistry. 21: 6536– 6544
4. Arakawa, T.,, and S. N. Timasheff. 1982b. Preferential interactions of proteins with salts in concentrated solutions. Biochemistry. 21: 6545– 6552
5. Arakawa, T.,, and S. N. Timasheff. 1983. Preferential interactions of proteins with solvent components in aqueous amino acid solutions. Arch. Biochem. Biophys. 224: 169– 177
6. Arakawa, T.,, and S. N. Timasheff. 1985a. Mechanism of poly(ethylene glycol) interaction with proteins. Biochemistry. 24: 6756– 6762
7. Arakawa, T.,, and S. N. Timasheff. 1985b. The stabilization of proteins by osmolytes. Biophys. J. 47: 411– 414
8. Baldwin, R. L. 1996. How Hofmeister ion interactions affect protein stability. Biophys. J. 71: 2056– 2063
9. Blöchl, E.,, S. Burggraf,, G. Fiala,, G. Lauerer,, G. Huber,, H. Huber,, R. Rachel,, A. Segerer,, K. O. Stetter, and, P. Völkl. 1995. Isolation, taxonomy and phylogeny of hyperthermophilic microorganisms. World J. Microbiol. Biotechnol. 11: 9– 16
10. Borges, N.,, A. Ramos,, N. D. H. Raven,, R. J. Sharp, and, H. Santos. 2002. Comparative study of the thermostabilizing properties of mannosylglycerate and other compatible solutes on model enzymes. Extremophiles. 6: 209– 216
11. Borges, N.,, J. D. Marugg,, N. Empadinhas,, M. S. da Costa, and, H. Santos. 2004. Specialized roles of the two pathways for the synthesis of mannosylglycerate in osmoadaptation and thermoadaptation of Rhodothermus marinus. J. Biol. Chem. 279: 9892– 9898
12. Bouveng, H.,, B. Lindberg, and, B. Wickberg. 1955. Low-molecular carbohydrates in algae. Acta Chem. Scand. 9: 807– 809
13. Brown, A. D. 1976. Microbial water stress. Bacteriol. Rev. 40: 803– 846
14. Busby, T. F.,, and K. C. Ingham. 1984. Thermal stabilization of antithrombin III by sugars and sugar derivatives and the effects of nonenzymatic glycosylation. Biochim. Biophys. Acta. 799: 80– 89
15. Ciulla, R. A.,, S. Burggraf,, K. O. Stetter, and, M. F. Roberts. 1994. Occurrence and role of di- myo-inositol-1,1′-phosphate in Methanococcus igneus. Appl. Env. Microbiol. 60: 3660– 3664
16. Chen, L.,, E. T. Spiliotis, and, M. F. Roberts. 1998. Biosynthesis of di- myo-inositol-1,1′-phosphate, a novel osmolyte in hyperthermophilic archaea. J. Bacteriol. 180: 3785– 3792
17. Chen, L.,, C. Zhou,, H. Yang, and, M. F. Roberts. 2000. Inositol-1-phosphate synthase from Archaeoglobus fulgidus is a class II aldolase. Biochemistry. 39: 12415– 12423
18. da Costa, M. S.,, H. Santos, and, E. A. Galinski. 1998. An overview of the role and diversity of compatible solutes in Bacteria and Archaea. Adv. Biochem. Eng. Biotechnol. 61: 117– 153
19. Davis-Searles, P. R.,, A. J. Saunders,, D. A. Erie,, D. J. Winzor, and, G. J. Pielak. 2001. Interpreting the effect of small uncharged solutes on protein-folding equilibria. Annu. Rev. Biophys. Biomol. Struct. 30: 271– 306
20. Empadinhas, N.,, J. D. Marugg,, N. Borges,, H. Santos, and, M. S. da Costa. 2001. Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes. J. Biol. Chem. 276: 43580– 43588
21. Empadinhas, N.,, L. Albuquerque,, A. Henne,, H. Santos, and, M. S. da Costa. 2003. The bacterium Thermus thermophilus, like hyperthermophilic archaea, uses a two-step pathway for the synthesis of mannosylglycerate. Appl. Environ. Microbiol. 69: 3272– 3279
22. Empadinhas, N.,, L. Albuquerque,, J. Costa,, S. H. Zinder,, M. A. Santos,, H. Santos, and, M. S. da Costa. 2004. A gene from the mesophilic bacterium Dehalococcoides ethenogenes encodes a novel mannosylglycerate synthase. J. Bacteriol. 186: 4075– 4084
23. Empadinhas, N. 2004. Pathways for the synthesis of mannosylglycerate in prokaryotes: genes, enzymes and evolutionary implications. Ph. D. thesis, University of Coimbra, Portugal.
24. Faria, T. Q.,, S. Knapp,, R. Ladenstein,, A. L. Maçanita, and, H. Santos. 2003. Protein stabilisation by compatible solutes: effect of mannosylglycerate on unfolding thermodynamics and activity of ribonuclease A. ChemBioChem. 4: 734– 741
25. Faria, T. Q.,, J. C. Lima,, M. Bastos,, A. L. Macanita, and, H. Santos. 2004. Protein stabilization by osmolytes from hyperthermophiles: effect of mannosylglycerate on the thermal unfolding of recombinant nuclease a from Staphylococcus aureus studied by picosecond time-resolved fluorescence and calorimetry. J. Biol. Chem. 279: 48680– 48691
26. Flint, J.,, E. Taylor,, M. Yang,, D. N. Bolam,, L. E. Tailford,, C. Martinez-Fleites,, E. J. Dodson,, B. G. Davis,, H. J. Gilbert, and, G. J. Davies. 2005. Structural dissection and high-throughput screening of mannosylglycerate synthase. Nat. Struct. Mol. Biol. 12: 608– 614
27. Foord, R. L.,, and R. J. Leatherbarrow. 1998. Effect of osmolytes on the exchange rates of backbone amide proton in proteins. Biochemistry. 37: 2969– 2978
28. Galinski, E. A. 1995. Osmoadaptation in Bacteria. Adv. Microb. Physiol. 37: 272– 328
29. Gekko, K.,, and S. N. Timasheff. 1981. Thermodynamic and kinetic examination of protein stabilization by glycerol. Biochemistry. 20: 4677– 4686
30. Gonçalves, L. G.,, R. Huber,, M. S. da Costa, and, H. Santos. 2003. A variant of the hyperthermophile Archaeoglobus fulgidus adapted to grow at high salinity. FEMS Microbiol. Lett. 218: 239– 244
31. Gorkovenko, A.,, M. F. Roberts, and, R. H. White. 1994. Identification, biosynthesis, and function of 1,3,4,6-hexanetetracarboxylic acid in Methanobacterium thermoautotrophicum DeltaH. Appl. Environ. Microbiol. 60: 1249– 1253
32. Hensel, R., and H. König. 1988. Thermoadaptation of methanogenic bacteria by intracellular ion concentration. FEMS Microbiol. Lett. 49: 75– 79
33. Hensel, R. 1993. Proteins of extreme thermophiles. New Comp. Biochem. 26: 209– 221
34. Karsten, U.,, K. D. Barrow,, A. S. Mostaert,, R. J. King, and, J. A. West. 1994. 13C- and 1H-NMR studies on digeneaside in the red alga Caloglossa leprieurii. A re-evaluation of its osmotic significance. Plant Physiol. Biochem. 32: 669– 676
35. Kaushik, J. K.,, and R. Bhat. 1998. Thermal stability of proteins in aqueous polyol solutions: role of the surface tension of water in the stabilizing effect of polyols. J. Phys. Chem. B. 102: 7058– 7066
36. Kaushik, J. K., and R. Bhat. 1999. A mechanistic analysis of the increase in the thermal stability of proteins in aqueous carboxylic acid salt solutions. Protein Sci. 8: 222– 233
37. Lamosa, P.,, L. O. Martins,, M. S. da Costa, and, H. Santos. 1998. Effects of temperature, salinity, and medium composition on compatible solute accumulation by Thermococcus spp. Appl. Environ. Microbiol. 64: 3591– 3598
38. Lamosa, P.,, A. Burke,, R. Peist,, R. Huber,, M. Y. Liu,, G. Silva,, C. Rodrigues-Pousada,, J. LeGall,, C. Maycock, and, H. Santos. 2000. Thermostabilization of proteins by diglycerol phosphate, a new compatible solute from the hyperthermophile Archaeoglobus fulgidus. Appl. Environ. Microbiol. 66: 1974– 1979
39. Lamosa, P.,, L. Brennan,, H. Vis,, D. L. Turner, and, H. Santos. 2001. NMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabilization by compatible solutes. Extremophiles. 5: 303– 311.
40. Lamosa, P.,, D. L. Turner,, R. Ventura,, C. Maycock, and, H. Santos. 2003. Protein stabilization by compatible solutes: effect of diglycerol phosphate on the dynamics of Desulfovibrio gigas rubredoxin studied by NMR. Eur. J. Biochem. 270: 4606– 4614
41. Lee, J. C.,, and S. N. Timasheff. 1981. The stabilization of proteins by sucrose. J. Biol. Chem. 256: 7193– 7201
42. Lin, T. Y.,, and S. N. Timasheff. 1996. On the role of surface tension in the stabilization of globular proteins. Protein Sci. 5: 372– 381
43. Liu, Y.,, and D. W. Bolen. 1995. The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes. Biochemistry. 34: 12884– 12891
44. Martin, D. D.,, R. A. Ciulla, and, M. F. Roberts. 1999. Osmoadaptation in Archaea. Appl. Environ. Microbiol. 65: 1815– 1825
45. Martins, L. O.,, and H. Santos. 1995. Accumulation of mannosylglycerate and di- myo-inositol-phosphate by Pyrococcus furiosos in response to salinity and temperature. Appl. Environ. Microbiol. 61: 3299– 3303
46. Martins, L. O.,, L. S. Carreto,, M. S. da Costa, and, H. Santos. 1996. New compatible solutes related to di- myo-inositol-phosphate in members of the order Thermotogales. J. Bacteriol. 178: 5644– 5651
47. Martins, L. O.,, R. Huber,, H. Huber,, K. O. Stetter,, M. S. da Costa, and, H. Santos. 1997. Organic solutes in hyperthermophilic Archaea. Appl. Environ. Microbiol. 63: 896– 902
48. Martins, L. O.,, N. Empadinhas,, J. D. Marugg,, C. Miguel,, C. Ferreira,, M. S. da Costa, and, H. Santos. 1999. Biosynthesis of mannosylglycerate in the thermophilic bacterium Rhodothermus marinus. Biochemical and genetic characterization of a mannosylglycerate synthase. J. Biol. Chem. 274: 35407– 35414
49. Neves, C.,, M. S. da Costa, and, H. Santos. 2005. Compatible solutes of the hyperthermophile Palaeococcus ferrophilus: osmoadaptation and thermoadaptation in the order Thermococcales. Appl. Environ. Microbiol. 71: 8091– 8098
50. Nunes, O. C.,, C. M. Manaia,, M. S. da Costa, and, H. Santos. 1995. Compatible solutes in the thermophilic bacteria Rhodothermus marinus and “Thermus thermophilus”. Appl. Environ. Microbiol. 61: 2351– 2357
51. Oren, A. 1999. Bioenergetic aspects of halophilism. Microbiol. Mol. Biol. Rev. 63: 334– 348
52. Pais, T. M.,, P. Lamosa,, W. dos Santos,, J. LeGall,, D. L. Turner, and, H. Santos. 2005. Structural determinants of protein stabilization by solutes. The importance of the hairpin loop in rubredoxins. FEBS J. 272: 999– 1011
53. Pittz, E. P.,, and S. N. Timasheff. 1978. Interaction of ribonuclease A with aqueous 2-methyl-2,4-pentanediol at pH 5.8. Biochemistry 17: 615– 623
54. Qu, Y.,, C. L. Bolen, and, D. W. Bolen. 1998. Osmolyte-driven contraction of a random coil protein. Proc. Natl. Acad. Sci. USA. 95: 9268– 9273
55. Ramakrishnan, V.,, Q. Teng, and, M. W. Adams. 1997. Characterization of UDP amino sugars as major phosphocompounds in the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 179: 1505– 1512
56. Ramos, A.,, N. D. H. Raven,, R. J. Sharp,, S. Bartolucci,, M. Rossi,, R. Cannio,, J. Lebbink,, J. van der Oost,, W. M. de Vos, and, H. Santos. 1997. Stabilization of enzymes against thermal stress and freeze-drying by mannosylglycerate. Appl. Environ. Microbiol. 63: 4020– 4025
57. Ramos, C. H. I.,, and R. L. Baldwin. 2002. Sulfate anion stabilization of native ribonuclease A both by anion binding and the Hofmeister effect. Protein Sci. 11: 1771– 1778
58. Robertson, D. E.,, M. F. Roberts,, N. Belay,, K. O. Stetter, and, D. R. Boone. 1990. Occurrence of β-glutamate, a novel osmolyte, in marine methanogenic bacteria. Appl. Environ. Microbiol. 56: 1504– 1508
59. Rohlin, L.,, J. D. Trent,, K. Salmon,, U. Kim,, R. P. Gunsalus, and, J. C. Liao. 2005. Heat shock response in Archaeoglobus fulgidus. J. Bacteriol. 187: 6046– 6057
60. Santos, H.,, P. Lamosa,, A. Burke, and, C. Maycock. 1999. Thermostabilisation, osmoprotection, and protection against desiccation of enzymes, and cell components by di-glycerol- phosphate. European patent no. 98670002.9.
61. Santos, H.,, and M. S. da Costa. 2001. Organic solutes from thermophiles and hyperthermophiles. Methods Enzymol. 334: 302– 315
62. Santos, H.,, and M. S. da Costa. 2002. Compatible solutes of organisms that live in hot saline environments. Environ. Microbiol. 4: 501– 509
63. Santos, H.,, P. Lamosa,, C. Jorge, and, M. S. da Costa. 2003. Diglycosyl glyceryl compounds for the stabilisation or preservation of biomaterials. Submitted to the European Patent Office. (International publication number WO 2004/094631 A1).
64. Santos, H.,, P. Lamosa,, N. D. Raven,, L. G. Gonçalves, and, M. V. Rodrigues. 2005. Glycerophosphoinositol as a stabilizer and/or preservative of biological materials. Submitted to the European Patent Office.
65. Santos, H.,, P. Lamosa, and, N. Borges. 2006. Characterization of organic compatible solutes of thermophilic microorganisms, p. 171–198. In A. Oren and, F. Rainey (ed.), Methods in Microbiology: Extremophiles. Elsevier, Amsterdam, The Netherlands.
66. Scholz, S.,, J. Sonnenbichler,, W. Schäfer, and, R. Hensel. 1992. Di -myo-inositol-1,1′-phosphate: a new inositol phosphate isolated from Pyrococcus woesei. FEBS Lett. 306: 239– 242
67. Scholz, S.,, S. Wolff, and, R. Hensel. 1998. The biosynthesis pathway of di- myo-inositol-1,1′-phosphate in Pyrococcus woesei. FEMS Microbiol. Lett. 168: 37– 42
68. Shima, S.,, D. A. Hérault,, A. Berkessel, and, R. K. Thauer. 1998. Activation and thermostabilization effects of cyclic 2,3-diphosphoglycerate on enzymes from the hyperthermophilic Methanopyrus kandleri. Arch. Microbiol. 170: 469– 472
69. Schokley, K. R.,, D. E. Ward,, S. R. Chhabra,, S. B. Conners,, C. I. Montero, and, R. M. Kelly. 2003. Heat shock response by the hyperthermophilic archaeon Pyrococcus furiosus. Appl. Environ. Microbiol. 69: 2365– 2371
70. Silva, Z.,, N. Borges,, L. O. Martins,, R. Wait,, M. S. da Costa, and, H. Santos. 1999. Combined effect of the growth temperature and salinity of the medium on the accumulation of compatible solutes by Rhodothermus marinus and Rhodothermus obamensis. Extremophiles. 3: 163– 172
71. Timasheff, S. N. 1993. The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annu. Rev. Biophys. Biomol. Struct. 22: 67– 97

Tables

The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles
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Citation: Santos H, Lamosa P, Faria T, Borges N, Neves C. 2007. The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles, p 86-103. In Gerday C, Glansdorff N (ed), Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC. doi: 10.1128/9781555815813.ch7
/content/10.1128/9781555815813.ch07.ch07tab01
Table 1.
Distribution of compatible solutes of (hyper)thermophilic microorganisms
Generic image for table
Table 1.

Distribution of compatible solutes of (hyper)thermophilic microorganisms

Citation: Santos H, Lamosa P, Faria T, Borges N, Neves C. 2007. The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles, p 86-103. In Gerday C, Glansdorff N (ed), Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC. doi: 10.1128/9781555815813.ch7
/content/10.1128/9781555815813.ch07.ch07tab02
Table 2.
Biochemical properties of recombinant mannosyl-3-phosphoglycerate synthase from and
Generic image for table
Table 2.

Biochemical properties of recombinant mannosyl-3-phosphoglycerate synthase from and

Citation: Santos H, Lamosa P, Faria T, Borges N, Neves C. 2007. The Physiological Role, Biosynthesis, and Mode of Action of Compatible Solutes from (Hyper)Thermophiles, p 86-103. In Gerday C, Glansdorff N (ed), Physiology and Biochemistry of Extremophiles. ASM Press, Washington, DC. doi: 10.1128/9781555815813.ch7

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