Evolutionary drivers of thermoadaptation in enzyme catalysis

Science

Volumn 355, Issue 6322, 2017, Pages 289-294

  Nguyen, Vy ^a   Wilson, Christopher ^a   Hoemberger, Marc ^a   Stiller, John B ^a   Agafonov, Roman V ^a   Kutter, Steffen ^a   English, Justin ^a   Theobald, Douglas L ^a   Kern, Dorothee ^a  

^a BRANDEIS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE KINASE; ENZYME; ADENYLATE CYCLASE;

ADAPTATION; CATALYSIS; ENZYME ACTIVITY; LOW TEMPERATURE; MOLECULAR ANALYSIS; THERMOPHILY; THERMOREGULATION; TRADE-OFF;

ARTICLE; CATALYSIS; CATALYTIC EFFICIENCY; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENVIRONMENTAL TEMPERATURE; ENZYME ACTIVITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN STABILITY; SUBSTRATE CONCENTRATION; TEMPERATURE ACCLIMATIZATION; TEMPERATURE DEPENDENCE; THERMOSTABILITY; BIOCATALYSIS; CHEMISTRY; CLASSIFICATION; GENETICS; HEAT; HEAT TOLERANCE; KINETICS; MOLECULAR EVOLUTION; MUTATION; PHYLOGENY;

ADENYLYL CYCLASES; BIOCATALYSIS; EVOLUTION, MOLECULAR; HOT TEMPERATURE; KINETICS; MUTATION; PHYLOGENY; THERMOTOLERANCE;

EID: 85007170381     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aah3717     Document Type: Article

References (38)

1. A. Clarke et al., PLOS ONE 8, e66207 (2013).
2. D. A. Cowan, Trends Microbiol. 12, 58-60 (2004).
3. J. W. Deming, Curr. Opin. Microbiol. 5, 301-309 (2002).
4. E. Blöchl et al., Extremophiles 1, 14-21 (1997).
5. F. D. Ciccarelli et al., Science 311, 1283-1287 (2006).
6. L. P. Knauth, D. R. Lowe, Geol. Soc. Am. Bull. 115, 566-580 (2003).
7. P. Fralick, J. E. Carter, Precambrian Res. 191, 78-84 (2011).
8. E. A. Gaucher, S. Govindarajan, O. K. Ganesh, Nature 451, 704-707 (2008).
9. S. Akanuma et al., Proc. Natl. Acad. Sci. U.S.A. 110, 11067-11072 (2013).
10. V. A. Risso, J. A. Gavira, D. F. Mejia-Carmona, E. A. Gaucher, J. M. Sanchez-Ruiz, J. Am. Chem. Soc. 135, 2899-2902 (2013).
11. J. K. Hobbs et al., Mol. Biol. Evol. 29, 825-835 (2012).
12. R. B. Stockbridge, C. A. Lewis Jr., Y. Yuan, R. Wolfenden, Proc. Natl. Acad. Sci. U.S.A. 107, 22102-22105 (2010).
13. R. Wolfenden, Cell. Mol. Life Sci. 71, 2909-2915 (2014).
14. M. J. Harms, J. W. Thornton, Nat. Rev. Genet. 14, 559-571 (2013).
15. R. Couñago, Y. Shamoo, Extremophiles 9, 135-144 (2005).
16. R. Couñago, S. Chen, Y. Shamoo, Mol. Cell 22, 441-449 (2006).
17. A. Moreno-Letelier, G. Olmedo-Alvarez, L. E. Eguiarte, V. Souza, Astrobiology 12, 674-684 (2012).
18. B. D. Redelings, M. A. Suchard, Syst. Biol. 54, 401-418 (2005).
19. F. U. Battistuzzi, A. Feijao, S. B. Hedges, BMC Evol. Biol. 4, 44 (2004).
20. P. D. Williams, D. D. Pollock, B. P. Blackburne, R. A. Goldstein, PLOS Comput. Biol. 2, e69 (2006).
21. A. Case, R. L. Stein, Biochemistry 42, 3335-3348 (2003).
22. S. J. Kerns et al., Nat. Struct. Mol. Biol. 22, 124-131 (2015).
23. M. Oliveberg, Y. J. Tan, A. R. Fersht, Proc. Natl. Acad. Sci. U.S.A. 92, 8926-8929 (1995).
24. G. A. Petsko, Methods Enzymol. 334, 469-478 (2001).
25. D. R. Zeigler, Microbiology 160, 1-11 (2014).
26. R. A. Goldstein, Proteins 79, 1396-1407 (2011).
27. E. Bornberg-Bauer, H. S. Chan, Proc. Natl. Acad. Sci. U.S.A. 96, 10689-10694 (1999).
28. V. A. Risso et al., J. Am. Chem. Soc. 135, 2899-2902 (2013).
29. E. Bae, G. N. Phillips Jr., J. Biol. Chem. 279, 28202-28208 (2004).
30. N. V. Prabhu, K. A. Sharp, Annu. Rev. Phys. Chem. 56, 521-548 (2005).
31. C. Canepa, Chem. Cent. J. 5, 22 (2011).
32. R. Nussinov, P. G. Wolynes, Phys. Chem. Chem. Phys. 16, 6321-6322 (2014).
33. P. G. Wolynes, W. A. Eaton, A. R. Fersht, Proc. Natl. Acad. Sci. U.S.A. 109, 17770-17771 (2012).
34. R. B. Stockbridge, R. Wolfenden, J. Biol. Chem. 284, 22747-22757 (2009).
35. G. Holtmann, E. Bremer, J. Bacteriol. 186, 1683-1693 (2004).
36. D. S. Nichols, P. D. Nichols, T. A. McMeekin, Sci. Prog. 78, 311-348 (1995).
37. T. N. Nazina et al., Int. J. Syst. Evol. Microbiol. 51, 433-446 (2001).
38. R. Huber, K. O. Stetter, Methods Enzymol. 330, 11-24 (2001).