메뉴 건너뛰기




Volumn 52, Issue 28, 2013, Pages 4774-4780

Evolvability of thermophilic proteins from archaea and bacteria

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTIC PROTEINS; EVOLUTION PROCESS; HYDROPHOBIC INTERACTIONS; LOSS OF STABILITY; PROMOTING PROTEIN; STABILIZATION MECHANISMS; THERMOPHILIC ARCHAEA; THERMOPHILIC PROTEINS;

EID: 84880563504     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400652c     Document Type: Article
Times cited : (24)

References (44)
  • 1
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke, R. and Bohm, G. (1998) The stability of proteins in extreme environments Curr. Opin. Struct. Biol. 8, 738-748
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 738-748
    • Jaenicke, R.1    Bohm, G.2
  • 2
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • Vieille, C. and Zeikus, G. J. (2001) Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability Microbiol. Mol. Biol. Rev. 65, 1-43
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 3
    • 0037016635 scopus 로고    scopus 로고
    • Some like it hot: The molecular determinants of protein thermostability
    • Perl, D. and Schmid, F. X. (2002) Some like it hot: The molecular determinants of protein thermostability ChemBioChem 3, 39-44
    • (2002) ChemBioChem , vol.3 , pp. 39-44
    • Perl, D.1    Schmid, F.X.2
  • 4
    • 33745726737 scopus 로고    scopus 로고
    • Lessons in stability from thermophilic proteins
    • Razvi, A. and Scholtz, J. M. (2006) Lessons in stability from thermophilic proteins Protein Sci. 15, 1569-1578
    • (2006) Protein Sci. , vol.15 , pp. 1569-1578
    • Razvi, A.1    Scholtz, J.M.2
  • 5
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese, C. R., Kandler, O., and Wheelis, M. L. (1990) Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya Proc. Natl. Acad. Sci. U.S.A. 87, 4576-4579
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 6
    • 0034524673 scopus 로고    scopus 로고
    • Hydrothermal circulation of seawater through hot vents and contribution of interface chemistry to prebiotic synthesis
    • Ogata, Y., Imai, E., Honda, H., Hatori, K., and Matsuno, K. (2000) Hydrothermal circulation of seawater through hot vents and contribution of interface chemistry to prebiotic synthesis Origins Life Evol. Biospheres 30, 527-537
    • (2000) Origins Life Evol. Biospheres , vol.30 , pp. 527-537
    • Ogata, Y.1    Imai, E.2    Honda, H.3    Hatori, K.4    Matsuno, K.5
  • 7
    • 0033609333 scopus 로고    scopus 로고
    • Evidence for lateral gene transfer between archaea and bacteria from genome sequence of Thermotoga maritima
    • Nelson, K. E. 1999, Evidence for lateral gene transfer between archaea and bacteria from genome sequence of Thermotoga maritima Nature 399, 323-329
    • (1999) Nature , vol.399 , pp. 323-329
    • Nelson, K.E.1
  • 8
    • 0032568375 scopus 로고    scopus 로고
    • The complete genome of the hyperthermophilic bacterium Aquifex aeolicus
    • Deckert, G. 1998, The complete genome of the hyperthermophilic bacterium Aquifex aeolicus Nature 392, 353-358
    • (1998) Nature , vol.392 , pp. 353-358
    • Deckert, G.1
  • 9
    • 0033534584 scopus 로고    scopus 로고
    • A nonhyperthermophilic common ancestor to extant life forms
    • Galtier, N., Tourasse, N., and Gouy, M. (1999) A nonhyperthermophilic common ancestor to extant life forms Science 283, 220-221
    • (1999) Science , vol.283 , pp. 220-221
    • Galtier, N.1    Tourasse, N.2    Gouy, M.3
  • 11
    • 34248161913 scopus 로고    scopus 로고
    • Environment specific substitution tables for thermophilic proteins
    • Mizuguchi, K., Sele, M., and Cubellis, M. V. (2007) Environment specific substitution tables for thermophilic proteins BMC Bioinf. 8 (Suppl. 1) S15
    • (2007) BMC Bioinf. , vol.8 , Issue.SUPPL. 1 , pp. 15
    • Mizuguchi, K.1    Sele, M.2    Cubellis, M.V.3
  • 12
    • 77954338351 scopus 로고    scopus 로고
    • Evolution and thermodynamics of slow unfolding of hyperstable monomeric proteins
    • Okada, J. 2010, Evolution and thermodynamics of slow unfolding of hyperstable monomeric proteins BMC Evol. Biol. 10, 207
    • (2010) BMC Evol. Biol. , vol.10 , pp. 207
    • Okada, J.1
  • 13
    • 23944490117 scopus 로고    scopus 로고
    • Missense meanderings in sequence space: A biophysical view of protein evolution
    • DePristo, M. A., Weinreich, D. M., and Hartl, D. L. (2005) Missense meanderings in sequence space: A biophysical view of protein evolution Nat. Rev. Genet. 6, 678-687
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 678-687
    • Depristo, M.A.1    Weinreich, D.M.2    Hartl, D.L.3
  • 15
    • 36049027813 scopus 로고    scopus 로고
    • Protein stability imposes limits on organism complexity and speed of molecular evolution
    • Zeldovich, K. B., Chen, P., and Shakhnovich, E. I. (2007) Protein stability imposes limits on organism complexity and speed of molecular evolution Proc. Natl. Acad. Sci. U.S.A. 104, 16152-16157
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 16152-16157
    • Zeldovich, K.B.1    Chen, P.2    Shakhnovich, E.I.3
  • 16
    • 0036295508 scopus 로고    scopus 로고
    • Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs
    • Wang, X., Minasov, G., and Shoichet, B. K. (2002) Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs J. Mol. Biol. 320, 85-95
    • (2002) J. Mol. Biol. , vol.320 , pp. 85-95
    • Wang, X.1    Minasov, G.2    Shoichet, B.K.3
  • 19
    • 0030483509 scopus 로고    scopus 로고
    • Directed evolution: Creating biocatalysts for the future
    • Arnold, F. (1996) Directed evolution: Creating biocatalysts for the future Chem. Eng. Sci. 51, 5091-5102
    • (1996) Chem. Eng. Sci. , vol.51 , pp. 5091-5102
    • Arnold, F.1
  • 22
    • 0036897839 scopus 로고    scopus 로고
    • Milestones in directed enzyme evolution
    • Tao, H. and Cornish, V. (2002) Milestones in directed enzyme evolution Curr. Opin. Chem. Biol. 6, 858-864
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 858-864
    • Tao, H.1    Cornish, V.2
  • 23
    • 0042432086 scopus 로고    scopus 로고
    • Directed evolution of industrial enzymes: An update
    • Cherry, J. R. and Fidantsef, A. L. (2003) Directed evolution of industrial enzymes: An update Curr. Opin. Biotechnol. 14, 438-443
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 438-443
    • Cherry, J.R.1    Fidantsef, A.L.2
  • 24
    • 66649132872 scopus 로고    scopus 로고
    • Chaperonin overexpression promotes genetic variation and enzyme evolution
    • Tokuriki, N. and Tawfik, D. S. (2009) Chaperonin overexpression promotes genetic variation and enzyme evolution Nature 459, 668-673
    • (2009) Nature , vol.459 , pp. 668-673
    • Tokuriki, N.1    Tawfik, D.S.2
  • 25
    • 84865274509 scopus 로고    scopus 로고
    • Structure and stability of a thermostable carboxylesterase from the thermoacidophilic archaeon Sulfolobus tokodaii
    • Angkawidjaja, C., Koga, Y., Takano, K., and Kanaya, S. (2012) Structure and stability of a thermostable carboxylesterase from the thermoacidophilic archaeon Sulfolobus tokodaii FEBS J. 279, 3071-3084
    • (2012) FEBS J. , vol.279 , pp. 3071-3084
    • Angkawidjaja, C.1    Koga, Y.2    Takano, K.3    Kanaya, S.4
  • 26
    • 0032524806 scopus 로고    scopus 로고
    • Overexpression and properties of a new thermophilic and thermostable esterase from Bacillus acidocaldarius with sequence similarity to hormone-sensitive lipase subfamily
    • Manco, G., Adinolfi, E., Pisani, F. M., Ottolina, G., Carrea, G., and Rossi, M. (1998) Overexpression and properties of a new thermophilic and thermostable esterase from Bacillus acidocaldarius with sequence similarity to hormone-sensitive lipase subfamily Biochem. J. 332, 203-212
    • (1998) Biochem. J. , vol.332 , pp. 203-212
    • Manco, G.1    Adinolfi, E.2    Pisani, F.M.3    Ottolina, G.4    Carrea, G.5    Rossi, M.6
  • 27
    • 9644275365 scopus 로고    scopus 로고
    • Role of the N terminus in enzyme activity, stability and specificity in thermophilic esterases belonging to the HSL family
    • Mandrich, L. 2005, Role of the N terminus in enzyme activity, stability and specificity in thermophilic esterases belonging to the HSL family J. Mol. Biol. 345, 501-512
    • (2005) J. Mol. Biol. , vol.345 , pp. 501-512
    • Mandrich, L.1
  • 28
    • 58149131238 scopus 로고    scopus 로고
    • Crystal structure and biochemical properties of a novel thermostable esterase containing an immunoglobulin-like domain
    • Levisson, M. 2009, Crystal structure and biochemical properties of a novel thermostable esterase containing an immunoglobulin-like domain J. Mol. Biol. 385, 949-962
    • (2009) J. Mol. Biol. , vol.385 , pp. 949-962
    • Levisson, M.1
  • 30
    • 2942522721 scopus 로고    scopus 로고
    • ASAView: Database and tool for solvent accessibility representation in proteins
    • Ahmad, S., Gromiha, M., Fawareh, H., and Sarai, A. (2004) ASAView: Database and tool for solvent accessibility representation in proteins BMC Bioinf. 5, 51
    • (2004) BMC Bioinf. , vol.5 , pp. 51
    • Ahmad, S.1    Gromiha, M.2    Fawareh, H.3    Sarai, A.4
  • 31
    • 0029620316 scopus 로고
    • Modeling unfolded states of peptides and proteins
    • Creamer, T. P., Srinivasan, R., and Rose, G. D. (1995) Modeling unfolded states of peptides and proteins Biochemistry 34, 16245-16250
    • (1995) Biochemistry , vol.34 , pp. 16245-16250
    • Creamer, T.P.1    Srinivasan, R.2    Rose, G.D.3
  • 32
    • 0030933329 scopus 로고    scopus 로고
    • Modeling unfolded states of proteins and peptides. II. Backbone solvent accessibility
    • Creamer, T. P., Srinivasan, R., and Rose, G. D. (1997) Modeling unfolded states of proteins and peptides. II. Backbone solvent accessibility Biochemistry 36, 2832-2835
    • (1997) Biochemistry , vol.36 , pp. 2832-2835
    • Creamer, T.P.1    Srinivasan, R.2    Rose, G.D.3
  • 34
    • 84874797243 scopus 로고    scopus 로고
    • Hydrophobic environment is a key factor for the stability of thermophilic proteins
    • Gromiha, M. M., Pathak, M. C., Saraboji, K., Ortlund, E. A., and Gaucher, E. A. (2013) Hydrophobic environment is a key factor for the stability of thermophilic proteins Proteins 81, 715-721
    • (2013) Proteins , vol.81 , pp. 715-721
    • Gromiha, M.M.1    Pathak, M.C.2    Saraboji, K.3    Ortlund, E.A.4    Gaucher, E.A.5
  • 35
    • 84871251754 scopus 로고    scopus 로고
    • Comprehensive analysis of surface charged residues involved in thermal stability in Alicyclobacillus acidocaldarius esterase 2
    • Pezzullo, M., Del Vecchio, P., Mandrich, L., Nucci, R., Rossi, M., and Manco, G. (2013) Comprehensive analysis of surface charged residues involved in thermal stability in Alicyclobacillus acidocaldarius esterase 2 Protein Eng., Des. Sel. 26, 47-58
    • (2013) Protein Eng., Des. Sel. , vol.26 , pp. 47-58
    • Pezzullo, M.1    Del Vecchio, P.2    Mandrich, L.3    Nucci, R.4    Rossi, M.5    Manco, G.6
  • 36
    • 34548730241 scopus 로고    scopus 로고
    • Different packing of external residues can explain differences in the thermostability of proteins from thermophilic and mesophilic organisms
    • Glyakina, A. V., Garbuzynskiy, S. O., Lobanov, M. Y., and Galzitskaya, O. V. (2007) Different packing of external residues can explain differences in the thermostability of proteins from thermophilic and mesophilic organisms Bioinformatics 23, 2231-2238
    • (2007) Bioinformatics , vol.23 , pp. 2231-2238
    • Glyakina, A.V.1    Garbuzynskiy, S.O.2    Lobanov, M.Y.3    Galzitskaya, O.V.4
  • 37
    • 33750349072 scopus 로고    scopus 로고
    • A hyperthermophilic protein acquires function at the cost of stability
    • Mukaiyama, A., Haruki, M., Ota, M., Koga, Y., Takano, K., and Kanaya, S. (2006) A hyperthermophilic protein acquires function at the cost of stability Biochemistry 45, 12673-12679
    • (2006) Biochemistry , vol.45 , pp. 12673-12679
    • Mukaiyama, A.1    Haruki, M.2    Ota, M.3    Koga, Y.4    Takano, K.5    Kanaya, S.6
  • 38
    • 74649086461 scopus 로고    scopus 로고
    • Structural bases for stability-function tradeoffs in antibiotic resistance
    • Thomas, V. L., McReynolds, A. C., and Shoichet, B. K. (2010) Structural bases for stability-function tradeoffs in antibiotic resistance J. Mol. Biol. 396, 47-59
    • (2010) J. Mol. Biol. , vol.396 , pp. 47-59
    • Thomas, V.L.1    McReynolds, A.C.2    Shoichet, B.K.3
  • 39
    • 70349901079 scopus 로고    scopus 로고
    • Stability effects of mutations and protein evolvability
    • Tokuriki, N. and Tawfik, D. S. (2009) Stability effects of mutations and protein evolvability Curr. Opin. Struct. Biol. 19, 596-604
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 596-604
    • Tokuriki, N.1    Tawfik, D.S.2
  • 40
    • 34248674895 scopus 로고    scopus 로고
    • The stability effects of protein mutations appear to be universally distributed
    • Tokuriki, N., Stricher, F., Schymkowitz, J., Serrano, L., and Tawfik, D. S. (2007) The stability effects of protein mutations appear to be universally distributed J. Mol. Biol. 369, 1318-1332
    • (2007) J. Mol. Biol. , vol.369 , pp. 1318-1332
    • Tokuriki, N.1    Stricher, F.2    Schymkowitz, J.3    Serrano, L.4    Tawfik, D.S.5
  • 41
    • 0036484726 scopus 로고    scopus 로고
    • Sulfolobus tokodaii sp. nov. (Sulfolobus sp. Strain 7), a new member of the genus Sulfolobus isolated from Beppu Hot Springs, Japan
    • Suzuki, T. 2002, Sulfolobus tokodaii sp. nov. (Sulfolobus sp. Strain 7), a new member of the genus Sulfolobus isolated from Beppu Hot Springs, Japan Extremophiles 6, 39-44
    • (2002) Extremophiles , vol.6 , pp. 39-44
    • Suzuki, T.1
  • 42
    • 8444239349 scopus 로고    scopus 로고
    • Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1
    • Atomi, H., Fukui, T., Kanai, T., Morikawa, M., and Imanaka, T. (2004) Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1 Archaea 1, 263-267
    • (2004) Archaea , vol.1 , pp. 263-267
    • Atomi, H.1    Fukui, T.2    Kanai, T.3    Morikawa, M.4    Imanaka, T.5
  • 43
    • 56349110780 scopus 로고    scopus 로고
    • Isolation, identification and typification of Alicyclobacillus acidoterrestris and Alicyclobacillus acidocaldarius strains from orchard soil and the fruit processing environment in South Africa
    • Groenewald, W. H., Gouws, P. A., and Witthuhn, R. C. (2009) Isolation, identification and typification of Alicyclobacillus acidoterrestris and Alicyclobacillus acidocaldarius strains from orchard soil and the fruit processing environment in South Africa Food Microbiol. 26, 71-76
    • (2009) Food Microbiol. , vol.26 , pp. 71-76
    • Groenewald, W.H.1    Gouws, P.A.2    Witthuhn, R.C.3
  • 44
    • 0022522022 scopus 로고
    • Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90 C
    • Huber, R. 1986, Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90 C Arch. Microbiol. 144, 324-333 Technology
    • (1986) Arch. Microbiol. , vol.144 , pp. 324
    • Huber, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.