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Volumn 82, Issue 6, 2014, Pages 887-896

Phenotypic comparisons of consensus variants versus laboratory resurrections of Precambrian proteins

Author keywords

Antibiotic degradation; Consensus proteins; Lactamases; Protein engineering; Protein stability; Resurrected proteins; Substrate promiscuity

Indexed keywords

AMINO ACID; BETA LACTAMASE; BETA LACTAMASE TEM 1; NUCLEOSIDE DIPHOSPHATE KINASE; PROTEIN VARIANT; BACTERIAL PROTEIN;

EID: 84900832991     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24575     Document Type: Article
Times cited : (52)

References (28)
  • 1
    • 0002725360 scopus 로고
    • Chemical paleogenetics. Molecular "restoration studies" of extinct forms of life
    • Pauling L, Zuckerkandl E. Chemical paleogenetics. Molecular "restoration studies" of extinct forms of life. Acta Chem Scan 1963;17:S9-S16.
    • (1963) Acta Chem Scan , vol.17
    • Pauling, L.1    Zuckerkandl, E.2
  • 3
    • 84900793027 scopus 로고    scopus 로고
    • Liberles DE, editor Oxford: Oxford University Press
    • Liberles DE, editor. Ancestral sequence reconstruction. Oxford: Oxford University Press; 2010. p 252.
    • (2010) Ancestral sequence reconstruction , pp. 252
  • 4
    • 84880862788 scopus 로고    scopus 로고
    • Evolutionary biochemistry: revealing the historical and physical causes of protein properties
    • Harms MJ, Thornton JW. Evolutionary biochemistry: revealing the historical and physical causes of protein properties. Nat Rev Genetics 2013;14:559-571.
    • (2013) Nat Rev Genetics , vol.14 , pp. 559-571
    • Harms, M.J.1    Thornton, J.W.2
  • 5
    • 38949093003 scopus 로고    scopus 로고
    • Paleotemperature trend for Precambrian life inferred from resurrected proteins
    • Gaucher EA, Govindarajan S, Ganesh OK. Paleotemperature trend for Precambrian life inferred from resurrected proteins. Nature 2008;451:704-707.
    • (2008) Nature , vol.451 , pp. 704-707
    • Gaucher, E.A.1    Govindarajan, S.2    Ganesh, O.K.3
  • 7
    • 84874602326 scopus 로고    scopus 로고
    • Hyperstability and substrate promiscuity in laboratory resurrections of Precambrian β-lactamases
    • Risso VA, Gavira JA, Mejia-Carmona DF, Gaucher EA, Sanchez-Ruiz JM. Hyperstability and substrate promiscuity in laboratory resurrections of Precambrian β-lactamases. J Am Chem Soc 2013;135:2899-2902.
    • (2013) J Am Chem Soc , vol.135 , pp. 2899-2902
    • Risso, V.A.1    Gavira, J.A.2    Mejia-Carmona, D.F.3    Gaucher, E.A.4    Sanchez-Ruiz, J.M.5
  • 9
    • 0028111743 scopus 로고
    • Sequence statistics reliably predict stabilizing mutations in a protein domain
    • Steipe B, Schiller B, Plückthum A, Steinbacher S. Sequence statistics reliably predict stabilizing mutations in a protein domain. J Mol Biol 1994;240:182-192.
    • (1994) J Mol Biol , vol.240 , pp. 182-192
    • Steipe, B.1    Schiller, B.2    Plückthum, A.3    Steinbacher, S.4
  • 10
    • 0034731381 scopus 로고    scopus 로고
    • The consensus concept for thermostability engineering of proteins
    • Lehman M, Pasamontes L, Lassen SF, Wyss M. The consensus concept for thermostability engineering of proteins. Biochim Biophys Acta 2000;1543:408-415.
    • (2000) Biochim Biophys Acta , vol.1543 , pp. 408-415
    • Lehman, M.1    Pasamontes, L.2    Lassen, S.F.3    Wyss, M.4
  • 11
    • 0742289618 scopus 로고    scopus 로고
    • Relation between protein stability, evolution and structure, as probed by carboxylic acid mutations
    • Godoy-Ruiz R, Perez-Jimenez R, Ibarra-Molero B, Sanchez-Ruiz JM. Relation between protein stability, evolution and structure, as probed by carboxylic acid mutations. J Mol Biol 2004;336:313-318.
    • (2004) J Mol Biol , vol.336 , pp. 313-318
    • Godoy-Ruiz, R.1    Perez-Jimenez, R.2    Ibarra-Molero, B.3    Sanchez-Ruiz, J.M.4
  • 12
    • 33748454832 scopus 로고    scopus 로고
    • Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments
    • Godoy-Ruiz R, Ariza F, Rodriguez-Larrea, Perez-Jimenez R, Ibarra-Molero B, Sanchez-Ruiz JM. Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. J Mol Biol 2006;362:966-978.
    • (2006) J Mol Biol , vol.362 , pp. 966-978
    • Godoy-Ruiz, R.1    Ariza, F.2    Rodriguez-Larrea3    Perez-Jimenez, R.4    Ibarra-Molero, B.5    Sanchez-Ruiz, J.M.6
  • 15
    • 84863000087 scopus 로고    scopus 로고
    • Bridging the gaps in design methodologies by evolutionary optimization of the stability and proficiency of designed Kemp eliminase KE59
    • Khersonsky O, Kiss G, Röthlisberger D, Dym O, ALbeck S, Houk KN, Baker D, Tawfik DS. Bridging the gaps in design methodologies by evolutionary optimization of the stability and proficiency of designed Kemp eliminase KE59. Proc Natl Acad Sci USA 2012;109:10358-10363.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 10358-10363
    • Khersonsky, O.1    Kiss, G.2    Röthlisberger, D.3    Dym, O.4    Albeck, S.5    Houk, K.N.6    Baker, D.7    Tawfik, D.S.8
  • 16
    • 84874041859 scopus 로고    scopus 로고
    • Protein engineering and stabilization from sequence statistics: variation and covariation analysis
    • Durani V, Magliery TJ. Protein engineering and stabilization from sequence statistics: variation and covariation analysis. Methods Enzymol 2013;523:237-256.
    • (2013) Methods Enzymol , vol.523 , pp. 237-256
    • Durani, V.1    Magliery, T.J.2
  • 18
    • 44349161622 scopus 로고    scopus 로고
    • Intense neutral drifts yield robust and evolvable consensus proteins
    • Bershtein S, Goldin K, Tawfik DS. Intense neutral drifts yield robust and evolvable consensus proteins. J Mol Biol 2008;379:1029-1044.
    • (2008) J Mol Biol , vol.379 , pp. 1029-1044
    • Bershtein, S.1    Goldin, K.2    Tawfik, D.S.3
  • 19
    • 79958011043 scopus 로고    scopus 로고
    • Utilizing natural diversity to evolve protein function: applications towards thermostability
    • Cole MF, Gaucher EA. Utilizing natural diversity to evolve protein function: applications towards thermostability. Curr Opin Chem Biol 2011;15:399-406.
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 399-406
    • Cole, M.F.1    Gaucher, E.A.2
  • 21
    • 84862528672 scopus 로고    scopus 로고
    • X-ray evidence of a native state with increased compactness populated by tryptophan-less B. licheniformis β-lactamase
    • Risso VA, Acierno JP, Capaldi S, Monaco HL, Ermácora MR. X-ray evidence of a native state with increased compactness populated by tryptophan-less B. licheniformis β-lactamase. Protein Sci 2012;21:964-976.
    • (2012) Protein Sci , vol.21 , pp. 964-976
    • Risso, V.A.1    Acierno, J.P.2    Capaldi, S.3    Monaco, H.L.4    Ermácora, M.R.5
  • 23
    • 79958097953 scopus 로고    scopus 로고
    • The moderately efficient enzyme: evolutionary and physicochemical trends shaping enzyme parameters
    • Bar-Even A, Noor E, Savir Y, Liebermeister W, Davidi D, Tawfik DS, Milo R. The moderately efficient enzyme: evolutionary and physicochemical trends shaping enzyme parameters. Biochemistry 2011;50:4402-4410.
    • (2011) Biochemistry , vol.50 , pp. 4402-4410
    • Bar-Even, A.1    Noor, E.2    Savir, Y.3    Liebermeister, W.4    Davidi, D.5    Tawfik, D.S.6    Milo, R.7
  • 24
    • 84870477768 scopus 로고    scopus 로고
    • Reconstitution of translation from Thermus Thermophilus reveals a minimal set of components sufficient for protein synthesis at high temperatures and functional conservation of modern and ancient translation components
    • Zhou Y, Asahara H, Gaucher EA, Chong S. Reconstitution of translation from Thermus Thermophilus reveals a minimal set of components sufficient for protein synthesis at high temperatures and functional conservation of modern and ancient translation components. Nucleic Acid Res 2012;40:7932-7945.
    • (2012) Nucleic Acid Res , vol.40 , pp. 7932-7945
    • Zhou, Y.1    Asahara, H.2    Gaucher, E.A.3    Chong, S.4
  • 25
    • 84881105793 scopus 로고    scopus 로고
    • Structure- and sequence-analysis inspired engineering of proteins for enhanced thermostability
    • Wijma Hj, Floor RJ, Janssen DB. Structure- and sequence-analysis inspired engineering of proteins for enhanced thermostability. Curr Opin Struc Biol 2013;23:588-594.
    • (2013) Curr Opin Struc Biol , vol.23 , pp. 588-594
    • Wijma, H.1    Floor, R.J.2    Janssen, D.B.3
  • 28
    • 84864050202 scopus 로고    scopus 로고
    • Probing the mutational interplay between primary and promiscuous protein functions: a computational-experimental approach
    • Garcia-Seisdedos H, Ibarra-Molero B, Sanchez-Ruiz JM. Probing the mutational interplay between primary and promiscuous protein functions: a computational-experimental approach. PLoS Comp Biol 2012;8:e1002558.
    • (2012) PLoS Comp Biol , vol.8
    • Garcia-Seisdedos, H.1    Ibarra-Molero, B.2    Sanchez-Ruiz, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.