메뉴 건너뛰기




Volumn 15, Issue 8, 1998, Pages 1055-1061

Determining the evolutionary potential of a gene

Author keywords

Ebg; Evolutionary potential; galactosidase

Indexed keywords

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; DNA BASE COMPOSITION; ENZYME ACTIVITY; ESCHERICHIA COLI; EVOLUTION; GENE MUTATION; GENETIC ANALYSIS; NONHUMAN;

EID: 0031880490     PISSN: 07374038     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.molbev.a026004     Document Type: Article
Times cited : (21)

References (27)
  • 3
    • 0028787537 scopus 로고
    • Catalysis by the large subunit of the second β-galactosidase of Escherichia coli in the absence of the small subunit
    • CALUGARU, S. V., B. G. HALL, and M. L. SINNOTT. 1995. Catalysis by the large subunit of the second β-galactosidase of Escherichia coli in the absence of the small subunit. Biochem. J. 312:281-286.
    • (1995) Biochem. J. , vol.312 , pp. 281-286
    • Calugaru, S.V.1    Hall, B.G.2    Sinnott, M.L.3
  • 4
    • 0030764031 scopus 로고    scopus 로고
    • Larger increases in sensitivity to paracatalytic inactivation than in catalytic competence during experimental evolution of the second β galactosidase of Escherichia coli
    • CALUGARU, S. V., S. KRISHNAN, C. J. CHANY II, B. G. HALL, and M. L. SINNOTT. 1997. Larger increases in sensitivity to paracatalytic inactivation than in catalytic competence during experimental evolution of the second β galactosidase of Escherichia coli. Biochem. J. 325:117-121.
    • (1997) Biochem. J. , vol.325 , pp. 117-121
    • Calugaru, S.V.1    Krishnan, S.2    Chany II, C.J.3    Hall, B.G.4    Sinnott, M.L.5
  • 6
    • 0030696044 scopus 로고    scopus 로고
    • Determining the divergence times with a protein clock: Update and reevaluation
    • FENG, D.-F., G. CHO, and R. F. DOOLITTLE. 1997. Determining the divergence times with a protein clock: update and reevaluation. Proc. Natl. Acad. Sci. USA 94:13028-13033.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13028-13033
    • Feng, D.-F.1    Cho, G.2    Doolittle, R.F.3
  • 7
    • 0017844361 scopus 로고
    • Experimental evolution of a new enzymatic function: II. Evolution of multiple functions for EBG enzyme in E. coli
    • HALL, B. G. 1978a. Experimental evolution of a new enzymatic function: II. Evolution of multiple functions for EBG enzyme in E. coli. Genetics 89:453-465.
    • (1978) Genetics , vol.89 , pp. 453-465
    • Hall, B.G.1
  • 8
    • 0018165814 scopus 로고
    • Regulation of newly evolved enzymes. IV. Directed evolution of the ebg repressor
    • _. 1978b. Regulation of newly evolved enzymes. IV. Directed evolution of the ebg repressor. Genetics 90:673-691.
    • (1978) Genetics , vol.90 , pp. 673-691
  • 9
    • 0019874718 scopus 로고
    • Changes in the substrate specificities of an enzyme during directed evolution of new functions
    • _. 1981. Changes in the substrate specificities of an enzyme during directed evolution of new functions. Biochemistry 20:4042-4049.
    • (1981) Biochemistry , vol.20 , pp. 4042-4049
  • 10
    • 0020412175 scopus 로고
    • Evolution of a regulated operon in the laboratory
    • _. 1982a. Evolution of a regulated operon in the laboratory. Genetics 101:335-344.
    • (1982) Genetics , vol.101 , pp. 335-344
  • 11
    • 0020030825 scopus 로고
    • Transgalactosylation activity of ebg β-galactosidase synthesizes allolactose from lactose
    • _. 1982b. Transgalactosylation activity of ebg β-galactosidase synthesizes allolactose from lactose. J. Bacteriol. 150:132-140.
    • (1982) J. Bacteriol. , vol.150 , pp. 132-140
  • 12
    • 0025521673 scopus 로고
    • Directed evolution of a bacterial operon
    • _. 1990. Directed evolution of a bacterial operon. BioEssays 12:551-558.
    • (1990) BioEssays , vol.12 , pp. 551-558
  • 13
    • 0029299672 scopus 로고
    • Evolutionary potential of the ebgA gene
    • _. 1995. Evolutionary potential of the ebgA gene. Mol. Biol. Evol. 12:514-517.
    • (1995) Mol. Biol. Evol. , vol.12 , pp. 514-517
  • 14
    • 0024317110 scopus 로고
    • DNA sequence analysis of artificially evolved ebg enzyme and ebg repressor genes
    • HALL, B. G., P. W. BETTS, and J. C. WOOTTON. 1989. DNA sequence analysis of artificially evolved ebg enzyme and ebg repressor genes. Genetics 123:635-648.
    • (1989) Genetics , vol.123 , pp. 635-648
    • Hall, B.G.1    Betts, P.W.2    Wootton, J.C.3
  • 15
    • 0017593609 scopus 로고
    • Regulation of newly evolved enzymes. III. Evolution of the ebg repressor during selection for enhanced lactase activity
    • HALL, B. G., and N. D. CLARKE. 1977. Regulation of newly evolved enzymes. III. Evolution of the ebg repressor during selection for enhanced lactase activity. Genetics 85:193-201.
    • (1977) Genetics , vol.85 , pp. 193-201
    • Hall, B.G.1    Clarke, N.D.2
  • 16
    • 0016828871 scopus 로고
    • Regulation of newly evolved enzymes. II. The ebg repressor
    • HALL, B. G., and D. L. HARTL. 1975. Regulation of newly evolved enzymes. II. The ebg repressor. Genetics 81:427-435.
    • (1975) Genetics , vol.81 , pp. 427-435
    • Hall, B.G.1    Hartl, D.L.2
  • 18
    • 0019216932 scopus 로고
    • The ebg operon consists of at least two genes
    • HALL, B. G., and T. ZUZEL. 1980. The ebg operon consists of at least two genes. J. Bacteriol. 144:1208-1211.
    • (1980) J. Bacteriol. , vol.144 , pp. 1208-1211
    • Hall, B.G.1    Zuzel, T.2
  • 19
    • 0029962946 scopus 로고    scopus 로고
    • Amino acid sequence determinants of β-lactamase structure and activity
    • HUANG, W., J. PETROSINO, M. SIRSCH, P. S. SHENKIN, and T. PALZKILL. 1996. Amino acid sequence determinants of β-lactamase structure and activity. J. Mol. Biol. 258:688-703.
    • (1996) J. Mol. Biol. , vol.258 , pp. 688-703
    • Huang, W.1    Petrosino, J.2    Sirsch, M.3    Shenkin, P.S.4    Palzkill, T.5
  • 20
    • 0028178377 scopus 로고
    • Three-dimensional structure of beta-galactosidase from E. coli
    • JACOBSON, R. H., X. J. ZHANG, R. F. DUBOSE, and B. W. MATTHEWS. 1994. Three-dimensional structure of beta-galactosidase from E. coli. Nature 369:761-766.
    • (1994) Nature , vol.369 , pp. 761-766
    • Jacobson, R.H.1    Zhang, X.J.2    Dubose, R.F.3    Matthews, B.W.4
  • 22
    • 0019206723 scopus 로고
    • A mutant ebg enzyme that converts lactose into an inducer of the lac operon
    • ROLSETH, S. J., V. A. FRIED, and B. G. HALL. 1980. A mutant ebg enzyme that converts lactose into an inducer of the lac operon. J. Bacteriol. 142:1036-1039.
    • (1980) J. Bacteriol. , vol.142 , pp. 1036-1039
    • Rolseth, S.J.1    Fried, V.A.2    Hall, B.G.3
  • 23
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructring phylogenetic trees
    • SAITOU, N., and M. NEI. 1987. The neighbor-joining method: a new method for reconstructring phylogenetic trees. Mol. Biol. Evol. 4:406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 24
    • 0029617829 scopus 로고
    • abcd, a "second generation" evolvant containing two supposedly "kinetically silent" mutations
    • abcd, a "second generation" evolvant containing two supposedly "kinetically silent" mutations. Biochem. J. 312:971-977.
    • (1995) Biochem. J. , vol.312 , pp. 971-977
    • Srinivasan, K.1    Hall, B.G.2    Sinnott, M.L.3
  • 25
    • 0027406564 scopus 로고
    • Large changes of transition state structure during experimental evolution of an enzyme
    • SRINIVASAN, K., A. KONSTANTINDIS, M. L. SINNOTT, and B. G. HALL. 1993. Large changes of transition state structure during experimental evolution of an enzyme. Biochem. J. 291:15-17.
    • (1993) Biochem. J. , vol.291 , pp. 15-17
    • Srinivasan, K.1    Konstantindis, A.2    Sinnott, M.L.3    Hall, B.G.4
  • 27
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice
    • THOMPSON, J. D., D. G. HIGGINS, and T. J. GIBSON. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.