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Volumn 285, Issue 1, 1999, Pages 73-83

Functional domains of an NAD+-dependent DNA ligase

Author keywords

DNA binding; DNA replication; Limited proteolysis; Protein DNA recognition; Zinc binding protein

Indexed keywords

DNA; NICOTINAMIDE ADENINE DINUCLEOTIDE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; THERMOLYSIN; ZINC ION;

EID: 0033534503     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2302     Document Type: Article
Times cited : (66)

References (31)
  • 1
    • 0019960536 scopus 로고
    • Cloning and amplified expression of the tryosyl-tRNA synthetase genes of Bacillus stearothermophilus andEscherichia coli
    • Baker D. G. Cloning and amplified expression of the tryosyl-tRNA synthetase genes of Bacillus stearothermophilus andEscherichia coli. Eur. J. Biochem. 125:1982;357-360.
    • (1982) Eur. J. Biochem. , vol.125 , pp. 357-360
    • Baker, D.G.1
  • 2
    • 0031046294 scopus 로고    scopus 로고
    • A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins
    • Bork P., Hofmann K., Bucher P., Neuwald A. F., Altschul S. F., Koonin E. V. A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins. FASEB J. 11:1997;68-76.
    • (1997) FASEB J. , vol.11 , pp. 68-76
    • Bork, P.1    Hofmann, K.2    Bucher, P.3    Neuwald, A.F.4    Altschul, S.F.5    Koonin, E.V.6
  • 3
    • 0027408354 scopus 로고
    • Covalent catalysis in nucleotidyl transfer. A KTDG motif is essential for enzyme-GMP complex formation by mRNA capping enzyme is conserved at the active sites of RNA and DNA ligases
    • Cong P., Shuman S. Covalent catalysis in nucleotidyl transfer. A KTDG motif is essential for enzyme-GMP complex formation by mRNA capping enzyme is conserved at the active sites of RNA and DNA ligases. J. Biol. Chem. 268:1993;7256-7260.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7256-7260
    • Cong, P.1    Shuman, S.2
  • 5
    • 0345602792 scopus 로고    scopus 로고
    • Functional domains of an ATP-dependent DNA ligase
    • Doherty A. J., Wigley D. B. Functional domains of an ATP-dependent DNA ligase. J. Mol. Biol. 1998.
    • (1998) J. Mol. Biol.
    • Doherty, A.J.1    Wigley, D.B.2
  • 6
    • 0029906410 scopus 로고    scopus 로고
    • Characterisation of the proteolytic fragments of bacteriophage T7 DNA ligase
    • Doherty A. J., Ashford S. R., Wigley D. B. Characterisation of the proteolytic fragments of bacteriophage T7 DNA ligase. Nucl. Acids Res. 24:1996;2281-2287.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 2281-2287
    • Doherty, A.J.1    Ashford, S.R.2    Wigley, D.B.3
  • 7
    • 77956919579 scopus 로고
    • DNA ligases
    • P. D. Boyer. New York: Academic Press
    • Engler M. J., Richardson C. C. DNA ligases. Boyer P. D. The Enzymes. 1982;3-29 Academic Press, New York.
    • (1982) The Enzymes , pp. 3-29
    • Engler, M.J.1    Richardson, C.C.2
  • 9
    • 0038228666 scopus 로고    scopus 로고
    • X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes
    • Håkansson K., Doherty A. J., Shuman S., Wigley D. B. X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes. Cell. 89:1997;545-553.
    • (1997) Cell , vol.89 , pp. 545-553
    • Håkansson, K.1    Doherty, A.J.2    Shuman, S.3    Wigley, D.B.4
  • 10
    • 0029032723 scopus 로고
    • Protein motifs 5: Zinc fingers
    • Klug A., Schwabe J. W. R. Protein motifs 5: Zinc fingers. FASEB J. 9:1995;597-604.
    • (1995) FASEB J. , vol.9 , pp. 597-604
    • Klug, A.1    Schwabe, J.W.R.2
  • 11
    • 0026059034 scopus 로고
    • In vitro mutagenesis and functional expression in Escherichia coli of a cDNA encoding the catalytic domain of human DNA ligase I
    • Kodama K., Barnes D. E., Lindahl T. In vitro mutagenesis and functional expression in Escherichia coli of a cDNA encoding the catalytic domain of human DNA ligase I. Nucl. Acids Res. 19:1991;6093-6099.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 6093-6099
    • Kodama, K.1    Barnes, D.E.2    Lindahl, T.3
  • 12
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel T. A., Roberts J. D., Zakour R. A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:1987;367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of T4 bacteriophage
    • Laemmli U. K. Cleavage of structural proteins during assembly of the head of T4 bacteriophage. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0014151907 scopus 로고
    • Enzymatic joining of DNA strands, II. An enzyme-adenylate intermediate in the DPN-dependent DNA ligase reaction
    • Little J. W., Zimmerman S. B., Oshinsky C. K., Gellert M. Enzymatic joining of DNA strands, II. An enzyme-adenylate intermediate in the DPN-dependent DNA ligase reaction. Proc. Natl Acad. Sci. USA. 58:1967;2004-2011.
    • (1967) Proc. Natl Acad. Sci. USA , vol.58 , pp. 2004-2011
    • Little, J.W.1    Zimmerman, S.B.2    Oshinsky, C.K.3    Gellert, M.4
  • 16
    • 0029744212 scopus 로고    scopus 로고
    • Identification of essential residues in Thermus thermophilus DNA ligase
    • Luo J., Barany F. Identification of essential residues in Thermus thermophilus DNA ligase. Nucl. Acids Res. 24:1996;3070-3085.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 3070-3085
    • Luo, J.1    Barany, F.2
  • 17
    • 0015857933 scopus 로고
    • Deoxyribonucleic acid ligase. A steady state kinetic analysis of the reaction catalysed by the enzyme fromEscherichia coli
    • Modrich P., Lehman I. R. Deoxyribonucleic acid ligase. A steady state kinetic analysis of the reaction catalysed by the enzyme fromEscherichia coli. J. Biol. Chem. 248:1973;7502-7511.
    • (1973) J. Biol. Chem. , vol.248 , pp. 7502-7511
    • Modrich, P.1    Lehman, I.R.2
  • 18
    • 0014084027 scopus 로고
    • Linkage of polynucleotides through phosphodiester bonds by an enzyme from Escherichia coli
    • Olivera B. M., Lehman I. R. Linkage of polynucleotides through phosphodiester bonds by an enzyme from Escherichia coli. Proc. Natl Acad. Sci. USA. 57:1967;1426-1433.
    • (1967) Proc. Natl Acad. Sci. USA , vol.57 , pp. 1426-1433
    • Olivera, B.M.1    Lehman, I.R.2
  • 19
    • 0017179326 scopus 로고
    • Modification of Escherichia coli DNA ligase by cleavage with trypsin
    • Panasenko S. M., Modrich P., Lehman I. R. Modification of Escherichia coli DNA ligase by cleavage with trypsin. J. Biol. Chem. 251:1976;3432-3435.
    • (1976) J. Biol. Chem. , vol.251 , pp. 3432-3435
    • Panasenko, S.M.1    Modrich, P.2    Lehman, I.R.3
  • 21
    • 0030755836 scopus 로고    scopus 로고
    • Domain structure of vaccinia DNA ligase
    • Sekiguchi J., Shuman S. Domain structure of vaccinia DNA ligase. Nucl. Acids Res. 25:1997;727-734.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 727-734
    • Sekiguchi, J.1    Shuman, S.2
  • 22
    • 0029152217 scopus 로고
    • Mutational analysis of Vaccinia DNA ligase defines residues essential for covalent catalysis
    • Shuman S., Ru X. Mutational analysis of Vaccinia DNA ligase defines residues essential for covalent catalysis. Virology. 211:1995;73-83.
    • (1995) Virology , vol.211 , pp. 73-83
    • Shuman, S.1    Ru, X.2
  • 23
    • 0029056990 scopus 로고
    • RNA capping enzyme and DNA ligase: A superfamily of covalent nucleotidyl transferases
    • Shuman S., Schwer B. RNA capping enzyme and DNA ligase: a superfamily of covalent nucleotidyl transferases. Mol. Microbiol. 17:1995;405-410.
    • (1995) Mol. Microbiol. , vol.17 , pp. 405-410
    • Shuman, S.1    Schwer, B.2
  • 24
    • 0032518177 scopus 로고    scopus 로고
    • Chlorella virus DNA ligase: Nick recognition and mutational analysis
    • Sriskanda V., Shuman S. Chlorella virus DNA ligase: nick recognition and mutational analysis. Nucl. Acids Res. 26:1998;525-531.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 525-531
    • Sriskanda, V.1    Shuman, S.2
  • 25
    • 0029938467 scopus 로고    scopus 로고
    • Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7
    • Subramanya H. S., Doherty A. J., Ashford S. R., Wigley D. B. Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7. Cell. 85:1996;607-615.
    • (1996) Cell , vol.85 , pp. 607-615
    • Subramanya, H.S.1    Doherty, A.J.2    Ashford, S.R.3    Wigley, D.B.4
  • 26
    • 0029096564 scopus 로고
    • Cloning and sequence analysis of the DNA ligase-encoding gene of Rhodothermus marinus, and overproduction, purification and characterization of two thermophilic DNA ligases
    • Thorbjarnardóttir S. H., Jonsson Z. O., Andresson O. S., Kristjansson J. K., Eggertsson G., Palsdottir A. Cloning and sequence analysis of the DNA ligase-encoding gene of Rhodothermus marinus, and overproduction, purification and characterization of two thermophilic DNA ligases. Gene. 161:1995;1-6.
    • (1995) Gene , vol.161 , pp. 1-6
    • Thorbjarnardóttir, S.H.1    Jonsson, Z.O.2    Andresson, O.S.3    Kristjansson, J.K.4    Eggertsson, G.5    Palsdottir, A.6
  • 27
    • 0031260117 scopus 로고    scopus 로고
    • Mammalian DNA ligases
    • Tomkinson A. E., Levin D. S. Mammalian DNA ligases. Bioessays. 19:1997;893-901.
    • (1997) Bioessays , vol.19 , pp. 893-901
    • Tomkinson, A.E.1    Levin, D.S.2
  • 28
    • 0026766091 scopus 로고
    • The N-end rule
    • Varshavsky A. The N-end rule. Cell. 69:1992;725-735.
    • (1992) Cell , vol.69 , pp. 725-735
    • Varshavsky, A.1
  • 29
    • 0026781934 scopus 로고
    • Analysis of the formation of AMP-DNA intermediate and the successive reaction by human DNA ligases I and II
    • Yang S., Chan J. Y. H. Analysis of the formation of AMP-DNA intermediate and the successive reaction by human DNA ligases I and II. J. Biol. Chem. 267:1992;8117-8122.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8117-8122
    • Yang, S.1    Chan, J.Y.H.2
  • 30
    • 0014670567 scopus 로고
    • Enzymatic joining of DNA strands. III Further purification of the deoxynucleic acid ligase fromEscherichia coli and multiple forms of the purified enzyme
    • Zimmerman S. B., Oshinsky C. K. Enzymatic joining of DNA strands. III Further purification of the deoxynucleic acid ligase fromEscherichia coli and multiple forms of the purified enzyme. J. Biol. Chem. 244:1969;4689-4695.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4689-4695
    • Zimmerman, S.B.1    Oshinsky, C.K.2
  • 31
    • 0014093442 scopus 로고
    • Enzymatic joining of DNA strands: A novel reaction of diphosphopyridine dinucleotide
    • Zimmerman S. B., Little J. W., Oshinsky C. K., Gellert M. Enzymatic joining of DNA strands: a novel reaction of diphosphopyridine dinucleotide. Proc. Natl Acad. Sci. USA. 57:1967;1841-1848.
    • (1967) Proc. Natl Acad. Sci. USA , vol.57 , pp. 1841-1848
    • Zimmerman, S.B.1    Little, J.W.2    Oshinsky, C.K.3    Gellert, M.4


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