메뉴 건너뛰기




Volumn 34, Issue 5, 2006, Pages 1588-1596

Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; BACTERIAL ENZYME; PROTEIN TYROSINE KINASE; SINGLE STRANDED DNA BINDING PROTEIN; BACTERIAL PROTEIN; DNA BINDING PROTEIN; ESCHERICHIA COLI PROTEIN; PROTEIN TYROSINE PHOSPHATASE; SINGLE STRANDED DNA; TYROSINE;

EID: 33645466839     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkj514     Document Type: Article
Times cited : (118)

References (54)
  • 2
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker,J.E., Saraste,M., Runswick,M.J. and Gay,N.J. (1982) Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J., 1, 945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 3
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks,S.K., Quinn,A.M. and Hunter,T. (1988) The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science, 241, 42-52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 4
    • 0034020990 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of CpsD negatively regulates capsular polysaccharide biosynthesis in Streptococcus pneumoniae
    • Morona,J.K., Paton,J.C., Miller,D.C. and Morona,R. (2000) Tyrosine phosphorylation of CpsD negatively regulates capsular polysaccharide biosynthesis in Streptococcus pneumoniae. Mol. Microbiol., 35, 431-1442.
    • (2000) Mol. Microbiol. , vol.35 , pp. 431-1442
    • Morona, J.K.1    Paton, J.C.2    Miller, D.C.3    Morona, R.4
  • 5
    • 0034405696 scopus 로고    scopus 로고
    • Relationship between exopolysaccharide production and protein-tyrosine phosphorylation in gram-negative bacteria
    • Vincent,C., Duclos,B., Grangeasse,C., Vaganay,E., Riberty,M., Cozzone,A.J. and Doublet,P. (2000) Relationship between exopolysaccharide production and protein-tyrosine phosphorylation in gram-negative bacteria. J. Mol. Biol., 304, 311-321.
    • (2000) J. Mol. Biol. , vol.304 , pp. 311-321
    • Vincent, C.1    Duclos, B.2    Grangeasse, C.3    Vaganay, E.4    Riberty, M.5    Cozzone, A.J.6    Doublet, P.7
  • 6
    • 0035951884 scopus 로고    scopus 로고
    • Phosphorylation of Wzc, a tyrosine autokinase, is essential for assembly of group 1 capsular polysaccharides in Escherichia coli
    • Wugeditsch,T., Paiment,A., Hocking,J., Drummelsmith,J., Forrester,C. and Whitfield,C. (2001) Phosphorylation of Wzc, a tyrosine autokinase, is essential for assembly of group 1 capsular polysaccharides in Escherichia coli. J. Biol. Chem., 276, 2361-2371.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2361-2371
    • Wugeditsch, T.1    Paiment, A.2    Hocking, J.3    Drummelsmith, J.4    Forrester, C.5    Whitfield, C.6
  • 7
    • 0036889026 scopus 로고    scopus 로고
    • Impact of phosphorylation of specific residues in the tyrosine autokinase, Wzc, on its activity in assembly of group 1 capsules in Escherichia coli
    • Paiment,A., Hocking,J. and Whitfield,C. (2002) Impact of phosphorylation of specific residues in the tyrosine autokinase, Wzc, on its activity in assembly of group 1 capsules in Escherichia coli. J. Bacteriol., 184, 6437-6447.
    • (2002) J. Bacteriol. , vol.184 , pp. 6437-6447
    • Paiment, A.1    Hocking, J.2    Whitfield, C.3
  • 8
    • 0036510550 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of protein kinase Wzc from Escherichia coli K12 occurs through a two-step process
    • Grangeasse,C., Doublet,P. and Cozzone,A.J. (2002) Tyrosine phosphorylation of protein kinase Wzc from Escherichia coli K12 occurs through a two-step process. J. Biol. Chem., 277, 7127-7135.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7127-7135
    • Grangeasse, C.1    Doublet, P.2    Cozzone, A.J.3
  • 10
    • 0141574316 scopus 로고    scopus 로고
    • Autophosphorylation of the Escherichia coli protein kinase Wzc regulates tyrosine phosphorylation of Ugd, a UDP-glucose dehydrogenase
    • Grangeasse,C., Obadia,B., Mijakovic,I., Deutscher,J., Cozzone,A.J. and Doublet,P. (2003) Autophosphorylation of the Escherichia coli protein kinase Wzc regulates tyrosine phosphorylation of Ugd, a UDP-glucose dehydrogenase. J. Biol. Chem., 278, 39323-39329.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39323-39329
    • Grangeasse, C.1    Obadia, B.2    Mijakovic, I.3    Deutscher, J.4    Cozzone, A.J.5    Doublet, P.6
  • 11
    • 0037384743 scopus 로고    scopus 로고
    • Phosphorylation-mediated regulation of heat shock response in Escherichia coli
    • Klein,G., Dartigalongue,C. and Raina,S. (2003) Phosphorylation-mediated regulation of heat shock response in Escherichia coli. Mol. Microbiol., 48, 269-285.
    • (2003) Mol. Microbiol. , vol.48 , pp. 269-285
    • Klein, G.1    Dartigalongue, C.2    Raina, S.3
  • 13
    • 0030009174 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in Myxococcus xanthus, a multicellular prokaryote
    • Frasch,S.C. and Dworkin,M. (1996) Tyrosine phosphorylation in Myxococcus xanthus, a multicellular prokaryote. J. Bacteriol., 178, 4084-4088.
    • (1996) J. Bacteriol. , vol.178 , pp. 4084-4088
    • Frasch, S.C.1    Dworkin, M.2
  • 14
    • 0018407415 scopus 로고
    • An Escherichia coli mutant defective in single-strand binding protein is defective in DNA replication
    • Meyer,R.R., Glassberg,J. and Kornberg,A. (1979) An Escherichia coli mutant defective in single-strand binding protein is defective in DNA replication. Proc. Natl Acad. Sci. USA, 76, 1702-1705.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 1702-1705
    • Meyer, R.R.1    Glassberg, J.2    Kornberg, A.3
  • 15
    • 0028072045 scopus 로고
    • Replication factor A is required in vivo for DNA replication, repair, and recombination
    • Longhese,M.P.,Plevani,P. and Lucchini,G. (1994) Replication factor A is required in vivo for DNA replication, repair, and recombination. Mol. Cell. Biol., 14, 7884-7890.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7884-7890
    • Longhese, M.P.1    Plevani, P.2    Lucchini, G.3
  • 16
    • 0018686338 scopus 로고
    • Mutant single-strand binding protein of Escherichia coli: Genetic and physiological characterization
    • Glassberg,J., Meyer,R.R. and Kornberg,A. (1979) Mutant single-strand binding protein of Escherichia coli: Genetic and physiological characterization. J. Bacteriol., 140, 14-19.
    • (1979) J. Bacteriol. , vol.140 , pp. 14-19
    • Glassberg, J.1    Meyer, R.R.2    Kornberg, A.3
  • 17
    • 0028838087 scopus 로고
    • A novel allele of Saccharomyces cerevisiae RFA1 that is deficient in recombination and repair and suppressible by RAD52
    • Firmenich,A.A., Elias-Arnanz,M. and Berg,P. (1995) A novel allele of Saccharomyces cerevisiae RFA1 that is deficient in recombination and repair and suppressible by RAD52. Mol. Cell. Biol., 15, 1620-1631.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1620-1631
    • Firmenich, A.A.1    Elias-Arnanz, M.2    Berg, P.3
  • 18
    • 0024396565 scopus 로고
    • DNA mismatch correction in a defined system
    • Lahue,R.S., Au,K.G. and Modrich,P. (1989) DNA mismatch correction in a defined system. Science, 245, 160-164.
    • (1989) Science , vol.245 , pp. 160-164
    • Lahue, R.S.1    Au, K.G.2    Modrich, P.3
  • 19
    • 0032522760 scopus 로고    scopus 로고
    • Devoted to the lagging strand-the subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly
    • Kelman,Z., Yuzhakov,A., Andjelkovic,J. and O'Donnell,M. (1998) Devoted to the lagging strand-the subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly. EMBO J., 17, 2436-2449.
    • (1998) EMBO J. , vol.17 , pp. 2436-2449
    • Kelman, Z.1    Yuzhakov, A.2    Andjelkovic, J.3    O'Donnell, M.4
  • 20
    • 2342516683 scopus 로고    scopus 로고
    • Physical and functional interaction of the archaeal single-stranded DNA-binding protein SSB with RNA polymerase
    • Richard,D.J., Bell,S.D. and White,M.F. (2004) Physical and functional interaction of the archaeal single-stranded DNA-binding protein SSB with RNA polymerase. Nucleic Acids Res., 32, 1065-1074.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1065-1074
    • Richard, D.J.1    Bell, S.D.2    White, M.F.3
  • 21
    • 0036639412 scopus 로고    scopus 로고
    • Modulation of enzymatic activities of Escherichia coli DnaB helicase by single-stranded DNA-binding proteins
    • Biswas,E.E., Chen,P.H. and Biswas,S.B. (2002) Modulation of enzymatic activities of Escherichia coli DnaB helicase by single-stranded DNA-binding proteins. Nucleic Acids Res., 30, 2809-2816.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2809-2816
    • Biswas, E.E.1    Chen, P.H.2    Biswas, S.B.3
  • 22
    • 0025365192 scopus 로고
    • Cell-cycle-regulated phosphorylation of DNA replication factor A from human and yeast cells
    • Din,S., Brill,S.J., Fairman,M.P. and Stillman,B. (1990) Cell-cycle-regulated phosphorylation of DNA replication factor A from human and yeast cells. Genes Dev., 4, 968-977.
    • (1990) Genes Dev. , vol.4 , pp. 968-977
    • Din, S.1    Brill, S.J.2    Fairman, M.P.3    Stillman, B.4
  • 24
    • 0026539144 scopus 로고
    • cdc2 family kinases phosphorylate a human cell DNA replication factor, RPA, and activate DNA replication
    • Dutta,A. and Stillman,B. (1992) cdc2 family kinases phosphorylate a human cell DNA replication factor, RPA, and activate DNA replication. EMBO J., 11, 2189-2199.
    • (1992) EMBO J. , vol.11 , pp. 2189-2199
    • Dutta, A.1    Stillman, B.2
  • 25
    • 0028016304 scopus 로고
    • Phosphorylation of the p34 subunit of human single-stranded-DNA-binding protein in cyclin A-activated G1 extracts is catalyzed by cdk-cyclin A complex and DNA-dependent protein kinase
    • Pan,Z.-Q., Amin,A.A., Gibbs,E., Niu,H. and Hurwitz,J. (1994) Phosphorylation of the p34 subunit of human single-stranded-DNA-binding protein in cyclin A-activated G1 extracts is catalyzed by cdk-cyclin A complex and DNA-dependent protein kinase. Proc. Natl Acad. Sci. USA, 91, 8343-8347.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8343-8347
    • Pan, Z.-Q.1    Amin, A.A.2    Gibbs, E.3    Niu, H.4    Hurwitz, J.5
  • 26
    • 0027177654 scopus 로고
    • DNA unwinding by replication protein A is a property of the 70 kDa subunit and is facilitated by phosphorylation of the 32 kDa subunit
    • Georgaki,A. and Hübscher,U. (1993) DNA unwinding by replication protein A is a property of the 70 kDa subunit and is facilitated by phosphorylation of the 32 kDa subunit. Nucleic Acids Res., 21, 3659-3665.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3659-3665
    • Georgaki, A.1    Hübscher, U.2
  • 27
    • 0027941616 scopus 로고
    • Replication protein A mutants lacking phosphorylation sites for p34cdc2 kinase support DNA replication
    • Henricksen,L.A. and Wold,M.S. (1994) Replication protein A mutants lacking phosphorylation sites for p34cdc2 kinase support DNA replication. J. Biol. Chem., 269, 24203-24208.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24203-24208
    • Henricksen, L.A.1    Wold, M.S.2
  • 28
    • 0029074504 scopus 로고
    • Phosphorylated and unphosphorylated forms of human single-stranded DNA-binding protein are equally active in simian virus 40 DNA replication and in nucleotide excision repair
    • Pan,Z.-Q., Park,C.-H., Amin,A.A., Hurwitz,J. and Sancar,A. (1995) Phosphorylated and unphosphorylated forms of human single-stranded DNA-binding protein are equally active in simian virus 40 DNA replication and in nucleotide excision repair. Proc. Natl Acad. Sci. USA, 92, 4636-4640.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 4636-4640
    • Pan, Z.-Q.1    Park, C.-H.2    Amin, A.A.3    Hurwitz, J.4    Sancar, A.5
  • 29
    • 1342325347 scopus 로고    scopus 로고
    • Replication protein A (RPA) phosphorylation prevents RPA association with replication centers
    • Vassin,V.M., Wold,M.S. and Borowiec,J.A. (2004) Replication protein A (RPA) phosphorylation prevents RPA association with replication centers. Mol. Cell. Biol., 24, 1930-1943.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1930-1943
    • Vassin, V.M.1    Wold, M.S.2    Borowiec, J.A.3
  • 30
    • 0028355488 scopus 로고
    • UV light-induced DNA synthesis arrest in HeLa cells is associated with changes in phosphorylation of human single-stranded DNA-binding protein
    • Carty,M.P., Zernik-Kobak,M., McGrath,S. and Dixon,K. (1994) UV light-induced DNA synthesis arrest in HeLa cells is associated with changes in phosphorylation of human single-stranded DNA-binding protein. EMBO J., 13, 2114-2123.
    • (1994) EMBO J. , vol.13 , pp. 2114-2123
    • Carty, M.P.1    Zernik-Kobak, M.2    McGrath, S.3    Dixon, K.4
  • 31
    • 0033559531 scopus 로고    scopus 로고
    • Hyperphosphorylation of replication protein A middle subunit (RPA32) in apoptosis
    • Treuner,K., Okuyama,A., Knippers,R. and Fackelmayer,F.O. (1999) Hyperphosphorylation of replication protein A middle subunit (RPA32) in apoptosis. Nucleic Acids Res., 27, 1499-1504.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1499-1504
    • Treuner, K.1    Okuyama, A.2    Knippers, R.3    Fackelmayer, F.O.4
  • 32
    • 34147224324 scopus 로고
    • The single-stranded DNA-binding protein of Escherichia coli
    • Meyer,R.R. and Laine,P.S. (1990) The single-stranded DNA-binding protein of Escherichia coli. Microbiol. Rev., 54, 342-380.
    • (1990) Microbiol. Rev. , vol.54 , pp. 342-380
    • Meyer, R.R.1    Laine, P.S.2
  • 33
    • 0028246888 scopus 로고
    • Escherichia coli single-stranded DNA-binding protein: Multiple DNA-binding modes and cooperativities
    • Lohman,T.M. and Ferrari,M.E. (1994) Escherichia coli single-stranded DNA-binding protein: Multiple DNA-binding modes and cooperativities. Annu. Rev. Biochem., 63, 527-570.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 527-570
    • Lohman, T.M.1    Ferrari, M.E.2
  • 35
    • 0020580529 scopus 로고
    • Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins
    • Williams,K.R., Spicer,E.K., LoPresti,M.B., Guggenheimer,R.A. and Chase,J.W. (1983) Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins. J. Biol. Chem., 258, 3346-3355.
    • (1983) J. Biol. Chem. , vol.258 , pp. 3346-3355
    • Williams, K.R.1    Spicer, E.K.2    LoPresti, M.B.3    Guggenheimer, R.A.4    Chase, J.W.5
  • 36
    • 0035907374 scopus 로고    scopus 로고
    • Chimeras between single-stranded DNA-binding proteins from Escherichia coli and Mycobacterium tuberculosis reveal that their C-terminal domains interact with uracil DNA glycosylases
    • Handa,P., Acharya,N. and Varshney,U. (2001) Chimeras between single-stranded DNA-binding proteins from Escherichia coli and Mycobacterium tuberculosis reveal that their C-terminal domains interact with uracil DNA glycosylases. J. Biol. Chem., 276, 16992-16997.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16992-16997
    • Handa, P.1    Acharya, N.2    Varshney, U.3
  • 37
    • 1142298583 scopus 로고    scopus 로고
    • Differential expression of two paralogous genes of Bacillus subtilis encoding single-stranded DNA binding protein
    • Lindner,C., Nijland,R., van Hartskamp,M., Bron,S., Hamoen,L.W. and Kuipers,O.P. (2004) Differential expression of two paralogous genes of Bacillus subtilis encoding single-stranded DNA binding protein. J. Bacteriol., 186, 1097-1105.
    • (2004) J. Bacteriol. , vol.186 , pp. 1097-1105
    • Lindner, C.1    Nijland, R.2    van Hartskamp, M.3    Bron, S.4    Hamoen, L.W.5    Kuipers, O.P.6
  • 38
    • 0036250071 scopus 로고    scopus 로고
    • Modulation of gene expression made easy
    • Solem,C. and Jensen,P.R. (2002) Modulation of gene expression made easy. Appl. Environ. Microbiol., 68, 2397-2403.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 2397-2403
    • Solem, C.1    Jensen, P.R.2
  • 39
    • 0042890402 scopus 로고    scopus 로고
    • Definition of a second Bacillus subtilis pur regulon comprising the pur and xpt-pbuX operons plus pbuG, nupG (yxjA), and pbuE (ydhL)
    • Johansen,L.E., Nygaard,P., Lassen,C., Agersø,Y. and Saxild,H.H. (2003) Definition of a second Bacillus subtilis pur regulon comprising the pur and xpt-pbuX operons plus pbuG, nupG (yxjA), and pbuE (ydhL). J. Bacteriol., 185, 5200-5209.
    • (2003) J. Bacteriol. , vol.185 , pp. 5200-5209
    • Johansen, L.E.1    Nygaard, P.2    Lassen, C.3    Agersø, Y.4    Saxild, H.H.5
  • 40
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagnostopoulos,C. and Spizizen,J. (1961) Requirements for transformation in Bacillus subtilis. J. Bacteriol., 81, 741-746.
    • (1961) J. Bacteriol. , vol.81 , pp. 741-746
    • Anagnostopoulos, C.1    Spizizen, J.2
  • 41
    • 0031737309 scopus 로고    scopus 로고
    • A vector for systematic gene inactivation in Bacillus subtilis
    • Vagner,V., Dervyn,E. and Ehrlich,S.D. (1998) A vector for systematic gene inactivation in Bacillus subtilis. Microbiology, 144, 3097-3104.
    • (1998) Microbiology , vol.144 , pp. 3097-3104
    • Vagner, V.1    Dervyn, E.2    Ehrlich, S.D.3
  • 42
    • 0015956559 scopus 로고
    • Formation and reversion of Streptomycete protoplasts: Cultural condition and morphological study
    • Okanishi,M., Suzuki,K. and Umezawa,H. (1974) Formation and reversion of Streptomycete protoplasts: Cultural condition and morphological study. J. Gen. Microbiol., 80, 389-400.
    • (1974) J. Gen. Microbiol. , vol.80 , pp. 389-400
    • Okanishi, M.1    Suzuki, K.2    Umezawa, H.3
  • 45
    • 0028798788 scopus 로고
    • Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL
    • Amrein,K.E., Takacs,B., Stieger,M., Molnos,J., Flint,N.A. and Burn,P. (1995) Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL. Proc. Natl Acad. Sci. USA, 92, 1048-1052.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1048-1052
    • Amrein, K.E.1    Takacs, B.2    Stieger, M.3    Molnos, J.4    Flint, N.A.5    Burn, P.6
  • 47
    • 3042815334 scopus 로고    scopus 로고
    • Trypsin cleaves exclusively C-terminal to arginine and lysine residues
    • Olsen,J.V., Ong,S.E. and Mann,M. (2004) Trypsin cleaves exclusively C-terminal to arginine and lysine residues. Mol. Cell Proteomics, 3, 608-614.
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 608-614
    • Olsen, J.V.1    Ong, S.E.2    Mann, M.3
  • 48
    • 0027459168 scopus 로고
    • Effects of protein kinase inhibitors on in vitro protein phosphorylation and cellular differentiation of Streptomyces griseus
    • Hong,S.K., Matsumoto,A., Horinouchi,S. and Beppu,T. (1993) Effects of protein kinase inhibitors on in vitro protein phosphorylation and cellular differentiation of Streptomyces griseus. Mol. Gen. Genet., 236, 347-354.
    • (1993) Mol. Gen. Genet. , vol.236 , pp. 347-354
    • Hong, S.K.1    Matsumoto, A.2    Horinouchi, S.3    Beppu, T.4
  • 49
    • 14544290034 scopus 로고    scopus 로고
    • High- and low- threshold genes in the Spo0A regulon of Bacillus subtilis
    • Fujita,M., Gonzalez-Pastor,J.E. and Losick,R. (2005) High- and low- threshold genes in the Spo0A regulon of Bacillus subtilis. J. Bacteriol., 187, 1357-1368.
    • (2005) J. Bacteriol. , vol.187 , pp. 1357-1368
    • Fujita, M.1    Gonzalez-Pastor, J.E.2    Losick, R.3
  • 50
    • 0035195997 scopus 로고    scopus 로고
    • Regulation of sporulation in Streptomyces coelicolor A3(2): A checkpoint multiplex?
    • Chater,K.F. (2001) Regulation of sporulation in Streptomyces coelicolor A3(2): A checkpoint multiplex? Curr. Opin. Microbiol., 4, 667-673.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 667-673
    • Chater, K.F.1
  • 51
    • 0041347886 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis single-stranded DNA-binding protein. Variability in quaternary structure and its implications
    • Saikrishnan,K., Jeyakanthan,J., Venkatesh,J., Acharya,N., Sekar,K., Varshney,U. and Vijayan,M. (2003) Structure of Mycobacterium tuberculosis single-stranded DNA-binding protein. Variability in quaternary structure and its implications. J. Mol. Biol., 331, 385-393.
    • (2003) J. Mol. Biol. , vol.331 , pp. 385-393
    • Saikrishnan, K.1    Jeyakanthan, J.2    Venkatesh, J.3    Acharya, N.4    Sekar, K.5    Varshney, U.6    Vijayan, M.7
  • 52
    • 0025905482 scopus 로고
    • An EPR study to determine the relative nucleic acid binding affinity of single-stranded DNA-binding protein from Escherichia coli
    • Bobst,E.V., Perrino,F.W., Meyer,R.R. and Bobst,A.M. (1991) An EPR study to determine the relative nucleic acid binding affinity of single-stranded DNA-binding protein from Escherichia coli. Biochim. Biophys. Acta, 1078, 199-207.
    • (1991) Biochim. Biophys. Acta , vol.1078 , pp. 199-207
    • Bobst, E.V.1    Perrino, F.W.2    Meyer, R.R.3    Bobst, A.M.4
  • 53
    • 0032715175 scopus 로고    scopus 로고
    • Recombinational repair of DNA damage in Escherichia coli and bacteriophage lambda
    • Kuzminov,A. (1999) Recombinational repair of DNA damage in Escherichia coli and bacteriophage lambda. Microbiol. Mol. Biol. Rev., 63, 751-813.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 751-813
    • Kuzminov, A.1
  • 54
    • 0037336269 scopus 로고    scopus 로고
    • High levels of intracellular cysteine promote oxidative DNA damage by driving the fenton reaction
    • Park,S. and Imlay,J.A. (2003) High levels of intracellular cysteine promote oxidative DNA damage by driving the fenton reaction. J. Bacteriol., 185, 1942-1950.
    • (2003) J. Bacteriol. , vol.185 , pp. 1942-1950
    • Park, S.1    Imlay, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.