메뉴 건너뛰기




Volumn 4, Issue , 2004, Pages 1-12

The single-stranded DNA-binding protein of Deinococcus radiodurans

Author keywords

[No Author keywords available]

Indexed keywords

CELL EXTRACT; CIRCULAR DNA; DIMER; DNA FRAGMENT; DOUBLE STRANDED DNA; GUANINE NUCLEOTIDE; MONOMER; OLIGOMER; OLIGONUCLEOTIDE; OLIGOSACCHARIDE; RECA PROTEIN; SINGLE STRANDED DNA BINDING PROTEIN; TETRAMER; DNA BINDING PROTEIN;

EID: 2942642109     PISSN: 14712180     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-4-2     Document Type: Article
Times cited : (74)

References (32)
  • 1
    • 0030755081 scopus 로고    scopus 로고
    • Against all odds - The survival strategies of deinococcus radiodurans
    • Battista JR: Against all odds - the survival strategies of deinococcus radiodurans. Annu Rev Microbiol 1997, 51:203-224.
    • (1997) Annu Rev Microbiol , vol.51 , pp. 203-224
    • Battista, J.R.1
  • 2
    • 0035102449 scopus 로고    scopus 로고
    • Genome of the extremely radiation-resistant bacterium Deinococcus radiodurans viewed from the perspective of comparative genomics
    • Makarova KS, Aravind L, Wolf YI, Tatusov RL, Minton KW, Koonin EV, Daly MJ: Genome of the extremely radiation-resistant bacterium Deinococcus radiodurans viewed from the perspective of comparative genomics. Microbiol Mol Biol Rev 2001, 65:44-79.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 44-79
    • Makarova, K.S.1    Aravind, L.2    Wolf, Y.I.3    Tatusov, R.L.4    Minton, K.W.5    Koonin, E.V.6    Daly, M.J.7
  • 3
    • 0028246888 scopus 로고
    • Escherichia coli single-stranded DNA-binding protein: Multiple DNA-binding modes and cooperativities
    • Lohman TM, Ferrari ME: Escherichia coli single-stranded DNA-binding protein: multiple DNA-binding modes and cooperativities. Annu Rev Biochemistry 1994, 63:527-570.
    • (1994) Annu Rev Biochemistry , vol.63 , pp. 527-570
    • Lohman, T.M.1    Ferrari, M.E.2
  • 7
    • 0036772213 scopus 로고    scopus 로고
    • Identification and characterization of single-stranded-DNA-binding proteins from Thermus thermophilus and Thermus aquaticus - New arrangement of binding domains
    • Dabrowski S, Olszewski M, Piatek R, Brillowska-Dabrowska A, Konopa G, Kur J: Identification and characterization of single-stranded-DNA-binding proteins from Thermus thermophilus and Thermus aquaticus - new arrangement of binding domains. Microbiology 2002, 148:3307-3315.
    • (2002) Microbiology , vol.148 , pp. 3307-3315
    • Dabrowski, S.1    Olszewski, M.2    Piatek, R.3    Brillowska-Dabrowska, A.4    Konopa, G.5    Kur, J.6
  • 8
    • 0036786891 scopus 로고    scopus 로고
    • Correlations between Shine-Dalgarno sequences and gene features such as predicted expression levels and operon structures
    • Ma J, Campbell A, Karlin S: Correlations between Shine-Dalgarno sequences and gene features such as predicted expression levels and operon structures. J Bacteriol 2002, 184:5733-5745.
    • (2002) J Bacteriol , vol.184 , pp. 5733-5745
    • Ma, J.1    Campbell, A.2    Karlin, S.3
  • 9
    • 0033831650 scopus 로고    scopus 로고
    • Characterization of the minimal replicon of a cryptic Deinococcus radiodurans SARK plasmid and development of versatile Escherichia coli-D.radiodurans shuttle vectors
    • Meima R, Lidstrom ME: Characterization of the minimal replicon of a cryptic Deinococcus radiodurans SARK plasmid and development of versatile Escherichia coli-D.radiodurans shuttle vectors. Appl Environ Microbiol 2000, 66:3856-3867.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 3856-3867
    • Meima, R.1    Lidstrom, M.E.2
  • 10
    • 0035035866 scopus 로고    scopus 로고
    • Promoter cloning in the radioresistant bacterium Deinococcus radiodurans
    • Meima R, Rothfuss HM, Gewin L, Lidstrom ME: Promoter cloning in the radioresistant bacterium Deinococcus radiodurans. J Bacteriol 2001, 183:3169-3175.
    • (2001) J Bacteriol , vol.183 , pp. 3169-3175
    • Meima, R.1    Rothfuss, H.M.2    Gewin, L.3    Lidstrom, M.E.4
  • 11
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin AG:OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J 1993, 12:861-867.
    • (1993) EMBO J , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 12
    • 0344541947 scopus 로고    scopus 로고
    • Novel homologs of replication protein A in archaea: Implications for the evolution of ssDNA-binding proteins
    • Chedin F, Seitz EM, Kowalczykowski SC: Novel homologs of replication protein A in archaea: implications for the evolution of ssDNA-binding proteins. Trends Biochem Sci 1998, 23:273-277.
    • (1998) Trends Biochem Sci , vol.23 , pp. 273-277
    • Chedin, F.1    Seitz, E.M.2    Kowalczykowski, S.C.3
  • 13
    • 0016609346 scopus 로고
    • The deoxyribonucleic acid unwinding protein of Escherichia coli. Properties and functions in replication
    • Weiner JH, Bertsch LL, Kornberg A: The deoxyribonucleic acid unwinding protein of Escherichia coli. Properties and functions in replication. J Biol Chem 1975, 250:1972-1980.
    • (1975) J Biol Chem , vol.250 , pp. 1972-1980
    • Weiner, J.H.1    Bertsch, L.L.2    Kornberg, A.3
  • 15
    • 0030014904 scopus 로고    scopus 로고
    • In vitro and in vivo function of the C-terminus of Escherichia coli single-stranded DNA binding protein
    • Curth U, Genschel J, Urbanke C, Greipel J: In vitro and in vivo function of the C-terminus of Escherichia coli single-stranded DNA binding protein. Nucleic Acids Res 1996, 24:2706-2711.
    • (1996) Nucleic Acids Res , vol.24 , pp. 2706-2711
    • Curth, U.1    Genschel, J.2    Urbanke, C.3    Greipel, J.4
  • 16
    • 0034092927 scopus 로고    scopus 로고
    • Roles of functional loops and the C-terminal segment of a single-stranded DNA binding protein elucidated by x-ray structure analysis
    • Matsumoto T, Morimoto Y, Shibata N, Kinebuchi T, Shimamoto N, Tsukihara T, Yasuoka N: Roles of functional loops and the C-terminal segment of a single-stranded DNA binding protein elucidated by x-ray structure analysis. J Biochem 2000, 127:329-335.
    • (2000) J Biochem , vol.127 , pp. 329-335
    • Matsumoto, T.1    Morimoto, Y.2    Shibata, N.3    Kinebuchi, T.4    Shimamoto, N.5    Tsukihara, T.6    Yasuoka, N.7
  • 17
    • 0023135142 scopus 로고
    • Effects of Escherichia coli SSB protein on the single-stranded DNA-dependent ATPase activity of Escherichia coli RecA protein. Evidence that SSB protein facilitates the binding of RecA protein to regions of secondary structure within single-stranded DNA
    • Kowalczykowski SC, Krupp RA: Effects of Escherichia coli SSB protein on the single-stranded DNA-dependent ATPase activity ofEscherichia coli RecA protein. Evidence that SSB protein facilitates the binding of RecA protein to regions of secondary structure within single-stranded DNA. J Mol Biol 1987, 193:97-113.
    • (1987) J Mol Biol , vol.193 , pp. 97-113
    • Kowalczykowski, S.C.1    Krupp, R.A.2
  • 18
    • 0026795611 scopus 로고
    • A postsynaptic role for single-stranded DNA-binding protein in recA protein-promoted DNA strand exchange
    • Lavery PE, Kowalczykowski SC: A postsynaptic role for single-stranded DNA-binding protein in recA protein-promoted DNA strand exchange. J Biol Chem 1992, 267:9315-9320.
    • (1992) J Biol Chem , vol.267 , pp. 9315-9320
    • Lavery, P.E.1    Kowalczykowski, S.C.2
  • 19
    • 0038470002 scopus 로고    scopus 로고
    • Characterization of DNA strand transfer promoted by Mycobacterium smegmatis RecA reveals functional diversity with Mycobacterium tuberculosis RecA
    • Ganesh N, Muniyappa K: Characterization of DNA strand transfer promoted by Mycobacterium smegmatis RecA reveals functional diversity with Mycobacterium tuberculosis RecA. Biochemistry 2003, 42:7216-7225.
    • (2003) Biochemistry , vol.42 , pp. 7216-7225
    • Ganesh, N.1    Muniyappa, K.2
  • 20
    • 0026701665 scopus 로고
    • Characterization of DNA-binding and strand-exchange stimulation properties of y-RPA, a yeast single-strand-DNA-binding protein
    • Alani E, Thresher R, Griffith JD, Kolodner RD: Characterization of DNA-binding and strand-exchange stimulation properties of y-RPA, a yeast single-strand-DNA-binding protein. J Mol Biol 1992, 227:54-71.
    • (1992) J Mol Biol , vol.227 , pp. 54-71
    • Alani, E.1    Thresher, R.2    Griffith, J.D.3    Kolodner, R.D.4
  • 21
    • 0034635469 scopus 로고    scopus 로고
    • Rad51 uses one mechanism to drive DNA strand exchange in both directions
    • Namsaraev EA, Berg P: Rad51 uses one mechanism to drive DNA strand exchange in both directions. J Biol Chem 2000, 275:3970-3976.
    • (2000) J Biol Chem , vol.275 , pp. 3970-3976
    • Namsaraev, E.A.1    Berg, P.2
  • 23
    • 0024328156 scopus 로고
    • Large-scale purification and characterization of the Escherichia coli rep gene product
    • Lohman TM, Chao K, Green JM, Sage S, Runyon GT: Large-scale purification and characterization of the Escherichia coli rep gene product. J Biol Chem 1989, 264:10139-10147.
    • (1989) J Biol Chem , vol.264 , pp. 10139-10147
    • Lohman, T.M.1    Chao, K.2    Green, J.M.3    Sage, S.4    Runyon, G.T.5
  • 24
    • 0029154926 scopus 로고
    • RuvB protein-mediated ATP hydrolysis: Functional asymmetry in the RuvB hexamer
    • Marrione PE, Cox MM: RuvB protein-mediated ATP hydrolysis: functional asymmetry in the RuvB hexamer. Biochemistry 1995, 34:9809-9818.
    • (1995) Biochemistry , vol.34 , pp. 9809-9818
    • Marrione, P.E.1    Cox, M.M.2
  • 25
    • 0029961677 scopus 로고    scopus 로고
    • DNA strand exchange promoted by RecA K72R. Two reaction phases with different Mg2+ requirements
    • Shan Q, Cox MM, Inman RB: DNA strand exchange promoted by RecA K72R. Two reaction phases with different Mg2+ requirements. J Biol Chem 1996, 271:5712-5724.
    • (1996) J Biol Chem , vol.271 , pp. 5712-5724
    • Shan, Q.1    Cox, M.M.2    Inman, R.B.3
  • 27
    • 0019840804 scopus 로고
    • Function of nucleoside triphosphate and polynucleotide in Escherichia coli recA protein-directed cleavage of phage lambda repressor
    • Craig NL, Roberts JW: Function of nucleoside triphosphate and polynucleotide in Escherichia coli recA protein-directed cleavage of phage lambda repressor. J Biol Chem 1981, 256:8039-8044.
    • (1981) J Biol Chem , vol.256 , pp. 8039-8044
    • Craig, N.L.1    Roberts, J.W.2
  • 28
    • 0021920551 scopus 로고
    • Two binding modes in Escherichia coli single strand binding protein-single stranded DNA complexes. Modulation by NaCl concentration
    • Lohman TM, Overman LB: Two binding modes in Escherichia coli single strand binding protein-single stranded DNA complexes. Modulation by NaCl concentration. J Biol Chem 1985, 260:3594-3603.
    • (1985) J Biol Chem , vol.260 , pp. 3594-3603
    • Lohman, T.M.1    Overman, L.B.2
  • 29
    • 0020645043 scopus 로고
    • New M13 vectors for cloning
    • Messing J: New M13 vectors for cloning. Methods Enzymol 1983, 101:20-78.
    • (1983) Methods Enzymol , vol.101 , pp. 20-78
    • Messing, J.1
  • 30
    • 0022973594 scopus 로고
    • Exchange of RecA protein between adjacent RecA protein-single-stranded DNA complexes
    • Neuendorf SK, Cox MM: Exchange of RecA protein between adjacent RecA protein-single-stranded DNA complexes. J Biol Chem 1986, 261:8276-8282.
    • (1986) J Biol Chem , vol.261 , pp. 8276-8282
    • Neuendorf, S.K.1    Cox, M.M.2
  • 31
    • 0347362796 scopus 로고    scopus 로고
    • A DNA pairing-enhanced conformation of bacterial RecA proteins
    • JBC papers in press - M308563200
    • Haruta N, Yu X, Yang S, Egelman EH, Cox MM: A DNA pairing-enhanced conformation of bacterial RecA proteins. J Biol Chem 2003, 278:52710-52723. (JBC papers in press - M308563200)
    • (2003) J Biol Chem , vol.278 , pp. 52710-52723
    • Haruta, N.1    Yu, X.2    Yang, S.3    Egelman, E.H.4    Cox, M.M.5
  • 32
    • 0031009811 scopus 로고    scopus 로고
    • Crystal structure of the homotetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-A resolution
    • Raghunathan S, Ricard CS, Lohman TM, Waksman G: Crystal structure of the homotetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-A resolution. Proc Natl Acad Sci U S A 1997, 94:6652-6657.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 6652-6657
    • Raghunathan, S.1    Ricard, C.S.2    Lohman, T.M.3    Waksman, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.