메뉴 건너뛰기




Volumn 17, Issue 10, 2010, Pages 1189-1197

Both OB folds of single-stranded DNA-binding protein are essential for its ssDNA binding activity in deinococcus radiodurans

Author keywords

Deinococcus; DNA repair; OB fold; Single strand binding protein; Subfunctionalization

Indexed keywords

DNA BINDING PROTEIN; SINGLE STRANDED DNA;

EID: 77958462141     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986610792231438     Document Type: Article
Times cited : (5)

References (24)
  • 1
    • 0030049354 scopus 로고    scopus 로고
    • Radioresistance of Deinococcus radiodurans: Functions necessary to survive ionizing radiation are also necessary to survive prolonged desiccation
    • Mattimore, V.; Battista, J.R. Radioresistance of Deinococcus radiodurans: functions necessary to survive ionizing radiation are also necessary to survive prolonged desiccation. J. Bacteriol., 1996, 178(3), 633-637.
    • (1996) J. Bacteriol , vol.178 , Issue.3 , pp. 633-637
    • Mattimore, V.1    Battista, J.R.2
  • 2
    • 33845249111 scopus 로고    scopus 로고
    • Polar destabilization of DNA duplexes with single-stranded overhangs by the Deinococcus radiodurans SSB protein
    • Eggington, J.M.; Kozlov, A.G.; Cox, M.M.; Lohman, T.M. Polar destabilization of DNA duplexes with single-stranded overhangs by the Deinococcus radiodurans SSB protein. Biochemistry (Washington), 2006, 45(48), 14490-14502.
    • (2006) Biochemistry (Washington) , vol.45 , Issue.48 , pp. 14490-14502
    • Eggington, J.M.1    Kozlov, A.G.2    Cox, M.M.3    Lohman, T.M.4
  • 3
    • 70349280357 scopus 로고    scopus 로고
    • Recombinational DNA repair in a cellular context: A search for the homology search
    • Weiner, A.; Zauberman, N.; Minsky, A. Recombinational DNA repair in a cellular context: a search for the homology search. Nat. Rev. Microbiol., 2009, 7(10), 748-755.
    • (2009) Nat. Rev. Microbiol , vol.7 , Issue.10 , pp. 748-755
    • Weiner, A.1    Zauberman, N.2    Minsky, A.3
  • 4
    • 45849084662 scopus 로고    scopus 로고
    • Deinococcus radiodurans: What belongs to the survival kit
    • Blasius, M.; Sommer, S.; Hubscher, U. Deinococcus radiodurans: what belongs to the survival kit? Crit. Rev. Biochem. Mol. Biol., 2008, 43(3), 221-238.
    • (2008) Crit. Rev. Biochem. Mol. Biol , vol.43 , Issue.3 , pp. 221-238
    • Blasius, M.1    Sommer, S.2    Hubscher, U.3
  • 5
    • 0028246888 scopus 로고
    • Escherichia coli single-stranded DNA-binding protein: Multiple DNA-binding modes and cooperativities
    • Lohman, T.M.; Ferrari, M.E. Escherichia coli single-stranded DNA-binding protein: multiple DNA-binding modes and cooperativities. Annu. Rev. Biochem., 1994, 63(1), 527-570.
    • (1994) Annu. Rev. Biochem , vol.63 , Issue.1 , pp. 527-570
    • Lohman, T.M.1    Ferrari, M.E.2
  • 6
    • 0027479161 scopus 로고
    • OB (oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin, A.G. OB (oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J., 1993, 12(3), 861.
    • (1993) EMBO J , vol.12 , Issue.3 , pp. 861
    • Murzin, A.G.1
  • 7
    • 33947572536 scopus 로고    scopus 로고
    • Identification and properties of the Deinococcus grandis and Deinococcus proteolyticus single-stranded DNA binding proteins (SSB)
    • Filipkowski, P.; Kur, J. Identification and properties of the Deinococcus grandis and Deinococcus proteolyticus single-stranded DNA binding proteins (SSB). Acta Biochim Pol., 2007, 54(1), 79.
    • (2007) Acta Biochim Pol , vol.54 , Issue.1 , pp. 79
    • Filipkowski, P.1    Kur, J.2
  • 8
    • 15044347420 scopus 로고    scopus 로고
    • Single-stranded DNA-binding protein of Deinococcus radiodurans: A biophysical characterization
    • Witte, G.; Urbanke, C.; Curth, U. Single-stranded DNA-binding protein of Deinococcus radiodurans: a biophysical characterization. Nucl. Acids Res.,2005, 33(5), 1662.
    • (2005) Nucl. Acids Res , vol.33 , Issue.5 , pp. 1662
    • Witte, G.1    Urbanke, C.2    Curth, U.3
  • 9
    • 2942642109 scopus 로고    scopus 로고
    • The single-stranded DNA-binding protein of Deinococcus radiodurans
    • Eggington, J.M.; Haruta, N.; Wood, E.A.; Cox, M.M. The single-stranded DNA-binding protein of Deinococcus radiodurans. BMC Microbiol., 2004, 4, 2.
    • (2004) BMC Microbiol , vol.4 , pp. 2
    • Eggington, J.M.1    Haruta, N.2    Wood, E.A.3    Cox, M.M.4
  • 10
    • 33746420480 scopus 로고    scopus 로고
    • Novel thermostable single-stranded DNA-binding protein (SSB) from Deinococcus geothermalis
    • Filipkowski, P.; Duraj-Thatte, A.; Kur, J. Novel thermostable single-stranded DNA-binding protein (SSB) from Deinococcus geothermalis. Arch. Microbiol., 2006, 186(2), 129-137.
    • (2006) Arch. Microbiol , vol.186 , Issue.2 , pp. 129-137
    • Filipkowski, P.1    Duraj-Thatte, A.2    Kur, J.3
  • 11
    • 33751096700 scopus 로고    scopus 로고
    • A highly thermostable, homodimeric single-stranded DNA-binding protein from Deinococcus radiopugnans
    • Filipkowski, P.; Koziatek, M.; Kur, J. A highly thermostable, homodimeric single-stranded DNA-binding protein from Deinococcus radiopugnans. Extremophiles, 2006, 10(6), 607-614.
    • (2006) Extremophiles , vol.10 , Issue.6 , pp. 607-614
    • Filipkowski, P.1    Koziatek, M.2    Kur, J.3
  • 12
    • 33847131819 scopus 로고    scopus 로고
    • Identification, cloning, expression, and characterization of a highly thermostable single-stranded-DNA-binding protein (SSB) from Deinococcus murrayi
    • Filipkowski, P.; Duraj-Thatte, A.; Kur, J. Identification, cloning, expression, and characterization of a highly thermostable single-stranded-DNA-binding protein (SSB) from Deinococcus murrayi. Protein Expr. Purif., 2007, 53(1), 201-208.
    • (2007) Protein Expr. Purif , vol.53 , Issue.1 , pp. 201-208
    • Filipkowski, P.1    Duraj-Thatte, A.2    Kur, J.3
  • 13
    • 33947572536 scopus 로고    scopus 로고
    • Identification and properties of the Deinococcus grandis and Deinococcus proteolyticus single-stranded DNA binding proteins (SSB)
    • Filipkowski, P.; Kur, J. Identification and properties of the Deinococcus grandis and Deinococcus proteolyticus single-stranded DNA binding proteins (SSB). Acta Biochim. Pol., 2007, 54(1), 79-87.
    • (2007) Acta Biochim. Pol , vol.54 , Issue.1 , pp. 79-87
    • Filipkowski, P.1    Kur, J.2
  • 14
    • 15044347420 scopus 로고    scopus 로고
    • Single-stranded DNA-binding protein of Deinococcus radiodurans: A biophysical characterization
    • Witte, G.; Urbanke, C.; Curth, U. Single-stranded DNA-binding protein of Deinococcus radiodurans: a biophysical characterization. Nucl. Acids Res., 2005, 33(5), 1662-1670.
    • (2005) Nucl. Acids Res , vol.33 , Issue.5 , pp. 1662-1670
    • Witte, G.1    Urbanke, C.2    Curth, U.3
  • 15
    • 2942597631 scopus 로고    scopus 로고
    • Crystal structure of the Deinococcus radiodurans single-stranded DNA-binding protein suggests a mechanism for coping with DNA damage
    • Bernstein, D.A.; Eggington, J.M.; Killoran, M.P.; Misic, A.M.; Cox, M.M.; Keck, J.L. Crystal structure of the Deinococcus radiodurans single-stranded DNA-binding protein suggests a mechanism for coping with DNA damage. PNAS, 2004, 101(23), 8575-8580.
    • (2004) PNAS , vol.101 , Issue.23 , pp. 8575-8580
    • Bernstein, D.A.1    Eggington, J.M.2    Killoran, M.P.3    Misic, A.M.4    Cox, M.M.5    Keck, J.L.6
  • 16
    • 33846092922 scopus 로고    scopus 로고
    • Three tandem HRDC domains have synergistic effect on the RecQ functions in Deinococcus radiodurans
    • Huang, L.; Hua, X.; Lu, H.; Gao, G.; Tian, B.; Shen, B.; Hua, Y. Three tandem HRDC domains have synergistic effect on the RecQ functions in Deinococcus radiodurans. DNA Repair (Amst), 2007, 6, 167-176.
    • (2007) DNA Repair (Amst) , vol.6 , pp. 167-176
    • Huang, L.1    Hua, X.2    Lu, H.3    Gao, G.4    Tian, B.5    Shen, B.6    Hua, Y.7
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Chem., 1976, 72(1-2), 248-254.
    • (1976) Anal. Chem , vol.72 , Issue.1-2 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 4444255459 scopus 로고    scopus 로고
    • The utility of a two-color fluorescence electrophoretic mobility shift assay procedure for the analysis of DNA replication complexes
    • Jing, D.; Beechem, J.M.; Patton, W.F. The utility of a two-color fluorescence electrophoretic mobility shift assay procedure for the analysis of DNA replication complexes. Electrophoresis, 2004, 25(15), 2439-2446.
    • (2004) Electrophoresis , vol.25 , Issue.15 , pp. 2439-2446
    • Jing, D.1    Beechem, J.M.2    Patton, W.F.3
  • 19
  • 20
    • 0036314935 scopus 로고    scopus 로고
    • Biochemical properties of single-stranded DNA-binding protein from Mycobacterium smegmatis, a fast-growing mycobacterium and its physical and functional interaction with uracil DNA glycosylases
    • Acharya, N.; Varshney, U. Biochemical properties of single-stranded DNA-binding protein from Mycobacterium smegmatis, a fast-growing mycobacterium and its physical and functional interaction with uracil DNA glycosylases. J. Mol. Biol., 2002, 318(5), 1251-1264.
    • (2002) J. Mol. Biol , vol.318 , Issue.5 , pp. 1251-1264
    • Acharya, N.1    Varshney, U.2
  • 21
    • 34248664689 scopus 로고    scopus 로고
    • Dynamic structural rearrangements between DNA binding modes of E. coli SSB protein
    • Roy, R.; Kozlov, A.G.; Lohman, T.M.; Ha, T. Dynamic structural rearrangements between DNA binding modes of E. coli SSB protein. J. Mol. Biol., 2007, 369(5), 1244.
    • (2007) J. Mol. Biol , vol.369 , Issue.5 , pp. 1244
    • Roy, R.1    Kozlov, A.G.2    Lohman, T.M.3    Ha, T.4
  • 22
    • 15544389841 scopus 로고    scopus 로고
    • Rapid subfunctionalization accompanied by prolonged and substantial neofunctionalization in duplicate gene evolution
    • He, X.; Zhang, J. Rapid subfunctionalization accompanied by prolonged and substantial neofunctionalization in duplicate gene evolution. Genetics 2005, 169(2), 1157-1164.
    • (2005) Genetics , vol.169 , Issue.2 , pp. 1157-1164
    • He, X.1    Zhang, J.2
  • 23
    • 21144453167 scopus 로고    scopus 로고
    • Structure, function, and evolution of the tRNA endonucleases of Archaea: An example of subfunctionalization
    • Tocchini-Valentini, G.D.; Fruscoloni, P.; Tocchini-Valentini, G.P. Structure, function, and evolution of the tRNA endonucleases of Archaea: An example of subfunctionalization. PNAS, 2005, 102(25), 8933-8938.
    • (2005) PNAS , vol.102 , Issue.25 , pp. 8933-8938
    • Tocchini-Valentini, G.D.1    Fruscoloni, P.2    Tocchini-Valentini, G.P.3
  • 24
    • 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. Nucl. Acids Res., 1996, 24(14), 2706.
    • (1996) Nucl. Acids Res , vol.24 , Issue.14 , pp. 2706
    • Curth, U.1    Genschel, J.2    Urbanke, C.3    Greipel, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.