메뉴 건너뛰기




Volumn 276, Issue 2, 2009, Pages 519-531

Helicobacter pylori single-stranded DNA binding protein - Functional characterization and modulation of H. pylori DnaB helicase activity

Author keywords

DNA replication; Helicase; Helicobacter pylori; Replication foci; Single stranded DNA binding protein

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DNAB HELICASE; SINGLE STRANDED DNA BINDING PROTEIN;

EID: 58149175920     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06799.x     Document Type: Article
Times cited : (17)

References (40)
  • 1
    • 33645740999 scopus 로고    scopus 로고
    • The pathogenesis of Helicobacter pylori-induced gastro-duodenal diseases
    • Atherton JC (2006) The pathogenesis of Helicobacter pylori-induced gastro-duodenal diseases. Annu Rev Pathol 1, 63 96.
    • (2006) Annu Rev Pathol , vol.1 , pp. 63-96
    • Atherton, J.C.1
  • 2
    • 0142181239 scopus 로고    scopus 로고
    • Molecular mechanism of action of major Helicobacter pylori virulence factors
    • Dhar SK, Soni RK, Das BK Mukhopadhyay G (2003) Molecular mechanism of action of major Helicobacter pylori virulence factors. Mol Cell Biochem 253, 207 215.
    • (2003) Mol Cell Biochem , vol.253 , pp. 207-215
    • Dhar, S.K.1    Soni, R.K.2    Das, B.K.3    Mukhopadhyay, G.4
  • 4
    • 41549155076 scopus 로고    scopus 로고
    • H. pylori recurrence after successful eradication
    • Niv Y (2008) H. pylori recurrence after successful eradication. World J Gastroenterol 14, 1477 1478.
    • (2008) World J Gastroenterol , vol.14 , pp. 1477-1478
    • Niv, Y.1
  • 5
    • 0025907279 scopus 로고
    • Characterization of the morphologic conversion of Helicobacter pylori from bacillary to coccoid forms
    • Catrenich CE Makin KM (1991) Characterization of the morphologic conversion of Helicobacter pylori from bacillary to coccoid forms. Scand J Gastroenterol 26 (Suppl. 181 58 64.
    • (1991) Scand J Gastroenterol , vol.26 , Issue.181 , pp. 58-64
    • Catrenich, C.E.1    Makin, K.M.2
  • 7
    • 85088330150 scopus 로고    scopus 로고
    • Coccoid forms of Helicobacter pylori
    • Cellini L (1996) Coccoid forms of Helicobacter pylori. J Infect Dis 173, 1288.
    • (1996) J Infect Dis , vol.173 , pp. 1288
    • Cellini, L.1
  • 12
    • 22544460494 scopus 로고    scopus 로고
    • Helicobacter pylori DnaB helicase can bypass Escherichia coli DnaC function in vivo
    • Soni RK, Mehra P, Mukhopadhyay G Dhar SK (2005) Helicobacter pylori DnaB helicase can bypass Escherichia coli DnaC function in vivo. Biochem J 389, 541 548.
    • (2005) Biochem J , vol.389 , pp. 541-548
    • Soni, R.K.1    Mehra, P.2    Mukhopadhyay, G.3    Dhar, S.K.4
  • 13
    • 34250632433 scopus 로고    scopus 로고
    • The domain structure of Helicobacter pylori DnaB helicase: The N-terminal domain can be dispensable for helicase activity whereas the extreme C-terminal region is essential for its function
    • Nitharwal RG, Paul S, Dar A, Choudhury NR, Soni RK, Prusty D, Sinha S, Kashav T, Mukhopadhyay G, Chaudhuri TK et al. (2007) The domain structure of Helicobacter pylori DnaB helicase: the N-terminal domain can be dispensable for helicase activity whereas the extreme C-terminal region is essential for its function. Nucleic Acids Res 35, 2861 2874.
    • (2007) Nucleic Acids Res , vol.35 , pp. 2861-2874
    • Nitharwal, R.G.1    Paul, S.2    Dar, A.3    Choudhury, N.R.4    Soni, R.K.5    Prusty, D.6    Sinha, S.7    Kashav, T.8    Mukhopadhyay, G.9    Chaudhuri, T.K.10
  • 15
    • 34547676738 scopus 로고    scopus 로고
    • Structural similarity between the DnaA-binding proteins HobA (HP1230) from Helicobacter pylori and DiaA from Escherichia coli
    • Natrajan G, Hall DR, Thompson AC, Gutsche I Terradot L (2007) Structural similarity between the DnaA-binding proteins HobA (HP1230) from Helicobacter pylori and DiaA from Escherichia coli. Mol Microbiol 65, 995 1005.
    • (2007) Mol Microbiol , vol.65 , pp. 995-1005
    • Natrajan, G.1    Hall, D.R.2    Thompson, A.C.3    Gutsche, I.4    Terradot, L.5
  • 16
    • 0029052511 scopus 로고
    • Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA
    • Shamoo Y, Friedman AM, Parsons MR, Konigsberg WH Steitz TA (1995) Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA. Nature 376, 362 366.
    • (1995) Nature , vol.376 , pp. 362-366
    • Shamoo, Y.1    Friedman, A.M.2    Parsons, M.R.3    Konigsberg, W.H.4    Steitz, T.A.5
  • 17
    • 0031567573 scopus 로고    scopus 로고
    • A common core for binding single-stranded DNA: Structural comparison of the single-stranded DNA-binding proteins (SSB) from E. coli and human mitochondria
    • Webster G, Genschel J, Curth U, Urbanke C, Kang C Hilgenfeld R (1997) A common core for binding single-stranded DNA: structural comparison of the single-stranded DNA-binding proteins (SSB) from E. coli and human mitochondria. FEBS Lett 411, 313 316.
    • (1997) FEBS Lett , vol.411 , pp. 313-316
    • Webster, G.1    Genschel, J.2    Curth, U.3    Urbanke, C.4    Kang, C.5    Hilgenfeld, R.6
  • 18
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin AG (1993) OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J 12, 861 867.
    • (1993) EMBO J , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 19
    • 0030903098 scopus 로고    scopus 로고
    • Functional domains of Escherichia coli single-stranded DNA binding protein as assessed by analyses of the deletion mutants
    • Kinebuchi T, Shindo H, Nagai H, Shimamoto N Shimizu M (1997) Functional domains of Escherichia coli single-stranded DNA binding protein as assessed by analyses of the deletion mutants. Biochemistry 36, 6732 6738.
    • (1997) Biochemistry , vol.36 , pp. 6732-6738
    • Kinebuchi, T.1    Shindo, H.2    Nagai, H.3    Shimamoto, N.4    Shimizu, M.5
  • 20
    • 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 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
  • 21
    • 2342516683 scopus 로고    scopus 로고
    • Physical and functional interaction of the archaeal single-stranded DNA-binding protein SSB with RNA polymerase
    • Richard DJ, Bell SD White MF (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
  • 22
    • 0036639412 scopus 로고    scopus 로고
    • Modulation of enzymatic activities of Escherichia coli DnaB helicase by single-stranded DNA-binding proteins
    • Biswas EE, Chen PH Biswas SB (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
  • 23
    • 13444282478 scopus 로고    scopus 로고
    • PriA helicase and SSB interact physically and functionally
    • Cadman CJ McGlynn P (2004) PriA helicase and SSB interact physically and functionally. Nucleic Acids Res 32, 6378 6387.
    • (2004) Nucleic Acids Res , vol.32 , pp. 6378-6387
    • Cadman, C.J.1    McGlynn, P.2
  • 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 (1996) In vitro and in vivo function of the C-terminus of Escherichia coli single-stranded DNA binding protein. Nucleic Acids Res 24, 2706 2711.
    • (1996) Nucleic Acids Res , vol.24 , pp. 2706-2711
    • Curth, U.1    Genschel, J.2    Urbanke, C.3    Greipel, J.4
  • 25
    • 0023655856 scopus 로고
    • Investigation of the role of individual tryptophan residues in the binding of Escherichia coli single-stranded DNA binding protein to single-stranded polynucleotides. a study by optical detection of magnetic resonance and site-selected mutagenesis
    • Khamis MI, Casas-Finet JR, Maki AH, Murphy JB Chase JW (1987) Investigation of the role of individual tryptophan residues in the binding of Escherichia coli single-stranded DNA binding protein to single-stranded polynucleotides. A study by optical detection of magnetic resonance and site-selected mutagenesis. J Biol Chem 262, 10938 10945.
    • (1987) J Biol Chem , vol.262 , pp. 10938-10945
    • Khamis, M.I.1    Casas-Finet, J.R.2    Maki, A.H.3    Murphy, J.B.4    Chase, J.W.5
  • 26
    • 0026064009 scopus 로고
    • Amino acid 55 plays a central role in tetramerization and function of Escherichia coli single-stranded DNA binding protein
    • Curth U, Bayer I, Greipel J, Mayer F, Urbanke C Maass G (1991) Amino acid 55 plays a central role in tetramerization and function of Escherichia coli single-stranded DNA binding protein. Eur J Biochem 196, 87 93.
    • (1991) Eur J Biochem , vol.196 , pp. 87-93
    • Curth, U.1    Bayer, I.2    Greipel, J.3    Mayer, F.4    Urbanke, C.5    Maass, G.6
  • 27
    • 0034307459 scopus 로고    scopus 로고
    • Distinct properties of Mycobacterium tuberculosis single-stranded DNA binding protein and its functional characterization in Escherichia coli
    • Handa P, Acharya N, Thanedar S, Purnapatre K Varshney U (2000) Distinct properties of Mycobacterium tuberculosis single-stranded DNA binding protein and its functional characterization in Escherichia coli. Nucleic Acids Res 28, 3823 3829.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3823-3829
    • Handa, P.1    Acharya, N.2    Thanedar, S.3    Purnapatre, K.4    Varshney, U.5
  • 28
    • 41149121779 scopus 로고    scopus 로고
    • Independent positioning and action of Escherichia coli replisomes in live cells
    • Reyes-Lamothe R, Possoz C, Danilova O Sherratt DJ (2008) Independent positioning and action of Escherichia coli replisomes in live cells. Cell 133, 90 102.
    • (2008) Cell , vol.133 , pp. 90-102
    • Reyes-Lamothe, R.1    Possoz, C.2    Danilova, O.3    Sherratt, D.J.4
  • 29
    • 0034074478 scopus 로고    scopus 로고
    • Interaction of E. coli single-stranded DNA binding protein (SSB) with exonuclease I. the carboxy-terminus of SSB is the recognition site for the nuclease
    • Genschel J, Curth U Urbanke C (2000) Interaction of E. coli single-stranded DNA binding protein (SSB) with exonuclease I. The carboxy-terminus of SSB is the recognition site for the nuclease. Biol Chem 381, 183 192.
    • (2000) Biol Chem , vol.381 , pp. 183-192
    • Genschel, J.1    Curth, U.2    Urbanke, C.3
  • 31
    • 0027716026 scopus 로고
    • The coccoid forms of Helicobacter pylori. Criteria for their viability
    • Bode G, Mauch F Malfertheiner P (1993) The coccoid forms of Helicobacter pylori. Criteria for their viability. Epidemiol Infect 111, 483 490.
    • (1993) Epidemiol Infect , vol.111 , pp. 483-490
    • Bode, G.1    Mauch, F.2    Malfertheiner, P.3
  • 32
    • 0031027614 scopus 로고    scopus 로고
    • Coccoid and spiral Helicobacter pylori differ in their abilities to adhere to gastric epithelial cells and induce interleukin-8 secretion
    • Cole SP, Cirillo D, Kagnoff MF, Guiney DG Eckmann L (1997) Coccoid and spiral Helicobacter pylori differ in their abilities to adhere to gastric epithelial cells and induce interleukin-8 secretion. Infect Immun 65, 843 846.
    • (1997) Infect Immun , vol.65 , pp. 843-846
    • Cole, S.P.1    Cirillo, D.2    Kagnoff, M.F.3    Guiney, D.G.4    Eckmann, L.5
  • 34
    • 0032432067 scopus 로고    scopus 로고
    • Diversity in protein synthesis and viability of Helicobacter pylori coccoid forms in response to various stimuli
    • Mizoguchi H, Fujioka T, Kishi K, Nishizono A, Kodama R Nasu M (1998) Diversity in protein synthesis and viability of Helicobacter pylori coccoid forms in response to various stimuli. Infect Immun 66, 5555 5560.
    • (1998) Infect Immun , vol.66 , pp. 5555-5560
    • Mizoguchi, H.1    Fujioka, T.2    Kishi, K.3    Nishizono, A.4    Kodama, R.5    Nasu, M.6
  • 35
    • 0033085161 scopus 로고    scopus 로고
    • In vitro aging of Helicobacter pylori: Changes in morphology, intracellular composition and surface properties
    • Enroth H, Wreiber K, Rigo R, Risberg D, Uribe A Engstrand L (1999) In vitro aging of Helicobacter pylori: changes in morphology, intracellular composition and surface properties. Helicobacter 4, 7 16.
    • (1999) Helicobacter , vol.4 , pp. 7-16
    • Enroth, H.1    Wreiber, K.2    Rigo, R.3    Risberg, D.4    Uribe, A.5    Engstrand, L.6
  • 36
    • 58149146941 scopus 로고    scopus 로고
    • Ausubel, F.M.*Brent R.*Kingston R.E.*Moore D.D.*Seidman J.G.*Smith J.A.*Struhl K. (. eds. pp. John Wiley & Sons, New York, NY.
    • Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA Struhl K (eds 1999) Short Protocols in Molecular Biology, 4th edn, pp. 1 22. John Wiley & Sons, New York, NY.
    • (1999) Short Protocols in Molecular Biology, 4th Edn , pp. 1-22
  • 37
    • 58149173244 scopus 로고
    • Sambrook, J., Fritsch, E.F. Maniatis, T. (. ed. pp. Cold Spring Harbor Press, Cold Spring Harbor, NY.
    • Sambrook J, Fritsch EF Maniatis T (ed 1989) Molecular Cloning: A Laboratory Manual, 2nd edn, pp. 4.21 4.32. Cold Spring Harbor Press, Cold Spring Harbor, NY.
    • (1989) Molecular Cloning: A Laboratory Manual, 2nd Edn , pp. 421-432
  • 38
    • 0004270170 scopus 로고    scopus 로고
    • Ausubel, F.M.*Brent R.*Kingston R.E.*Moore D.D.*Seidman J.G.*Smith J.A.*Struhl K. (. eds. Vol. 1, pp. 1.1.1. John Wiley & Sons, New York, NY.
    • Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA Struhl K (eds 1998) Current Protocols in Molecular Biology. Vol. 1, pp. 1.1.1. John Wiley & Sons, New York, NY.
    • (1998) Current Protocols in Molecular Biology.
  • 39
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner NC, Campbell RE, Steinbach PA, Giepmans BN, Palmer AE Tsien RY (2004) Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat Biotechnol 22, 1567 1572.
    • (2004) Nat Biotechnol , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5    Tsien, R.Y.6
  • 40
    • 0003694904 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • Harlow E Lane D (1988) Antibodies. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) Antibodies.
    • Harlow, E.1    Lane, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.