메뉴 건너뛰기




Volumn 1, Issue 5, 2010, Pages 330-334

Structural insight into Helicobacter pylori DNA replication initiation

Author keywords

Bacterial replication; DiaA; DnaA; DnaB; Isothermal titration calorimetry; X ray crystallography

Indexed keywords

BACTERIAL DNA; BACTERIAL PROTEIN; DIAA PROTEIN; HOBA PROTEIN; MOLECULAR SCAFFOLD; OLIGOMER; REPLICATION INITIATOR PROTEIN DNAA; TETRAMER; UNCLASSIFIED DRUG;

EID: 77957669361     PISSN: 19490976     EISSN: 19490984     Source Type: Journal    
DOI: 10.4161/gmic.1.5.13115     Document Type: Article
Times cited : (8)

References (25)
  • 1
    • 34247271405 scopus 로고    scopus 로고
    • DNA replication initiation: Mechanisms and regulation in bacteria
    • Mott ML, Berger JM. DNA replication initiation: mechanisms and regulation in bacteria. Nat Rev Microbiol 2007; 5:343-54.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 343-354
    • Mott, M.L.1    Berger, J.M.2
  • 2
    • 33750312968 scopus 로고    scopus 로고
    • DnaA: Controlling the Initiation of Bacterial DNA Replication and More
    • Kaguni JM. DnaA: Controlling the Initiation of Bacterial DNA Replication and More. Annu Rev Microbiol 2006; 60:351-71.
    • (2006) Annu Rev Microbiol , vol.60 , pp. 351-371
    • Kaguni, J.M.1
  • 3
    • 34547100313 scopus 로고    scopus 로고
    • Structure and function of DnaA N-terminal domains: Specific sites and mechanisms in inter-DnaA interaction and in DnaB helicase loading on oriC
    • Abe Y, Jo T, Matsuda Y, Matsunaga C, Katayama T, Ueda T. Structure and function of DnaA N-terminal domains: specific sites and mechanisms in inter-DnaA interaction and in DnaB helicase loading on oriC. J Biol Chem 2007; 282:17816-27.
    • (2007) J Biol Chem , vol.282 , pp. 17816-17827
    • Abe, Y.1    Jo, T.2    Matsuda, Y.3    Matsunaga, C.4    Katayama, T.5    Ueda, T.6
  • 4
    • 0033812649 scopus 로고    scopus 로고
    • The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli
    • Seitz H, Weigel C, Messer W. The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli. Mol Microbiol 2000; 37:1270-9.
    • (2000) Mol Microbiol , vol.37 , pp. 1270-1279
    • Seitz, H.1    Weigel, C.2    Messer, W.3
  • 5
    • 55649098814 scopus 로고    scopus 로고
    • Structural synergy and molecular crosstalk between bacterial helicase loaders and replication initiators
    • Mott ML, Erzberger JP, Coons MM, Berger JM. Structural synergy and molecular crosstalk between bacterial helicase loaders and replication initiators. Cell 2008; 135:623-34.
    • (2008) Cell , vol.135 , pp. 623-634
    • Mott, M.L.1    Erzberger, J.P.2    Coons, M.M.3    Berger, J.M.4
  • 6
    • 67650717209 scopus 로고    scopus 로고
    • DnaA structure, function and dynamics in the initiation at the chromosomal origin
    • Ozaki S, Katayama T. DnaA structure, function and dynamics in the initiation at the chromosomal origin. Plasmid 2009; 62:71-82.
    • (2009) Plasmid , vol.62 , pp. 71-82
    • Ozaki, S.1    Katayama, T.2
  • 7
    • 0032844522 scopus 로고    scopus 로고
    • The N-terminus promotes oligomerization of the Escherichia coli initiator protein DnaA
    • Weigel C, Schmidt A, Seitz H, Tungler D, Welzeck M, Messer W. The N-terminus promotes oligomerization of the Escherichia coli initiator protein DnaA. Mol Microbiol 1999; 34:53-66.
    • (1999) Mol Microbiol , vol.34 , pp. 53-66
    • Weigel, C.1    Schmidt, A.2    Seitz, H.3    Tungler, D.4    Welzeck, M.5    Messer, W.6
  • 8
    • 0042665854 scopus 로고    scopus 로고
    • DnaA Protein of Escherichia coli: Oligomerization at the E. coli chromosomal origin is required for initiation and involves specific N-terminal amino acids
    • Simmons LA, Felczak M, Kaguni JM. DnaA Protein of Escherichia coli: oligomerization at the E. coli chromosomal origin is required for initiation and involves specific N-terminal amino acids. Mol Microbiol 2003; 49:849-58.
    • (2003) Mol Microbiol , vol.49 , pp. 849-858
    • Simmons, L.A.1    Felczak, M.2    Kaguni, J.M.3
  • 9
    • 33746860263 scopus 로고    scopus 로고
    • Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling
    • Epub 2006 Jul 9
    • Erzberger JP, Mott ML, Berger JM. Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat Struct Mol Biol 2006; 13:676-83. Epub 2006 Jul 9.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 676-683
    • Erzberger, J.P.1    Mott, M.L.2    Berger, J.M.3
  • 10
    • 0035422651 scopus 로고    scopus 로고
    • Hda, a novel DnaA-related protein, regulates the replication cycle in Escherichia coli
    • Kato J, Katayama T. Hda, a novel DnaA-related protein, regulates the replication cycle in Escherichia coli. EMBO J 2001; 20:4253-62.
    • (2001) EMBO J , vol.20 , pp. 4253-4262
    • Kato, J.1    Katayama, T.2
  • 11
    • 38449105269 scopus 로고    scopus 로고
    • Escherichia coli DnaA interacts with HU in initiation at the E. coli replication origin
    • Chodavarapu S, Felczak MM, Yaniv JR, Kaguni JM. Escherichia coli DnaA interacts with HU in initiation at the E. coli replication origin. Mol Microbiol 2008; 67:781-92.
    • (2008) Mol Microbiol , vol.67 , pp. 781-792
    • Chodavarapu, S.1    Felczak, M.M.2    Yaniv, J.R.3    Kaguni, J.M.4
  • 12
    • 34547941118 scopus 로고    scopus 로고
    • The interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP DnaA-specific initiation complexes
    • Keyamura K, Fujikawa N, Ishida T, Ozaki S, Su'etsugu M, Fujimitsu K, et al. The interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP DnaA-specific initiation complexes. Genes Dev 2007; 21:2083-99.
    • (2007) Genes Dev , vol.21 , pp. 2083-2099
    • Keyamura, K.1    Fujikawa, N.2    Ishida, T.3    Ozaki, S.4    Su'etsugu, M.5    Fujimitsu, K.6
  • 13
    • 70350155327 scopus 로고    scopus 로고
    • A role for nonessential domain II of initiator protein, DnaA, in replication control
    • Molt KL, Sutera VA Jr, Moore KK, Lovett ST. A role for nonessential domain II of initiator protein, DnaA, in replication control. Genetics 2009; 183:39-49.
    • (2009) Genetics , vol.183 , pp. 39-49
    • Molt, K.L.1    Sutera Jr., V.A.2    Moore, K.K.3    Lovett, S.T.4
  • 14
    • 8544240894 scopus 로고    scopus 로고
    • DiaA, a novel DnaA-binding protein, ensures the timely initiation of Escherichia coli chromosome replication
    • Ishida T, Akimitsu N, Kashioka T, Hatano M, Kubota T, Ogata Y, et al. DiaA, a novel DnaA-binding protein, ensures the timely initiation of Escherichia coli chromosome replication. J Biol Chem 2004; 279:45546-55.
    • (2004) J Biol Chem , vol.279 , pp. 45546-45555
    • Ishida, T.1    Akimitsu, N.2    Kashioka, T.3    Hatano, M.4    Kubota, T.5    Ogata, Y.6
  • 16
    • 34547683989 scopus 로고    scopus 로고
    • HobA-a novel protein involved in initiation of chromosomal replication in Helicobacter pylori
    • Epub 2007 Jul 21
    • Zawilak-Pawlik A, Kois A, Stingl K, Boneca IG, Skrobuk P, Piotr J, et al. HobA-a novel protein involved in initiation of chromosomal replication in Helicobacter pylori. Mol Microbiol 2007; 65:979-94; Epub 2007 Jul 21.
    • (2007) Mol Microbiol , vol.65 , pp. 979-994
    • Zawilak-Pawlik, A.1    Kois, A.2    Stingl, K.3    Boneca, I.G.4    Skrobuk, P.5    Piotr, J.6
  • 17
    • 4444378917 scopus 로고    scopus 로고
    • Biochemical characterization of protein complexes from the Helicobacter pylori protein interaction map: Strategies for complex formation and evidence for novel interactions within type IV secretion systems
    • Terradot L, Durnell N, Li M, Li M, Ory J, Labigne A, et al. Biochemical characterization of protein complexes from the Helicobacter pylori protein interaction map: strategies for complex formation and evidence for novel interactions within type IV secretion systems. Mol Cell Proteomics 2004; 3:809-19.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 809-819
    • Terradot, L.1    Durnell, N.2    Li, M.3    Li, M.4    Ory, J.5    Labigne, A.6
  • 18
    • 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. Structural similarity between the DnaA-binding proteins HobA (HP1230) from Helicobacter pylori and DiaA from Escherichia coli. Mol Microbiol 2007; 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
  • 19
    • 75849129293 scopus 로고    scopus 로고
    • The structure of a DnaA/HobA complex from Helicobacter pylori provides insight into regulation of DNA replication in bacteria
    • Natrajan G, Noirot-Gros MF, Zawilak-Pawlik A, Kapp U, Terradot L. The structure of a DnaA/HobA complex from Helicobacter pylori provides insight into regulation of DNA replication in bacteria. Proc Natl Acad Sci USA 2009; 106:21115-20.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 21115-21120
    • Natrajan, G.1    Noirot-Gros, M.F.2    Zawilak-Pawlik, A.3    Kapp, U.4    Terradot, L.5
  • 21
    • 63449095763 scopus 로고    scopus 로고
    • Natural transformation of Helicobacter pylori involves the integration of short DNA fragments interrupted by gaps of variable size
    • Lin EA, Zhang XS, Levine SM, Gill SR, Falush D, Blaser MJ. Natural transformation of Helicobacter pylori involves the integration of short DNA fragments interrupted by gaps of variable size. PLoS Pathog 2009; 5:1000337.
    • (2009) PLoS Pathog , vol.5 , pp. 1000337
    • Lin, E.A.1    Zhang, X.S.2    Levine, S.M.3    Gill, S.R.4    Falush, D.5    Blaser, M.J.6
  • 22
    • 35948940844 scopus 로고    scopus 로고
    • Plastic cells and populations: DNA substrate characteristics in Helicobacter pylori transformation define a flexible but conservative system for genomic variation
    • Levine SM, Lin EA, Emara W, Kang J, DiBenedetto M, Ando T, et al. Plastic cells and populations: DNA substrate characteristics in Helicobacter pylori transformation define a flexible but conservative system for genomic variation. Faseb J 2007; 21:3458-67.
    • (2007) Faseb J , vol.21 , pp. 3458-3467
    • Levine, S.M.1    Lin, E.A.2    Emara, W.3    Kang, J.4    DiBenedetto, M.5    Ando, T.6
  • 24
    • 0035369055 scopus 로고    scopus 로고
    • Identification of a putative chromosomal replication origin from Helicobacter pylori and its interaction with the initiator protein DnaA
    • Zawilak A, Cebrat S, Mackiewicz P, Krol-Hulewicz A, Jakimowicz D, Messer W, et al. Identification of a putative chromosomal replication origin from Helicobacter pylori and its interaction with the initiator protein DnaA. Nucleic Acids Res 2001; 29:2251-9.
    • (2001) Nucleic Acids Res , vol.29 , pp. 2251-2259
    • Zawilak, A.1    Cebrat, S.2    Mackiewicz, P.3    Krol-Hulewicz, A.4    Jakimowicz, D.5    Messer, W.6
  • 25
    • 75849165082 scopus 로고    scopus 로고
    • DiaA dynamics are coupled with changes in initial origin complexes leading to helicase loading
    • Keyamura K, Abe Y, Higashi M, Ueda T, Katayama T. DiaA dynamics are coupled with changes in initial origin complexes leading to helicase loading. J Biol Chem 2009; 24:24.
    • (2009) J Biol Chem , vol.24 , pp. 24
    • Keyamura, K.1    Abe, Y.2    Higashi, M.3    Ueda, T.4    Katayama, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.