메뉴 건너뛰기




Volumn 404, Issue 1, 2011, Pages 546-551

Identification of a novel protein, PriB, in Klebsiella pneumoniae

Author keywords

PriA; PriB; Primosome; SSB; SsDNA binding

Indexed keywords

ALANINE; BACTERIAL PROTEIN; HOMODIMER; MONOMER; POLYPEPTIDE; PRIB PROTEIN; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 78650901944     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.12.023     Document Type: Article
Times cited : (13)

References (30)
  • 1
    • 33845330910 scopus 로고    scopus 로고
    • Replisome assembly and the direct restart of stalled replication forks
    • Heller R.C., Marians K.J. Replisome assembly and the direct restart of stalled replication forks. Nat. Rev. Mol. Cell Biol. 2006, 7:932-943.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 932-943
    • Heller, R.C.1    Marians, K.J.2
  • 3
    • 0036844340 scopus 로고    scopus 로고
    • Recombinational repair and restart of damaged replication forks
    • McGlynn P., Lloyd R.G. Recombinational repair and restart of damaged replication forks. Nat. Rev. Mol. Cell Biol. 2002, 3:859-870.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 859-870
    • McGlynn, P.1    Lloyd, R.G.2
  • 4
    • 0033988501 scopus 로고    scopus 로고
    • Role of PriA in replication fork reactivation in Escherichia coli
    • Sandler S.J., Marians K.J. Role of PriA in replication fork reactivation in Escherichia coli. J. Bacteriol. 2000, 182:9-13.
    • (2000) J. Bacteriol. , vol.182 , pp. 9-13
    • Sandler, S.J.1    Marians, K.J.2
  • 5
    • 0034177963 scopus 로고    scopus 로고
    • PriA-directed replication fork restart in Escherichia coli
    • Marians K.J. PriA-directed replication fork restart in Escherichia coli. Trends Biochem. Sci. 2000, 25:185-189.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 185-189
    • Marians, K.J.1
  • 6
    • 77954833871 scopus 로고    scopus 로고
    • Stalled replication forks: making ends meet for recognition and stabilization
    • Masai H., Tanaka T., Kohda D. Stalled replication forks: making ends meet for recognition and stabilization. Bioessays 2010, 32:687-697.
    • (2010) Bioessays , vol.32 , pp. 687-697
    • Masai, H.1    Tanaka, T.2    Kohda, D.3
  • 7
    • 76749101865 scopus 로고    scopus 로고
    • Recruitment to stalled replication forks of the PriA DNA helicase and replisome-loading activities is essential for survival
    • Gabbai C.B., Marians K.J. Recruitment to stalled replication forks of the PriA DNA helicase and replisome-loading activities is essential for survival. DNA Repair (Amst.) 2010, 9:202-209.
    • (2010) DNA Repair (Amst.) , vol.9 , pp. 202-209
    • Gabbai, C.B.1    Marians, K.J.2
  • 8
    • 31844456472 scopus 로고    scopus 로고
    • Replication fork reactivation downstream of a blocked nascent leading strand
    • Heller R.C., Marians K.J. Replication fork reactivation downstream of a blocked nascent leading strand. Nature 2006, 439:557-562.
    • (2006) Nature , vol.439 , pp. 557-562
    • Heller, R.C.1    Marians, K.J.2
  • 9
    • 34250380631 scopus 로고    scopus 로고
    • A hand-off mechanism for primosome assembly in replication restart
    • Lopper M., Boonsombat R., Sandler S.J., Keck J.L. A hand-off mechanism for primosome assembly in replication restart. Mol. Cell 2007, 26:781-793.
    • (2007) Mol. Cell , vol.26 , pp. 781-793
    • Lopper, M.1    Boonsombat, R.2    Sandler, S.J.3    Keck, J.L.4
  • 10
    • 28844489365 scopus 로고    scopus 로고
    • PriB stimulates PriA helicase via an interaction with single-stranded DNA
    • Cadman C.J., Lopper M., Moon P.B., Keck J.L., McGlynn P. PriB stimulates PriA helicase via an interaction with single-stranded DNA. J. Biol. Chem. 2005, 280:39693-39700.
    • (2005) J. Biol. Chem. , vol.280 , pp. 39693-39700
    • Cadman, C.J.1    Lopper, M.2    Moon, P.B.3    Keck, J.L.4    McGlynn, P.5
  • 11
    • 0029666278 scopus 로고    scopus 로고
    • The ordered assembly of the phiX174-type primosome. III. PriB facilitates complex formation between PriA and DnaT
    • Liu J., Nurse P., Marians K.J. The ordered assembly of the phiX174-type primosome. III. PriB facilitates complex formation between PriA and DnaT. J. Biol. Chem. 1996, 271:15656-15661.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15656-15661
    • Liu, J.1    Nurse, P.2    Marians, K.J.3
  • 12
    • 63349092249 scopus 로고    scopus 로고
    • The crystal structure of a replicative hexameric helicase DnaC and its complex with single-stranded DNA
    • Lo Y.H., Tsai K.L., Sun Y.J., Chen W.T., Huang C.Y., Hsiao C.D. The crystal structure of a replicative hexameric helicase DnaC and its complex with single-stranded DNA. Nucleic Acids Res. 2009, 37:804-814.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 804-814
    • Lo, Y.H.1    Tsai, K.L.2    Sun, Y.J.3    Chen, W.T.4    Huang, C.Y.5    Hsiao, C.D.6
  • 13
    • 35348979683 scopus 로고    scopus 로고
    • Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase
    • Bailey S., Eliason W.K., Steitz T.A. Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science 2007, 318:459-463.
    • (2007) Science , vol.318 , pp. 459-463
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 14
    • 0028049949 scopus 로고
    • Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork
    • Tougu K., Peng H., Marians K.J. Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork. J. Biol. Chem. 1994, 269:4675-4682.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4675-4682
    • Tougu, K.1    Peng, H.2    Marians, K.J.3
  • 15
    • 77449143367 scopus 로고    scopus 로고
    • The crystal structure of Neisseria gonorrhoeae PriB reveals mechanistic differences among bacterial DNA replication restart pathways
    • Dong J., George N.P., Duckett K.L., DeBeer M.A., Lopper M.E. The crystal structure of Neisseria gonorrhoeae PriB reveals mechanistic differences among bacterial DNA replication restart pathways. Nucleic Acids Res. 2010, 38:499-509.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 499-509
    • Dong, J.1    George, N.P.2    Duckett, K.L.3    DeBeer, M.A.4    Lopper, M.E.5
  • 16
    • 10644282271 scopus 로고    scopus 로고
    • Crystal structure of a biologically functional form of PriB from Escherichia coli reveals a potential single-stranded DNA-binding site
    • Shioi S., Ose T., Maenaka K., Shiroishi M., Abe Y., Kohda D., Katayama T., Ueda T. Crystal structure of a biologically functional form of PriB from Escherichia coli reveals a potential single-stranded DNA-binding site. Biochem. Biophys. Res. Commun. 2005, 326:766-776.
    • (2005) Biochem. Biophys. Res. Commun. , vol.326 , pp. 766-776
    • Shioi, S.1    Ose, T.2    Maenaka, K.3    Shiroishi, M.4    Abe, Y.5    Kohda, D.6    Katayama, T.7    Ueda, T.8
  • 17
    • 7944229709 scopus 로고    scopus 로고
    • Crystal structure of PriB, a component of the Escherichia coli replication restart primosome
    • Lopper M., Holton J.M., Keck J.L. Crystal structure of PriB, a component of the Escherichia coli replication restart primosome. Structure 2004, 12:1967-1975.
    • (2004) Structure , vol.12 , pp. 1967-1975
    • Lopper, M.1    Holton, J.M.2    Keck, J.L.3
  • 18
  • 20
    • 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, 12:861-867.
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 21
    • 33748568506 scopus 로고    scopus 로고
    • Complexed crystal structure of replication restart primosome protein PriB reveals a novel single-stranded DNA-binding mode
    • Huang C.Y., Hsu C.H., Sun Y.J., Wu H.N., Hsiao C.D. Complexed crystal structure of replication restart primosome protein PriB reveals a novel single-stranded DNA-binding mode. Nucleic Acids Res. 2006, 34:3878-3886.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3878-3886
    • Huang, C.Y.1    Hsu, C.H.2    Sun, Y.J.3    Wu, H.N.4    Hsiao, C.D.5
  • 22
    • 77950858634 scopus 로고    scopus 로고
    • Interactions of the Escherichia coli primosomal PriB protein with the single-stranded DNA. Stoichiometries, intrinsic affinities, cooperativities, and base specificities
    • Szymanski M.R., Jezewska M.J., Bujalowski W. Interactions of the Escherichia coli primosomal PriB protein with the single-stranded DNA. Stoichiometries, intrinsic affinities, cooperativities, and base specificities. J. Mol. Biol. 2010, 398:8-25.
    • (2010) J. Mol. Biol. , vol.398 , pp. 8-25
    • Szymanski, M.R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 23
    • 64649099756 scopus 로고    scopus 로고
    • Single-stranded DNA-binding protein complex from Helicobacter pylori suggests an ssDNA-binding surface
    • Chan K.W., Lee Y.J., Wang C.H., Huang H., Sun Y.J. Single-stranded DNA-binding protein complex from Helicobacter pylori suggests an ssDNA-binding surface. J. Mol. Biol. 2009, 388:508-519.
    • (2009) J. Mol. Biol. , vol.388 , pp. 508-519
    • Chan, K.W.1    Lee, Y.J.2    Wang, C.H.3    Huang, H.4    Sun, Y.J.5
  • 25
    • 77956264695 scopus 로고    scopus 로고
    • Identification and characterization of a putative dihydroorotase, KPN01074, from Klebsiella pneumoniae
    • Wang C.C., Tsau H.W., Chen W.T., Huang C.Y. Identification and characterization of a putative dihydroorotase, KPN01074, from Klebsiella pneumoniae. Protein J. 2010, 29:445-452.
    • (2010) Protein J. , vol.29 , pp. 445-452
    • Wang, C.C.1    Tsau, H.W.2    Chen, W.T.3    Huang, C.Y.4
  • 26
    • 52049102229 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of Geobacillus kaustophilus HTA426 DnaD protein
    • Huang C.Y., Chang Y.W., Chen W.T. Crystal structure of the N-terminal domain of Geobacillus kaustophilus HTA426 DnaD protein. Biochem. Biophys. Res. Commun. 2008, 375:220-224.
    • (2008) Biochem. Biophys. Res. Commun. , vol.375 , pp. 220-224
    • Huang, C.Y.1    Chang, Y.W.2    Chen, W.T.3
  • 27
    • 0027172789 scopus 로고
    • A double-filter method for nitrocellulose-filter binding: application to protein-nucleic acid interactions
    • Wong I., Lohman T.M. A double-filter method for nitrocellulose-filter binding: application to protein-nucleic acid interactions. Proc. Natl. Acad. Sci. USA 1993, 90:5428-5432.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5428-5432
    • Wong, I.1    Lohman, T.M.2
  • 28
    • 14144251267 scopus 로고    scopus 로고
    • The structure of the excisionase (Xis) protein from conjugative transposon Tn916 provides insights into the regulation of heterobivalent tyrosine recombinases
    • Abbani M., Iwahara M., Clubb R.T. The structure of the excisionase (Xis) protein from conjugative transposon Tn916 provides insights into the regulation of heterobivalent tyrosine recombinases. J. Mol. Biol. 2005, 347:11-25.
    • (2005) J. Mol. Biol. , vol.347 , pp. 11-25
    • Abbani, M.1    Iwahara, M.2    Clubb, R.T.3
  • 30
    • 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, 63:527-570.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 527-570
    • Lohman, T.M.1    Ferrari, M.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.