title: Sulfolobus replication factor C stimulates the activity of DNA polymerase B1.
abstract: Replication factor C (RFC) is known to function in loading proliferating cell nuclear antigen (PCNA) onto primed DNA, allowing PCNA to tether DNA polymerase for highly processive DNA synthesis in eukaryotic and archaeal replication. In this report, we show that an RFC complex from the hyperthermophilic archaea of the genus Sulfolobus physically interacts with DNA polymerase B1 (PolB1) and enhances both the polymerase and 3'-5' exonuclease activities of PolB1 in an ATP-independent manner. Stimulation of the PolB1 activity by RFC is independent of the ability of RFC to bind DNA but is consistent with the ability of RFC to facilitate DNA binding by PolB1 through protein-protein interaction. These results suggest that Sulfolobus RFC may play a role in recruiting DNA polymerase for efficient primer extension, in addition to clamp loading, during DNA replication.
authors.affiliation: State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
authors.forename: Xuanxuan
authors.initials: X
authors.lastname: Xing
authors.affiliation: State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
authors.forename: Likui
authors.initials: L
authors.lastname: Zhang
authors.affiliation: State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
authors.forename: Li
authors.initials: L
authors.lastname: Guo
authors.affiliation: Danish Archaea Centre, Department of Biology, Copenhagen University, Copenhagen, Denmark.
authors.forename: Qunxin
authors.initials: Q
authors.lastname: She
authors.affiliation: State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China huangl@sun.im.ac.cn.
authors.forename: Li
authors.initials: L
authors.lastname: Huang
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology*; D015971:Gene Expression Regulation, Enzymologic / Q000502:physiology*; D016297:Mutagenesis, Site-Directed; D011485:Protein Binding; D051818:Replication Protein C / Q000235:genetics / Q000378:metabolism*; D016944:Sulfolobus / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D004259:DNA-Directed DNA Polymerase; D051818:Replication Protein C
references.citation: Mol Cell. 2007 Aug 17;27(4):527-38
references.pmid: 17707226
references.citation: Mol Cell Biol. 2009 Apr;29(8):2042-52
references.pmid: 19223468
references.citation: Cell. 2001 Aug 24;106(4):429-41
references.pmid: 11525729
references.citation: EMBO J. 2006 May 17;25(10):2209-18
references.pmid: 16628222
references.citation: Nucleic Acids Res. 2007;35(20):6904-16
references.pmid: 17932049
references.citation: J Biol Chem. 2000 Mar 10;275(10):7327-36
references.pmid: 10702304
references.citation: Mol Cell. 2003 Jan;11(1):275-82
references.pmid: 12535540
references.citation: J Mol Biol. 2000 Aug 4;301(1):61-73
references.pmid: 10926493
references.citation: J Biol Chem. 1991 Jan 25;266(3):1950-60
references.pmid: 1671045
references.citation: J Biol Chem. 2005 Dec 23;280(51):41852-63
references.pmid: 16257971
references.citation: Mol Microbiol. 2007 Apr;64(2):308-18
references.pmid: 17493121
references.citation: Mol Microbiol. 2008 Apr;68(1):216-22
references.pmid: 18312273
references.citation: J Biol Chem. 2011 Sep 9;286(36):31180-93
references.pmid: 21784862
references.citation: Extremophiles. 2009 Jul;13(4):735-46
references.pmid: 19513584
references.citation: Genes Cells. 2002 Sep;7(9):911-22
references.pmid: 12296822
references.citation: J Mol Biol. 2002 Nov 8;323(5):795-810
references.pmid: 12417194
references.citation: EMBO J. 1999 Nov 1;18(21):6189-99
references.pmid: 10545128
references.citation: Nat Protoc. 2006;1(1):418-28
references.pmid: 17406264
references.citation: Science. 2010 Apr 23;328(5977):498-501
references.pmid: 20413500
references.citation: Nucleic Acids Res. 2002 Oct 15;30(20):4329-38
references.pmid: 12384579
references.citation: Nature. 2004 Jun 17;429(6993):724-30
references.pmid: 15201901
references.citation: J Biol Chem. 2001 Sep 14;276(37):34776-83
references.pmid: 11432856
references.citation: Trends Microbiol. 2007 Apr;15(4):156-64
references.pmid: 17350265
references.citation: Nat Struct Mol Biol. 2011 Dec 11;19(1):113-6
references.pmid: 22157955
references.citation: Nucleic Acids Res. 2009 Nov;37(21):7194-205
references.pmid: 19773426
references.citation: J Biol Chem. 2009 Apr 17;284(16):10387-99
references.pmid: 19208620
references.citation: J Struct Biol. 2001 Apr;134(1):35-45
references.pmid: 11469875
references.citation: Extremophiles. 2003 Dec;7(6):493-8
references.pmid: 12955604
references.citation: Mol Microbiol. 2007 Feb;63(3):826-37
references.pmid: 17181784
references.citation: Biol Direct. 2008 Aug 06;3:32
references.pmid: 18684330
references.citation: Curr Opin Struct Biol. 2006 Feb;16(1):35-41
references.pmid: 16377178
references.citation: J Biol Chem. 1998 Nov 27;273(48):31992-9
references.pmid: 9822671
references.citation: J Mol Biol. 2013 Nov 29;425(23):4820-36
references.pmid: 24035812
references.citation: J Biol Chem. 2004 Dec 31;279(53):55196-201
references.pmid: 15502161
references.citation: Nat Struct Mol Biol. 2005 Feb;12(2):183-90
references.pmid: 15665871
references.citation: Biochem Soc Trans. 2009 Feb;37(Pt 1):92-6
references.pmid: 19143609
references.citation: FEMS Microbiol Lett. 2004 Feb 9;231(1):111-7
references.pmid: 14769474
references.citation: J Biol Chem. 2006 Jun 23;281(25):17528-17539
references.pmid: 16608854
references.citation: J Biol Chem. 2001 Sep 14;276(37):34768-75
references.pmid: 11432853
references.citation: J Biol Chem. 2012 Oct 26;287(44):36711-9
references.pmid: 22952233