| Structural highlights
Function
CTF18_HUMAN Chromosome cohesion factor involved in sister chromatid cohesion and fidelity of chromosome transmission. Component of one of the cell nuclear antigen loader complexes, CTF18-replication factor C (CTF18-RFC), which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. The CTF18-RFC complex binds to single-stranded and primed DNAs and has weak ATPase activity that is stimulated by the presence of primed DNA, replication protein A (RPA) and by proliferating cell nuclear antigen (PCNA). The CTF18-RFC complex catalyzes the ATP-dependent loading of PCNA onto primed and gapped DNA. Interacts with and stimulates DNA polymerase POLH. During DNA repair synthesis, involved in loading DNA polymerase POLE at the sites of local damage (PubMed:20227374).[1] [2] [3] [4]
References
- ↑ Merkle CJ, Karnitz LM, Henry-Sánchez JT, Chen J. Cloning and characterization of hCTF18, hCTF8, and hDCC1. Human homologs of a Saccharomyces cerevisiae complex involved in sister chromatid cohesion establishment. J Biol Chem. 2003 Aug 8;278(32):30051-6. PMID:12766176 doi:10.1074/jbc.M211591200
- ↑ Bermudez VP, Maniwa Y, Tappin I, Ozato K, Yokomori K, Hurwitz J. The alternative Ctf18-Dcc1-Ctf8-replication factor C complex required for sister chromatid cohesion loads proliferating cell nuclear antigen onto DNA. Proc Natl Acad Sci U S A. 2003 Sep 2;100(18):10237-42. PMID:12930902 doi:10.1073/pnas.1434308100
- ↑ Shiomi Y, Masutani C, Hanaoka F, Kimura H, Tsurimoto T. A second proliferating cell nuclear antigen loader complex, Ctf18-replication factor C, stimulates DNA polymerase eta activity. J Biol Chem. 2007 Jul 20;282(29):20906-14. PMID:17545166 doi:10.1074/jbc.M610102200
- ↑ Ogi T, Limsirichaikul S, Overmeer RM, Volker M, Takenaka K, Cloney R, Nakazawa Y, Niimi A, Miki Y, Jaspers NG, Mullenders LH, Yamashita S, Fousteri MI, Lehmann AR. Three DNA polymerases, recruited by different mechanisms, carry out NER repair synthesis in human cells. Mol Cell. 2010 Mar 12;37(5):714-27. doi: 10.1016/j.molcel.2010.02.009. PMID:20227374 doi:http://dx.doi.org/10.1016/j.molcel.2010.02.009
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