RFC3

RFC3

Replication factor C (activator 1) 3, 38kDa, also known as RFC3, is a human gene.cite web | title = Entrez Gene: RFC3 replication factor C (activator 1) 3, 38kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5983| accessdate = ]

PBB_Summary
section_title =
summary_text = The elongation of primed DNA templates by DNA polymerase delta and DNA polymerase epsilon requires the accessory proteins proliferating cell nuclear antigen (PCNA) and replication factor C (RFC). RFC, also named activator 1, is a protein complex consisting of five distinct subunits of 140, 40, 38, 37, and 36 kDa. This gene encodes the 38 kDa subunit. This subunit is essential for the interaction between the 140 kDa subunit and the core complex that consists of the 36, 37, and 40 kDa subunits. Alternatively spliced transcript variants encoding distinct isoforms have been described.cite web | title = Entrez Gene: RFC3 replication factor C (activator 1) 3, 38kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5983| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Okumura K, Nogami M, Taguchi H, "et al." |title=Assignment of the 36.5-kDa (RFC5), 37-kDa (RFC4), 38-kDa (RFC3), and 40-kDa (RFC2) subunit genes of human replication factor C to chromosome bands 12q24.2-q24.3, 3q27, 13q12.3-q13, and 7q11.23. |journal=Genomics |volume=25 |issue= 1 |pages= 274–8 |year= 1995 |pmid= 7774928 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=O'Donnell M, Onrust R, Dean FB, "et al." |title=Homology in accessory proteins of replicative polymerases--E. coli to humans. |journal=Nucleic Acids Res. |volume=21 |issue= 1 |pages= 1–3 |year= 1993 |pmid= 8441605 |doi=
*cite journal | author=Uhlmann F, Cai J, Flores-Rozas H, "et al." |title=In vitro reconstitution of human replication factor C from its five subunits. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 13 |pages= 6521–6 |year= 1996 |pmid= 8692848 |doi=
*cite journal | author=Uhlmann F, Cai J, Gibbs E, "et al." |title=Deletion analysis of the large subunit p140 in human replication factor C reveals regions required for complex formation and replication activities. |journal=J. Biol. Chem. |volume=272 |issue= 15 |pages= 10058–64 |year= 1997 |pmid= 9092549 |doi=
*cite journal | author=Cujec TP, Cho H, Maldonado E, "et al." |title=The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 1817–23 |year= 1997 |pmid= 9121429 |doi=
*cite journal | author=Cai J, Gibbs E, Uhlmann F, "et al." |title=A complex consisting of human replication factor C p40, p37, and p36 subunits is a DNA-dependent ATPase and an intermediate in the assembly of the holoenzyme. |journal=J. Biol. Chem. |volume=272 |issue= 30 |pages= 18974–81 |year= 1997 |pmid= 9228079 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Ellison V, Stillman B |title=Reconstitution of recombinant human replication factor C (RFC) and identification of an RFC subcomplex possessing DNA-dependent ATPase activity. |journal=J. Biol. Chem. |volume=273 |issue= 10 |pages= 5979–87 |year= 1998 |pmid= 9488738 |doi=
*cite journal | author=Zhang G, Gibbs E, Kelman Z, "et al." |title=Studies on the interactions between human replication factor C and human proliferating cell nuclear antigen. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 5 |pages= 1869–74 |year= 1999 |pmid= 10051561 |doi=
*cite journal | author=Rauen M, Burtelow MA, Dufault VM, Karnitz LM |title=The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29767–71 |year= 2000 |pmid= 10884395 |doi= 10.1074/jbc.M005782200
*cite journal | author=Lindsey-Boltz LA, Bermudez VP, Hurwitz J, Sancar A |title=Purification and characterization of human DNA damage checkpoint Rad complexes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 20 |pages= 11236–41 |year= 2001 |pmid= 11572977 |doi= 10.1073/pnas.201373498
*cite journal | author=Griffith JD, Lindsey-Boltz LA, Sancar A |title=Structures of the human Rad17-replication factor C and checkpoint Rad 9-1-1 complexes visualized by glycerol spray/low voltage microscopy. |journal=J. Biol. Chem. |volume=277 |issue= 18 |pages= 15233–6 |year= 2002 |pmid= 11907025 |doi= 10.1074/jbc.C200129200
*cite journal | author=Ohta S, Shiomi Y, Sugimoto K, "et al." |title=A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein. |journal=J. Biol. Chem. |volume=277 |issue= 43 |pages= 40362–7 |year= 2002 |pmid= 12171929 |doi= 10.1074/jbc.M206194200
*cite journal | author=Maruyama T, Farina A, Dey A, "et al." |title=A Mammalian bromodomain protein, brd4, interacts with replication factor C and inhibits progression to S phase. |journal=Mol. Cell. Biol. |volume=22 |issue= 18 |pages= 6509–20 |year= 2002 |pmid= 12192049 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Merkle CJ, Karnitz LM, Henry-Sánchez JT, Chen J |title=Cloning and characterization of hCTF18, hCTF8, and hDCC1. Human homologs of a Saccharomyces cerevisiae complex involved in sister chromatid cohesion establishment. |journal=J. Biol. Chem. |volume=278 |issue= 32 |pages= 30051–6 |year= 2003 |pmid= 12766176 |doi= 10.1074/jbc.M211591200
*cite journal | author=Bermudez VP, Maniwa Y, Tappin I, "et al." |title=The alternative Ctf18-Dcc1-Ctf8-replication factor C complex required for sister chromatid cohesion loads proliferating cell nuclear antigen onto DNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 18 |pages= 10237–42 |year= 2003 |pmid= 12930902 |doi= 10.1073/pnas.1434308100
*cite journal | author=Zou L, Liu D, Elledge SJ |title=Replication protein A-mediated recruitment and activation of Rad17 complexes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 24 |pages= 13827–32 |year= 2004 |pmid= 14605214 |doi= 10.1073/pnas.2336100100
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285

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  • Replication factor C — The replication factor C, or RFC, is a five subunit protein complex that is required for DNA replication.The subunits of this heteropentamer are named Rfc1, Rfc2, Rfc3, Rfc4, and Rfc5 (in S. cerevisiae). RFC is used in eukaryotic replication as a …   Wikipedia

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