POLE4
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Polymerase (DNA-directed), epsilon 4, accessory subunit is a protein that in humans is encoded by the POLE4 gene.[1]
Function
POLE4 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complexes for DNA transcription, replication, and packaging.[1]
References
Further reading
- Post SM, Tomkinson AE, Lee EY (2003). "The human checkpoint Rad protein Rad17 is chromatin-associated throughout the cell cycle, localizes to DNA replication sites, and interacts with DNA polymerase epsilon". Nucleic Acids Res. 31 (19): 5568–75. doi:10.1093/nar/gkg765. PMC 206465. PMID 14500819.
- Li Y, Pursell ZF, Linn S (2000). "Identification and cloning of two histone fold motif-containing subunits of HeLa DNA polymerase epsilon". J. Biol. Chem. 275 (30): 23247–52. doi:10.1074/jbc.M002548200. PMID 10801849.
- Wang YL, Faiola F, Xu M, Pan S, Martinez E (2008). "Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel NC2-like histone fold module that interacts with the TATA-binding protein". J. Biol. Chem. 283 (49): 33808–15. doi:10.1074/jbc.M806936200. PMC 2590711. PMID 18838386.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
This article on a gene on human chromosome 2 is a stub. You can help Wikipedia by expanding it. |