Transcription of protein-coding genes can be reconstituted on naked DNA with only the general transcription factors and RNA polymerase II. However, this minimal system cannot transcribe DNA packaged into chromatin, indicating that accessory factors may facilitate access to DNA. One such factor, FACT (facilitates chromatin transcription), interacts specifically with histones H2A/H2B to effect nucleosome disassembly and transcription elongation. FACT is composed of an 80 kDa subunit and a 140 kDa subunit, the latter of which is the protein encoded by this gene.[3]
↑Orphanides G, LeRoy G, Chang CH, Luse DS, Reinberg D (Mar 1998). "FACT, a factor that facilitates transcript elongation through nucleosomes". Cell. 92 (1): 105–16. doi:10.1016/S0092-8674(00)80903-4. PMID9489704.
↑Keller DM, Zeng X, Wang Y, Zhang QH, Kapoor M, Shu H, Goodman R, Lozano G, Zhao Y, Lu H (Mar 2001). "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1". Mol Cell. 7 (2): 283–92. doi:10.1016/S1097-2765(01)00176-9. PMID11239457.
↑Kitagawa H, Fujiki R, Yoshimura K, Mezaki Y, Uematsu Y, Matsui D, Ogawa S, Unno K, Okubo M, Tokita A, Nakagawa T, Ito T, Ishimi Y, Nagasawa H, Matsumoto T, Yanagisawa J, Kato S (Jun 2003). "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome". Cell. 113 (7): 905–17. doi:10.1016/S0092-8674(03)00436-7. PMID12837248.
Further reading
LeRoy G, Orphanides G, Lane WS, Reinberg D (1998). "Requirement of RSF and FACT for transcription of chromatin templates in vitro". Science. 282 (5395): 1900–4. doi:10.1126/science.282.5395.1900. PMID9836642.
Orphanides G, Wu WH, Lane WS, Hampsey M, Reinberg D (1999). "The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins". Nature. 400 (6741): 284–8. doi:10.1038/22350. PMID10421373.
Kang SW, Kuzuhara T, Horikoshi M (2000). "Functional interaction of general transcription initiation factor TFIIE with general chromatin factor SPT16/CDC68". Genes Cells. 5 (4): 251–63. doi:10.1046/j.1365-2443.2000.00323.x. PMID10792464.
Wada T, Orphanides G, Hasegawa J, Kim DK, Shima D, Yamaguchi Y, Fukuda A, Hisatake K, Oh S, Reinberg D, Handa H (2000). "FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH". Mol. Cell. 5 (6): 1067–72. doi:10.1016/S1097-2765(00)80272-5. PMID10912001.
Keller DM, Lu H (2003). "p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex". J. Biol. Chem. 277 (51): 50206–13. doi:10.1074/jbc.M209820200. PMID12393879.
Kitagawa H, Fujiki R, Yoshimura K, Mezaki Y, Uematsu Y, Matsui D, Ogawa S, Unno K, Okubo M, Tokita A, Nakagawa T, Ito T, Ishimi Y, Nagasawa H, Matsumoto T, Yanagisawa J, Kato S (2003). "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome". Cell. 113 (7): 905–17. doi:10.1016/S0092-8674(03)00436-7. PMID12837248.
Tan BC, Lee SC (2004). "Nek9, a novel FACT-associated protein, modulates interphase progression". J. Biol. Chem. 279 (10): 9321–30. doi:10.1074/jbc.M311477200. PMID14660563.
Fryer CJ, White JB, Jones KA (2005). "Mastermind recruits CycC:CDK8 to phosphorylate the Notch ICD and coordinate activation with turnover". Mol. Cell. 16 (4): 509–20. doi:10.1016/j.molcel.2004.10.014. PMID15546612.