TAF1A
TATA box-binding protein-associated factor RNA polymerase I subunit A is an enzyme that in humans is encoded by the TAF1A gene.[1][2]
Function
Initiation of transcription by RNA polymerase I requires the formation of a complex composed of the TATA-binding protein (TBP) and three TBP-associated factors (TAFs) specific for RNA polymerase I. This complex, known as SL1, binds to the core promoter of ribosomal RNA genes to position the polymerase properly and acts as a channel for regulatory signals. This gene encodes the smallest SL1-specific TAF. Two transcripts encoding different isoforms have been identified.[2]
Interactions
TAF1A has been shown to interact with Acidic leucine-rich nuclear phosphoprotein 32 family member A[3] and Protein SET.[3]
References
- ↑ Comai L, Zomerdijk JC, Beckmann H, Zhou S, Admon A, Tjian R (December 1994). “Reconstitution of transcription factor SL1: exclusive binding of TBP by SL1 or TFIID subunits”. Science. 266 (5193): 1966–72. doi:10.1126/science.7801123. PMID 7801123.
- ↑ 2.0 2.1 “Entrez Gene: TAF1A TATA box binding protein (TBP)-associated factor, RNA polymerase I, A, 48kDa”.
- ↑ 3.0 3.1 Seo SB, McNamara P, Heo S, Turner A, Lane WS, Chakravarti D (January 2001). “Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein”. Cell. 104 (1): 119–30. doi:10.1016/S0092-8674(01)00196-9. PMID 11163245.
Further reading
- Rudloff U, Eberhard D, Tora L, Stunnenberg H, Grummt I (1994). “TBP-associated factors interact with DNA and govern species specificity of RNA polymerase I transcription”. EMBO J. 13 (11): 2611–6. PMC 395135. PMID 8013460.
- Di Pietro C, Rapisarda A, Amico V, Bonaiuto C, Viola A, Scalia M, Motta S, Amato A, Engel H, Messina A, Sichel G, Grzeschik K, Purrello M (2000). “Genomic localization of the human genes TAF1A, TAF1B and TAF1C, encoding TAF(I)48, TAF(I)63 and TAF(I)110 subunits of class I general transcription initiation factor SL1”. Cytogenet. Cell Genet. 89 (1–2): 133–6. doi:10.1159/000015592. PMID 10894955.
- Zhai W, Comai L (2000). “Repression of RNA polymerase I transcription by the tumor suppressor p53”. Mol. Cell. Biol. 20 (16): 5930–8. doi:10.1128/MCB.20.16.5930-5938.2000. PMC 86070. PMID 10913176.
- Seo SB, McNamara P, Heo S, Turner A, Lane WS, Chakravarti D (2001). “Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein”. Cell. 104 (1): 119–30. doi:10.1016/S0092-8674(01)00196-9. PMID 11163245.
- Miller G, Panov KI, Friedrich JK, Trinkle-Mulcahy L, Lamond AI, Zomerdijk JC (2001). “hRRN3 is essential in the SL1-mediated recruitment of RNA Polymerase I to rRNA gene promoters”. EMBO J. 20 (6): 1373–82. doi:10.1093/emboj/20.6.1373. PMC 145519. PMID 11250903.
- Dynes JL, Xu S, Bothner S, Lahti JM, Hori RT (2004). “The carboxyl-terminus directs TAF(I)48 to the nucleus and nucleolus and associates with multiple nuclear import receptors”. J. Biochem. 135 (3): 429–38. doi:10.1093/jb/mvh051. PMID 15113842.
- Yamamoto K, Yamamoto M, Hanada K, Nogi Y, Matsuyama T, Muramatsu M (2004). “Multiple protein-protein interactions by RNA polymerase I-associated factor PAF49 and role of PAF49 in rRNA transcription”. Mol. Cell. Biol. 24 (14): 6338–49. doi:10.1128/MCB.24.14.6338-6349.2004. PMC 434256. PMID 15226435.
- Grandori C, Gomez-Roman N, Felton-Edkins ZA, Ngouenet C, Galloway DA, Eisenman RN, White RJ (2005). “c-Myc binds to human ribosomal DNA and stimulates transcription of rRNA genes by RNA polymerase I”. Nat. Cell Biol. 7 (3): 311–8. doi:10.1038/ncb1224. PMID 15723054.
- Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). “Towards a proteome-scale map of the human protein-protein interaction network”. Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
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