Biology:TADA2L
 Generic protein structure example |
Transcriptional adapter 2-alpha is a protein that in humans is encoded by the TADA2A gene.[1][2]
Function
Many DNA-binding transcriptional activator proteins enhance the initiation rate of RNA polymerase II-mediated gene transcription by interacting functionally with the general transcription machinery bound at the basal promoter. Adaptor proteins are usually required for this activation, possibly to acetylate and destabilize nucleosomes, thereby relieving chromatin constraints at the promoter. The protein encoded by this gene is a transcriptional activator adaptor and has been found to be part of the PCAF histone acetylase complex. Two transcript variants encoding different isoforms have been identified for this gene.[2]
Interactions
TADA2L has been shown to interact with GCN5L2,[3][4] TADA3L[5][6] and Myc.[7]
References
- ↑ "Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5". Molecular and Cellular Biology 16 (2): 593–602. Feb 1996. doi:10.1128/mcb.16.2.593. PMID 8552087.
- ↑ 2.0 2.1 "Entrez Gene: TADA2L transcriptional adaptor 2 (ADA2 homolog, yeast)-like". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6871.
- ↑ "Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex". Molecular and Cellular Biology 18 (3): 1349–58. Mar 1998. doi:10.1128/mcb.18.3.1349. PMID 9488450.
- ↑ "Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation". Molecular and Cellular Biology 17 (1): 519–27. Jan 1997. doi:10.1128/mcb.17.1.519. PMID 8972232.
- ↑ "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. Oct 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- ↑ "hADA3 is required for p53 activity". The EMBO Journal 20 (22): 6404–13. Nov 2001. doi:10.1093/emboj/20.22.6404. PMID 11707411.
- ↑ "c-Myc transformation domain recruits the human STAGA complex and requires TRRAP and GCN5 acetylase activity for transcription activation". The Journal of Biological Chemistry 278 (22): 20405–12. May 2003. doi:10.1074/jbc.M211795200. PMID 12660246.
Further reading
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. Jan 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation". Molecular and Cellular Biology 17 (1): 519–27. Jan 1997. doi:10.1128/mcb.17.1.519. PMID 8972232.
- "The human transcriptional adaptor genes TADA2L and GCN5L2 colocalize to chromosome 17q12-q21 and display a similar tissue expression pattern". Genomics 40 (3): 497–500. Mar 1997. doi:10.1006/geno.1996.4605. PMID 9073520.
- "Role of the Ada adaptor complex in gene activation by the glucocorticoid receptor". Molecular and Cellular Biology 17 (6): 3065–73. Jun 1997. doi:10.1128/mcb.17.6.3065. PMID 9154805.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. Oct 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "Histone-like TAFs within the PCAF histone acetylase complex". Cell 94 (1): 35–44. Jul 1998. doi:10.1016/S0092-8674(00)81219-2. PMID 9674425.
- "The 400 kDa subunit of the PCAF histone acetylase complex belongs to the ATM superfamily". Molecular Cell 2 (6): 869–75. Dec 1998. doi:10.1016/S1097-2765(00)80301-9. PMID 9885574.
- "hADA3 is required for p53 activity". The EMBO Journal 20 (22): 6404–13. Nov 2001. doi:10.1093/emboj/20.22.6404. PMID 11707411.
- "A novel human Ada2 homologue functions with Gcn5 or Brg1 to coactivate transcription". Molecular and Cellular Biology 23 (19): 6944–57. Oct 2003. doi:10.1128/MCB.23.19.6944-6957.2003. PMID 12972612.
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. Oct 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- "Structure and chromosomal DNA binding of the SWIRM domain". Nature Structural & Molecular Biology 12 (12): 1078–85. Dec 2005. doi:10.1038/nsmb1022. PMID 16299514.
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