Biology:GTF2H5
 Generic protein structure example |
General transcription factor IIH subunit 5 is a protein that in humans is encoded by the GTF2H5 gene.[1][2]
Function
The GTF2H5(TTDA) gene encodes a small (71 amino acid) protein that stabilizes the multi-subunit transcription repair factor IIH(TFIIH). TFIIH plays a key role in a major DNA repair process, nucleotide excision repair (NER), by opening the DNA double helix after the initial recognition of damage in one strand. This step is followed by excision of the damaged region to generate a single-strand gap, and then repair synthesis, using the undamaged strand as template, to accurately fill in the gap. Disruption of the GTF2H5(TTDA) gene in a knockout mouse-model completely inactivates NER.[3] In humans, mutation in any one of four genes can give rise to the trichothiodystrophy phenotype. These genes are TTDN1, XPB, XPD and GTF2H5(TTDA).[3]
Interactions
GTF2H5 has been shown to interact with GTF2H2[1][4] and XPB.[1]
References
- ↑ 1.0 1.1 1.2 "A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A". Nat. Genet. 36 (7): 714–9. June 2004. doi:10.1038/ng1387. PMID 15220921.
- ↑ "Entrez Gene: GTF2H5 general transcription factor IIH, polypeptide 5". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=404672.
- ↑ 3.0 3.1 "TTDA: big impact of a small protein". Exp. Cell Res. 329 (1): 61–8. 2014. doi:10.1016/j.yexcr.2014.07.008. PMID 25016283.
- ↑ "Sublimiting concentration of TFIIH transcription/DNA repair factor causes TTD-A trichothiodystrophy disorder". Nat. Genet. 26 (3): 307–13. November 2000. doi:10.1038/81603. PMID 11062469.
Further reading
- "Sublimiting concentration of TFIIH transcription/DNA repair factor causes TTD-A trichothiodystrophy disorder". Nat. Genet. 26 (3): 307–13. 2000. doi:10.1038/81603. PMID 11062469.
- "p8/TTD-A as a repair-specific TFIIH subunit". Mol. Cell 21 (2): 215–26. 2006. doi:10.1016/j.molcel.2005.10.024. PMID 16427011.
- "Dynamic interaction of TTDA with TFIIH is stabilized by nucleotide excision repair in living cells". PLOS Biol. 4 (6): e156. 2006. doi:10.1371/journal.pbio.0040156. PMID 16669699.
- "Solution structure and self-association properties of the p8 TFIIH subunit responsible for trichothiodystrophy". J. Mol. Biol. 368 (2): 473–80. 2007. doi:10.1016/j.jmb.2007.02.020. PMID 17350038.
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