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In vivo interactions of TTDA mutant proteins within TFIIH.

Authors
  • Nonnekens, Julie
  • Cabantous, Stéphanie
  • Slingerland, Joris
  • Mari, Pierre-Olivier
  • Giglia-Mari, Giuseppina
Type
Published Article
Journal
Journal of Cell Science
Publisher
The Company of Biologists
Publication Date
Aug 01, 2013
Volume
126
Issue
Pt 15
Pages
3278–3283
Identifiers
DOI: 10.1242/jcs.126839
PMID: 23729738
Source
Medline
Keywords
License
Unknown

Abstract

Trichothiodystrophy group A (TTD-A) patients carry a mutation in the transcription factor II H (TFIIH) subunit TTDA. Using a novel in vivo tripartite split-GFP system, we show that TTDA interacts with the TFIIH subunit p52 and the p52-TTDA-GFP product is incorporated into TFIIH. p52-TTDA-GFP is able to bind DNA and is recruited to UV-damaged DNA. Furthermore, we show that two patient-mutated TTDA proteins can interact with p52, are able to bind to the DNA and can localize to damaged DNA. Our findings give new insights into the behavior of TTDA within the context of a living cell and thereby shed light on the complex phenotype of TTD-A patients.

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