Nucleic Acids Research, Vol 25, Issue 12 2274-2283, Copyright © 1997 by Oxford University Press
G Weeda, M Rossignol, RA Fraser, GS Winkler, W Vermeulen, LJ van't Veer, L Ma, JH Hoeijmakers and JM Egly
Mutations in the basal transcription initiation/DNA repair factor TFIIH are
responsible for three human disorders: xeroderma pigmentosum (XP), cockayne
syndrome (CS) and trichothiodystrophy (TTD). The non-repair features of CS
and TTD are thought to be due to a partial inactivation of the
transcription function of the complex. To search for proteins whose
interaction with TFIIH subunits is disturbed by mutations in patients we
used the yeast two-hybrid system and report the isolation of a novel XPB
interacting protein, SUG1. The interaction was validated in vivo and in
vitro in the following manner. (i) SUG1 interacts with XPB but not with the
other core TFIIH subunits in the two-hybrid assay. (ii) Physical
interaction is observed in a baculovirus co-expression system. (iii) In
fibroblasts under non-overexpression conditions a portion of SUG1 is bound
to the TFIIH holocomplex as deduced from co- purification,
immunopurification and nickel-chelate affinity chromatography using
functional tagged TFIIH. Furthermore, overexpression of SUG1 in normal
fibroblasts induced arrest of transcription and a chromatin collapse in
vivo. Interestingly, the interaction was diminished with a mutant form of
XPB, thus providing a potential link with the clinical features of XP-B
patients. Since SUG1 is an integral component of the 26S proteasome and may
be part of the mediator, our findings disclose a SUG1-dependent link
between TFIIH and the cellular machinery involved in protein
modelling/degradation.
ARTICLES
The XPB subunit of repair/transcription factor TFIIH directly interacts with SUG1, a subunit of the 26S proteasome and putative transcription factor
Department of Cell Biology, Medical Genetics Center, Erasmus University, Rotterdam, PO Box 1738, 3000 DR Rotterdam, The Netherlands. weeda@gen.fgg.eur.nl
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