Molecular and Cellular Biology, June 2006, p. 3999-4005, Vol. 26, No. 11
0270-7306/06/$08.00+0 doi:10.1128/MCB.00293-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Sealy Center for Molecular Science, University of Texas Medical Branch, Galveston, Texas
Received 16 February 2006/ Returned for modification 8 March 2006/ Accepted 9 March 2006
Treatment of Saccharomyces cerevisiae and human cells with DNA-damaging agents such as UV light or 4-nitroquinoline-1-oxide induces polyubiquitylation of the largest RNA polymerase II (Pol II) subunit, Rpb1, which results in rapid Pol II degradation by the proteasome. Here we identify a novel role for the yeast Elc1 protein in mediating Pol II polyubiquitylation and degradation in DNA-damaged yeast cells and propose the involvement of a ubiquitin ligase, of which Elc1 is a component, in this process. In addition, we present genetic evidence for a possible involvement of Elc1 in Rad7-Rad16-dependent nucleotide excision repair (NER) of lesions from the nontranscribed regions of the genome and suggest a role for Elc1 in increasing the proficiency of repair of nontranscribed DNA, where as a component of the Rad7-Rad16-Elc1 ubiquitin ligase, it would promote the efficient turnover of the NER ensemble from the lesion site in a Rad23-19S proteasomal complex-dependent reaction.
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