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J Biol Chem, Vol. 273, Issue 9, 5184-5189, February 27, 1998
From the We have shown previously that UV radiation and
other DNA-damaging agents induce the ubiquitination of a portion of the
RNA polymerase II large subunit (Pol II LS). In the present study UV
irradiation of repair-competent fibroblasts induced a transient reduction of the Pol II LS level; new protein synthesis restored Pol II
LS to the base-line level within 16-24 h. In repair-deficient xeroderma pigmentosum cells, UV radiation-induced ubiquitination of Pol
II LS was followed by a sustained reduction of Pol II LS level. In both
normal and xeroderma pigmentosum cells, the ubiquitinated Pol II LS had
a hyperphosphorylated COOH-terminal domain (CTD), which is
characteristic of elongating Pol II. The portion of Pol II LS whose
steady-state level diminished most quickly had a relatively hypophosphorylated CTD. The ubiquitinated residues did not map to the
CTD. Importantly, UV-induced reduction of Pol II LS level in
repair-competent or -deficient cells was inhibited by the proteasome inhibitors lactacystin or MG132. These data demonstrate that UV-induced ubiquitination of Pol II LS is followed by its degradation in the
proteasome. These results suggest, contrary to a current model of
transcription-coupled DNA repair, that elongating Pol II complexes which arrest at intragenic DNA lesions may be aborted rather than resuming elongation after repair takes place.
Ultraviolet Radiation-induced Ubiquitination and Proteasomal
Degradation of the Large Subunit of RNA Polymerase II
IMPLICATIONS FOR TRANSCRIPTION-COUPLED DNA REPAIR
,,
Department of Pathology, Albert Einstein
College of Medicine, Bronx, New York 10461, the
§ Department of Molecular Biology and Genetics, The Johns
Hopkins University School of Medicine, Baltimore, Maryland 21205, and
¶ NeXstar Pharmaceuticals, Boulder, Colorado 80301
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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