Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
|
pubmed:dateCreated |
1998-3-25
|
pubmed:abstractText |
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.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase II,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
27
|
pubmed:volume |
273
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
5184-9
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:9478972-Cell Line,
pubmed-meshheading:9478972-Cysteine Endopeptidases,
pubmed-meshheading:9478972-Cysteine Proteinase Inhibitors,
pubmed-meshheading:9478972-DNA Repair,
pubmed-meshheading:9478972-Humans,
pubmed-meshheading:9478972-Multienzyme Complexes,
pubmed-meshheading:9478972-Proteasome Endopeptidase Complex,
pubmed-meshheading:9478972-Protein Processing, Post-Translational,
pubmed-meshheading:9478972-RNA Polymerase II,
pubmed-meshheading:9478972-Transcription, Genetic,
pubmed-meshheading:9478972-Ubiquitins,
pubmed-meshheading:9478972-Ultraviolet Rays,
pubmed-meshheading:9478972-Xeroderma Pigmentosum
|
pubmed:year |
1998
|
pubmed:articleTitle |
Ultraviolet radiation-induced ubiquitination and proteasomal degradation of the large subunit of RNA polymerase II. Implications for transcription-coupled DNA repair.
|
pubmed:affiliation |
Department of Pathology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|