Document Detail

Elongating RNA polymerase II is disassembled through specific degradation of its largest but not other subunits in response to DNA damage in vivo.
MedLine Citation:
PMID:  18195014     Owner:  NLM     Status:  MEDLINE    
Although previous biochemical studies have demonstrated global degradation of the largest subunit, Rpb1p, of RNA polymerase II in response to DNA damage, it is still not clear whether the initiating or elongating form of Rpb1p is targeted for degradation in vivo. Further, whether other components of RNA polymerase II are degraded in response to DNA damage remains unknown. Here, we show that the Rpb1p subunit of the elongating, but not initiating, form of RNA polymerase II is degraded at the active genes in response to 4-nitroquinoline-1-oxide-induced DNA damage in Saccharomyces cerevisiae. However, other subunits of RNA polymerase II are not degraded in response to DNA damage. Further, we show that Rpb1p is essential for RNA polymerase II assembly at the active gene, and thus, the degradation of Rpb1p following DNA damage disassembles elongating RNA polymerase II. Taken together, our data demonstrate that Rpb1p but not other subunits of elongating RNA polymerase II is specifically degraded in response to DNA damage, and such a degradation of Rpb1p is critical for the disassembly of elongating RNA polymerase II at the DNA lesion in vivo.
Shivani Malik; Shruti Bagla; Priyasri Chaurasia; Zhen Duan; Sukesh R Bhaumik
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-01-14
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  283     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2008 Mar 
Date Detail:
Created Date:  2008-03-10     Completed Date:  2008-05-20     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  6897-905     Citation Subset:  IM    
Department of Biochemistry and Molecular Biology, Southern Illinois University, School of Medicine, Carbondale, Illinois 62901, USA.
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MeSH Terms
4-Nitroquinoline-1-oxide / pharmacology
DNA Damage*
DNA Repair
Gene Expression Regulation, Fungal*
Genome, Fungal
Models, Biological
Mutagens / pharmacology
Open Reading Frames
RNA Polymerase II / chemistry,  physiology*
RNA-Binding Proteins / metabolism
Saccharomyces cerevisiae / enzymology*,  metabolism
Saccharomyces cerevisiae Proteins / metabolism
Time Factors
Transcription, Genetic
Transcriptional Activation
Reg. No./Substance:
0/Mutagens; 0/NGR1 protein, S cerevisiae; 0/RNA-Binding Proteins; 0/Saccharomyces cerevisiae Proteins; 56-57-5/4-Nitroquinoline-1-oxide; EC 2.7.7.-/RNA Polymerase II

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