Document Detail


Growth-related changes in phosphorylation of yeast RNA polymerase II.
MedLine Citation:
PMID:  9468530     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The largest subunit of RNA polymerase II contains a unique C-terminal domain (CTD) consisting of tandem repeats of the consensus heptapeptide sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. Two forms of the largest subunit can be separated by SDS-polyacrylamide gel electrophoresis. The faster migrating form termed IIA contains little or no phosphate on the CTD, whereas the slower migrating II0 form is multiply phosphorylated. CTD kinases with different phosphoryl acceptor specificities are able to convert IIA to II0 in vitro, and different phosphoisomers have been identified in vivo. In this paper we report the binding specificities of a set of monoclonal antibodies that recognize different phosphoepitopes on the CTD. Monoclonal antibodies like H5 recognize phosphoserine in position 2, whereas monoclonal antibodies like H14 recognize phosphoserine in position 5. The relative abundance of these phosphoepitopes changes when growing yeast enter stationary phase or are heat-shocked. These results indicate that phosphorylation of different CTD phosphoacceptor sites are independently regulated in response to environmental signals.
Authors:
M Patturajan; R J Schulte; B M Sefton; R Berezney; M Vincent; O Bensaude; S L Warren; J L Corden
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  273     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1998 Feb 
Date Detail:
Created Date:  1998-03-19     Completed Date:  1998-03-19     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  4689-94     Citation Subset:  IM    
Affiliation:
Department of Molecular Biology and Genetics, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Antibodies, Monoclonal / immunology
Epitopes / immunology
Mice
Oligopeptides / immunology,  metabolism
Phosphorylation
RNA Polymerase II / metabolism*
Recombinant Fusion Proteins / metabolism
Saccharomyces cerevisiae / enzymology*,  growth & development
Substrate Specificity
Chemical
Reg. No./Substance:
0/Antibodies, Monoclonal; 0/Epitopes; 0/Oligopeptides; 0/Recombinant Fusion Proteins; EC 2.7.7.-/RNA Polymerase II

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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