Growth-related changes in phosphorylation of yeast RNA polymerase II

Meera Patturajan, Roberta J. Schulte, Bartholomew M. Sefton, Ronald Berezney, Michel Vincent, Olivier Bensaude, Stephen L. Warren, Jeffry L. Corden

Research output: Contribution to journalArticlepeer-review

Abstract

The largest subunit of RNA polymerase H contains a unique C-terminal domain (CTD) consisting of tandem repeats of the consensus heptapeptide sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. To forms of the largest subunit can be separated by SDS-polyacrylamide gel electrophoresis. The faster migrating form termed HA 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.

Original languageEnglish (US)
Pages (from-to)4689-4694
Number of pages6
JournalJournal of Biological Chemistry
Volume273
Issue number8
DOIs
StatePublished - Feb 20 1998

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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