Construction and analysis of yeast RNA polymerase II CTD deletion and substitution mutations

M. L. West, J. L. Corden

Research output: Contribution to journalArticlepeer-review

Abstract

The carboxyl-terminal domain (CTD) of the RNA polymerase II largest subunit plays an essential but poorly understood role in transcription. The CTD is highly phosphorylated in vivo and this modification may be important in the transition from transcription initiation to elongation. We report here the development of a strategy for creating novel yeast CTDs. We have used this approach to show that the minimum viable CTD in yeast contains eight consensus (Tyr1,Ser3,Pro3,Thr4,Ser5,Pro6,Ser7) heptapeptide repeats. Substitution of alanine or glutamate for serines in positions two or five is lethal. In addition, changing tyrosine in position one to phenylalanine is lethal. The effects of mutations that alter potential phosphorylation sites are consistent with a requirement for CTD phosphorylation in vivo.

Original languageEnglish (US)
Pages (from-to)1223-1233
Number of pages11
JournalGenetics
Volume140
Issue number4
StatePublished - 1995

ASJC Scopus subject areas

  • Genetics

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