Transcribing RNA polymerase II is phosphorylated at CTD residue serine-7

Rob D. Chapman, Martin Heidemann, Thomas K. Albert, Reinhard Mailhammer, Andrew Flatley, Michael Meisterernst, Elisabeth Kremmer, Dirk Eick

Research output: Contribution to journalArticlepeer-review

240 Scopus citations

Abstract

RNA polymerase II is distinguished by its large carboxyl-terminal repeat domain (CTD), composed of repeats of the consensus heptapeptide Tyr 1-Ser2-Pro3-Thr4-Ser 5-Pro6-Ser7. Differential phosphorylation of serine-2 and serine-5 at the 5′ and 3′ regions of genes appears to coordinate the localization of transcription and RNA processing factors to the elongating polymerase complex. Using monoclonal antibodies, we reveal serine-7 phosphorylation on transcribed genes. This position does not appear to be phosphorylated in CTDs of less than 20 consensus repeats. The position of repeats where serine-7 is substituted influenced the appearance of distinct phosphorylated forms, suggesting functional differences between CTD regions. Our results indicate that restriction of serine-7 epitopes to the Linker-proximal region limits CTD phosphorylation patterns and is a requirement for optimal gene expression.

Original languageEnglish
Pages (from-to)1780-1782
Number of pages3
JournalScience
Volume318
Issue number5857
DOIs
StatePublished - 14 Dec 2007
Externally publishedYes

Fingerprint

Dive into the research topics of 'Transcribing RNA polymerase II is phosphorylated at CTD residue serine-7'. Together they form a unique fingerprint.

Cite this