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

Science 318, 1780-1782 (2007)
DOI
Open Access Green as soon as Postprint is submitted to ZB.
RNA polymerase II is distinguished by its large carboxyl-terminal repeat domain (CTD), composed of repeats of the consensus heptapeptide Tyr1-Ser2-Pro3-Thr4-Ser5-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.
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Publication type Article: Journal article
Document type Scientific Article
ISSN (print) / ISBN 0036-8075
e-ISSN 1095-9203
Journal Science
Quellenangaben Volume: 318, Issue: 5857, Pages: 1780-1782 Article Number: , Supplement: ,
Publisher American Association for the Advancement of Science (AAAS)
Reviewing status Peer reviewed