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Open Access Green as soon as Postprint is submitted to ZB.
Transcribing RNA polymerase II is phosphorylated at CTD residue serine-7.
Science 318, 1780-1782 (2007)
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
Publisher
American Association for the Advancement of Science (AAAS)
Non-patent literature
Publications
Reviewing status
Peer reviewed