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Open Access Green as soon as Postprint is submitted to ZB.
CTD tyrosine phosphorylation impairs termination factor recruitment to RNA polymerase II.
Science 336, 1723-1725 (2012)
In different phases of the transcription cycle, RNA polymerase (Pol) II recruits various factors via its C-terminal domain (CTD), which consists of conserved heptapeptide repeats with the sequence Tyr(1)-Ser(2)-Pro(3)-Thr(4)-Ser(5)-Pro(6)-Ser(7). We show that the CTD of transcribing yeast Pol II is phosphorylated at Tyr(1), in addition to Ser(2), Thr(4), Ser(5), and Ser(7). Tyr(1) phosphorylation stimulates binding of elongation factor Spt6 and impairs recruitment of termination factors Nrd1, Pcf11, and Rtt103. Tyr(1) phosphorylation levels rise downstream of the transcription start site and decrease before the polyadenylation site, largely excluding termination factors from gene bodies. These results show that CTD modifications trigger and block factor recruitment and lead to an extended CTD code that explains transcription cycle coordination on the basis of differential phosphorylation of Tyr(1), Ser(2), and Ser(5).
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
ELONGATION-FACTOR SPT6; TANDEM SH2 DOMAIN; TRANSCRIPTION TERMINATION; S. CEREVISIAE; CODE; COMPLEX; PROTEIN; IICTD; ASSOCIATION; SERINE-7
ISSN (print) / ISBN
0036-8075
e-ISSN
1095-9203
Journal
Science
Quellenangaben
Volume: 336,
Issue: 6089,
Pages: 1723-1725
Publisher
American Association for the Advancement of Science (AAAS)
Non-patent literature
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Reviewing status
Peer reviewed