Transcriptomics

Dataset Information

241

ChIP-chip by array of termination factors Nrd1 and Rtt103, and CTD phosphorylated RNA polymerase II in yeast


ABSTRACT: ChIP-chip was performed to identify the genomic binding locations for the termination factors Nrd1, and Rtt103, and for RNA polymerase (Pol) II phosphorylated at the tyrosine 1 and threonine 4 position of its C-terminal domain (CTD). In different phases of the transcription cycle, Pol II recruits different factors via its CTD, which consists of heptapeptide repeats with the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. Here we show that the CTD of transcribing yeast Pol II is phosphorylated at Tyr1, and that this impairs recruitment of termination factors. Tyr1 phosphorylation levels rise downstream of the transcription start site (TSS), and decrease before the polyadenylation (pA) site. Tyr1-phosphorylated gene bodies are depleted of CTD-binding termination factors Nrd1, Pcf11, and Rtt103. Tyr1 phosphorylation blocks CTD binding by these termination factors, but stimulates binding of elongation factor Spt6. These results show that CTD modifications can not only stimulate but also block factor recruitment, and lead to an extended CTD code for transcription cycle coordination.

ORGANISM(S): Saccharomyces cerevisiae  

SUBMITTER: Michael Lidschreiber  

PROVIDER: E-MTAB-1060 | ArrayExpress | 2012-06-29

REPOSITORIES: ArrayExpress

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Publications

CTD tyrosine phosphorylation impairs termination factor recruitment to RNA polymerase II.

Mayer Andreas A   Heidemann Martin M   Lidschreiber Michael M   Schreieck Amelie A   Sun Mai M   Hintermair Corinna C   Kremmer Elisabeth E   Eick Dirk D   Cramer Patrick P  

Science (New York, N.Y.) 20120601 6089


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, Pc  ...[more]

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