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Serine-7 of the RNA polymerase II CTD is specifically required for snRNA gene expression.

ABSTRACT: RNA polymerase II (Pol II) transcribes genes that encode proteins and noncoding small nuclear RNAs (snRNAs). The carboxyl-terminal repeat domain (CTD) of the largest subunit of mammalian RNA Pol II, comprising tandem repeats of the heptapeptide consensus Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7, is required for expression of both gene types. We show that mutation of serine-7 to alanine causes a specific defect in snRNA gene expression. We also present evidence that phosphorylation of serine-7 facilitates interaction with the snRNA gene-specific Integrator complex. These findings assign a biological function to this amino acid and highlight a gene type-specific requirement for a residue within the CTD heptapeptide, supporting the existence of a CTD code.

SUBMITTER: Egloff S

PROVIDER: S-EPMC2263945 | biostudies-literature | 2007 Dec

REPOSITORIES: biostudies-literature

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Serine-7 of the RNA polymerase II CTD is specifically required for snRNA gene expression.

Egloff Sylvain S O'Reilly Dawn D Chapman Rob D RD Taylor Alice A Tanzhaus Katrin K Pitts Laura L Eick Dirk D Murphy Shona S

Science (New York, N.Y.) 20071201 5857

RNA polymerase II (Pol II) transcribes genes that encode proteins and noncoding small nuclear RNAs (snRNAs). The carboxyl-terminal repeat domain (CTD) of the largest subunit of mammalian RNA Pol II, comprising tandem repeats of the heptapeptide consensus Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7, is required for expression of both gene types. We show that mutation of serine-7 to alanine causes a specific defect in snRNA gene expression. We also present evidence that phosphorylation of serine-7 facilita ...[more]

PMID: 18079403

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Gene-specific RNA polymerase II phosphorylation and the CTD code.

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CTD serine-2 plays a critical role in splicing and termination factor recruitment to RNA polymerase II in vivo.

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