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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.

Original publication

DOI

10.1126/science.1145989

Type

Journal article

Journal

Science

Publication Date

14/12/2007

Volume

318

Pages

1777 - 1779

Keywords

Alanine, Amino Acid Sequence, Cell Line, Consensus Sequence, Gene Expression Regulation, Heterogeneous-Nuclear Ribonucleoproteins, Humans, Mutation, Oligopeptides, Phosphorylation, Protein Structure, Tertiary, Protein Subunits, RNA Polymerase II, RNA Processing, Post-Transcriptional, RNA, Messenger, RNA, Small Nuclear, Serine, Templates, Genetic, Transcription, Genetic