Phosphorylation of RNA polymerase by the murine homologue of the cell-cycle control protein cdc2

Lars J. Cisek; Jeffry L. Corden

doi:10.1038/339679a0

Phosphorylation of RNA polymerase by the murine homologue of the cell-cycle control protein cdc2

Lars J. Cisek, Jeffry L. Corden

School of Medicine

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Abstract

Actively transcribing eukaryotic RNA polymerase II is highly phosphorylated on its repetitive carboxyl-terminal domain. We have isolated a protein kinase that phosphorylates serine residues in this repetitive domain. A component of this kinase is cdc2, the product of a cell-cycle control gene previously shown to be a component of M-phase-promoting factor and M-phase-specific histone H1 kinase. This observation suggests a role for the cdc2 protein kinase in transcriptional regulation.

Original language	English (US)
Pages (from-to)	679-684
Number of pages	6
Journal	Nature
Volume	339
Issue number	6227
DOIs	https://doi.org/10.1038/339679a0
State	Published - Jan 1 1989

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AB - Actively transcribing eukaryotic RNA polymerase II is highly phosphorylated on its repetitive carboxyl-terminal domain. We have isolated a protein kinase that phosphorylates serine residues in this repetitive domain. A component of this kinase is cdc2, the product of a cell-cycle control gene previously shown to be a component of M-phase-promoting factor and M-phase-specific histone H1 kinase. This observation suggests a role for the cdc2 protein kinase in transcriptional regulation.

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Phosphorylation of RNA polymerase by the murine homologue of the cell-cycle control protein cdc2

Abstract

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