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Reversible Phosphorylation of the C-terminal Domain of RNA Polymerase II

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Dahmus, Michael E.·1996·Journal of Biological Chemistry

Abstract

RNA polymerase (RNAP)1 II is responsible for the synthesis of pre-mRNA in eukaryotic cells. The subunit structure of RNAP II is similar to that of other RNAPs in that it is comprised of two large subunits with a molecular weight in excess of 100,000 and a collection of smaller subunits (1, 2). However, the largest subunit of RNAP II is unique in that it contains an unusual domain at its C terminus comprised of tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser (3). The consensus repeat has been conserved in evolution although the number of repeats present varies in different species.

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Metadata

Authors
Dahmus, M. E.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1996-08
Volume
271
Issue
32
Pages
19009-19012
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2072836045
Cited by
498
References
0
FWCI
13.24
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Reversible Phosphorylation of the C-terminal Domain of RNA Polymerase II. https://app.cochat.ai/papers/10.1074/jbc.271.32.19009
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Dahmus, M. E. (1996). Reversible Phosphorylation of the C-terminal Domain of RNA Polymerase II. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.271.32.19009

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.