CTD Tyrosine Phosphorylation Impairs Termination Factor Recruitment to RNA Polymerase II-Reference-Cited by-同舟云学术

CTD Tyrosine Phosphorylation Impairs Termination Factor Recruitment to RNA Polymerase II

Published:2012-06-29 Issue:6089 Volume:336 Page:1723-1725
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Mayer Andreas¹,Heidemann Martin²,Lidschreiber Michael¹,Schreieck Amelie¹,Sun Mai¹,Hintermair Corinna²,Kremmer Elisabeth³,Eick Dirk²,Cramer Patrick¹

Affiliation:

1. Gene Center and Department of Biochemistry, Center for Integrated Protein Science Munich (CIPSM), Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25, 81377 Munich, Germany.

2. Department of Molecular Epigenetics, Helmholtz Zentrum München and CIPSM, Marchioninistrasse 25, 81377 Munich, Germany.

3. Institute of Molecular Immunology, Helmholtz Zentrum München, Marchioninistrasse 25, 81377 Munich, Germany.

Abstract

Don't Terminate Me! DNA transcription progresses through three phases—initiation, elongation, and termination—of messenger RNA chains. The transcribing enzyme, RNA polymerase (Pol) II, recruits factors that assist in each of these phases. Mayer et al. (p. 1723 ) now show that the C-terminal domain (CTD) of actively elongating Pol II is phosphorylated at conserved tyrosine residues. This modification impairs recruitment of termination factors. Factor exchange on the transcribing polymerase enzyme may be explained by an extended CTD code that is based on differential phosphorylation of the tyrosines and two well-characterized serine residues in the CTD.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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