H2B ubiquitylation acts as a barrier to Ctk1 nucleosomal recruitment prior to removal by Ubp8 within a SAGA-related complex.

H2B ubiquitylation acts as a barrier to Ctk1 nucleosomal recruitment prior to removal by Ubp8 within a SAGA-related complex. Research Abstract Details 

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H2B ubiquitylation acts as a barrier to Ctk1 nucleosomal recruitment prior to removal by Ubp8 within a SAGA-related complex. Abstract Text:

Anastasia Wyce,Tiaojiang Xiao,Kelly A Whelan,Christine Kosman,Wendy Walter,Dirk Eick,Timothy R Hughes,Nevan J Krogan,Brian D Strahl,Shelley L Berger,

Histone modifications play an important role in transcription. We previously studied histone H2B ubiquitylation on lysine 123 and subsequent deubiquitylation by SAGA-associated Ubp8. Unlike other histone modifications, both the addition and removal of ubiquitin are required for optimal transcription. Here we report that deubiquitylation of H2B is important for recruitment of a complex containing the kinase Ctk1, resulting in phosphorylation of the RNA polymerase II (Pol II) C-terminal domain (CTD), and for subsequent recruitment of the Set2 methyltransferase. We find that Ctk1 interacts with histones H2A and H2B, and that persistent H2B ubiquitylation disrupts these interactions. We further show that Ubp8 enters the GAL1 coding region through an interaction with Pol II. These findings reveal a mechanism by which H2B ubiquitylation acts as a barrier to Ctk1 association with active genes, while subsequent deubiquitylation by Ubp8 triggers Ctk1 recruitment at the appropriate point in activation.

H2B ubiquitylation acts as a barrier to Ctk1 nucleosomal recruitment prior to removal by Ubp8 within a SAGA-related complex. Publishing Authors By Initials

A Wyce,T Xiao,KA Whelan,C Kosman,W Walter,D Eick,TR Hughes,NJ Krogan,BD Strahl,SL Berger,

For similar proteins: ubiquitins: ubiquitin research abstracts see: proteins: ubiquitins: ubiquitin research

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H2B ubiquitylation acts as a barrier to Ctk1 nucleosomal recruitment prior to removal by Ubp8 within a SAGA-related complex. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Molecular cell

VOLUME: 27

Page Numbers: 275-88

Journal Abbreviation: Mol. Cell

ISSN: 1097-2765

DAY: 20

MONTH: Jul

YEAR: 2007

H2B ubiquitylation acts as a barrier to Ctk1 nucleosomal recruitment prior to removal by Ubp8 within a SAGA-related complex. Information

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LANGUAGE: eng

NlmUniqueID: 9802571

H2B ubiquitylation acts as a barrier to Ctk1 nucleosomal recruitment prior to removal by Ubp8 within a SAGA-related complex. Keywords Mesh Terms:

KEYWORDS: Ubiquitin

MESH TERMS: metabolism

Chemical & Substance for Abstract: H2B ubiquitylation acts as a barrier to Ctk1 nucleosomal recruitment prior to removal by Ubp8 within a SAGA-related complex. Information

Substance Name: UBP8 protein, S cerevisiae

Registry Number: EC 3.4.99.-

Grant and Affiliation Information for H2B ubiquitylation acts as a barrier to Ctk1 nucleosomal recruitment prior to removal by Ubp8 within a SAGA-related complex.

AFFILIATION: Gene Expression and Regulation Program, The Wistar Institute, Philadelphia, PA 19104, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: T32 GM008216

ACRONYM: GM

MEDLINETA: Mol Cell

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