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The Histone Acetyltransferase Mst2 Protects Active Chromatin from Epigenetic Silencing by Acetylating the Ubiquitin Ligase Brl1.

Abstract：

:Faithful propagation of functionally distinct chromatin states is crucial for maintaining cellular identity, and its breakdown can lead to diseases such as cancer. Whereas mechanisms that sustain repressed states have been intensely studied, regulatory circuits that protect active chromatin from inactivating signals are not well understood. Here we report a positive feedback loop that preserves the transcription-competent state of RNA polymerase II-transcribed genes. We found that Pdp3 recruits the histone acetyltransferase Mst2 to H3K36me3-marked chromatin. Thereby, Mst2 binds to all transcriptionally active regions genome-wide. Besides acetylating histone H3K14, Mst2 also acetylates Brl1, a component of the histone H2B ubiquitin ligase complex. Brl1 acetylation increases histone H2B ubiquitination, which positively feeds back on transcription and prevents ectopic heterochromatin assembly. Our work uncovers a molecular pathway that secures epigenome integrity and highlights the importance of opposing feedback loops for the partitioning of chromatin into transcriptionally active and inactive states.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Flury V,Georgescu PR,Iesmantavicius V,Shimada Y,Kuzdere T,Braun S,Bühler M

doi

10.1016/j.molcel.2017.05.026

subject

Has Abstract

pub_date

2017-07-20 00:00:00

pages

294-307.e9

issue

2

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(17)30366-0

journal_volume

67

pub_type

杂志文章

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