Activation and regulation of H2B-Ubiquitin-dependent histone methyltransferases.

Abstract:

:Covalent modifications of histone proteins regulate a wide variety of cellular processes. Methylation of histone H3K79 and H3K4 is associated with active transcription and is catalyzed by Dot1L and Set1, respectively. Both Dot1L and Set1 are activated by prior ubiquitination of histone H2B on K120 in a process termed 'histone crosstalk'. Recent structures of Dot1L bound to a ubiquitinated nucleosome revealed how Dot1L is activated by ubiquitin and how Dot1L distorts the nucleosome to access its substrate. Structures of Dot1L-interacting proteins have provided insight into how Dot1L is recruited to sites of active transcription. Cryo-EM and crystallographic studies of the complex of proteins associated with Set1 (COMPASS), uncovered the architecture of COMPASS and how Set1 is activated upon complex assembly.

journal_name

Curr Opin Struct Biol

authors

Worden EJ,Wolberger C

doi

10.1016/j.sbi.2019.05.009

subject

Has Abstract

pub_date

2019-12-01 00:00:00

pages

98-106

eissn

0959-440X

issn

1879-033X

pii

S0959-440X(19)30024-7

journal_volume

59

pub_type

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