Activation and regulation of H2B-Ubiquitin-dependent histone methyltransferases

Evan J. Worden, Cynthia Wolberger

Research output: Contribution to journalReview article

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.

Original languageEnglish (US)
Pages (from-to)98-106
Number of pages9
JournalCurrent Opinion in Structural Biology
Volume59
DOIs
StatePublished - Dec 1 2019

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Ubiquitin
Histones
Nucleosomes
Proteins
Histone Code
Ubiquitination
Methylation
Catalytic Domain
histone methyltransferase

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Activation and regulation of H2B-Ubiquitin-dependent histone methyltransferases. / Worden, Evan J.; Wolberger, Cynthia.

In: Current Opinion in Structural Biology, Vol. 59, 01.12.2019, p. 98-106.

Research output: Contribution to journalReview article

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