Histone sumoylation is associated with transcriptional repression

Yuzuru Shiio, Robert N. Eisenman

Research output: Contribution to journalArticle

449 Citations (Scopus)

Abstract

Histone proteins are subject to modifications, such as acetylation, methylation, phosphorylation, ubiquitination, glycosylation, and ADP ribosylation, some of which are known to play important roles in the regulation of chromatin structure and function. Here we report that histone H4 is modified by small ubiquitin-related modifier (SUMO) family proteins both in vivo and in vitro. H4 binds to the SUMO-conjugating enzyme (E2), UBC9, and can be sumoylated in an E1 (SUMO-activating enzyme)- and E2-dependent manner. We present evidence suggesting that histone sumoylation mediates gene silencing through recruitment of histone deacetylase and heterochromatin protein 1.

Original languageEnglish (US)
Pages (from-to)13225-13230
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume100
Issue number23
DOIs
StatePublished - Nov 11 2003
Externally publishedYes

Fingerprint

Sumoylation
Histones
Ubiquitin
Small Ubiquitin-Related Modifier Proteins
Histone Deacetylases
Ubiquitination
Gene Silencing
Enzymes
Acetylation
Glycosylation
Adenosine Diphosphate
Methylation
Chromatin
Phosphorylation
Proteins

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Histone sumoylation is associated with transcriptional repression. / Shiio, Yuzuru; Eisenman, Robert N.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 100, No. 23, 11.11.2003, p. 13225-13230.

Research output: Contribution to journalArticle

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