Histone sumoylation is associated with transcriptional repression

Yuzuru Shiio, Robert N. Eisenman

Research output: Contribution to journalArticlepeer-review

537 Scopus citations


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
Issue number23
StatePublished - Nov 11 2003
Externally publishedYes

ASJC Scopus subject areas

  • General


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