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Histone sumoylation is associated with transcriptional repression.

Shiio, Yuzuru and Eisenman, Robert N (2003) Histone sumoylation is associated with transcriptional repression. Proceedings of the National Academy of Sciences of the United States of America, 100 (23). pp. 13225-13230. ISSN 0027-8424

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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.

Item Type: Article or Abstract
Additional Information: This article is freely available in PubMed Central and at the journal's website.
DOI: 10.1073/pnas.1735528100
PubMed ID: 14578449
PMCID: PMC263760
Grant Numbers: R01CA57138, Interdisciplinary Research Training Fellowship
Keywords or MeSH Headings: Animals; Binding Sites; Cell Line; Chromatin/metabolism; Chromosomal Proteins, Non-Histone/metabolism; Glutathione Transferase/metabolism; Histone Deacetylases/metabolism; Histones/metabolism; Humans; Immunoblotting; Luciferases/metabolism; Models, Genetic; Precipitin Tests; Protein Binding; Repressor Proteins/metabolism; Small Ubiquitin-Related Modifier Proteins/metabolism; Subcellular Fractions/metabolism; Transcription, Genetic;
Subjects: Molecules > Chromosomes > Chromatin
Cellular and Organismal Processes > Genetic processes > Transcription
Depositing User: Library Staff
Date Deposited: 24 Nov 2008 19:28
Last Modified: 07 May 2010 21:51

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