Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
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.

Bibliography

Shiio, Y., & Eisenman, R. N. (2003). Histone sumoylation is associated with transcriptional repression. Proceedings of the National Academy of Sciences, 100(23), 13225–13230.

Dates
Type When
Created 21 years, 9 months ago (Nov. 16, 2003, 3:42 p.m.)
Deposited 3 years, 4 months ago (April 13, 2022, 3:40 a.m.)
Indexed 2 weeks, 4 days ago (Aug. 7, 2025, 4:53 a.m.)
Issued 21 years, 10 months ago (Oct. 24, 2003)
Published 21 years, 10 months ago (Oct. 24, 2003)
Published Online 21 years, 10 months ago (Oct. 24, 2003)
Published Print 21 years, 9 months ago (Nov. 11, 2003)
Funders 0

None

@article{Shiio_2003, title={Histone sumoylation is associated with transcriptional repression}, volume={100}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.1735528100}, DOI={10.1073/pnas.1735528100}, number={23}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Shiio, Yuzuru and Eisenman, Robert N.}, year={2003}, month=oct, pages={13225–13230} }