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Published online on October 24, 2003, 10.1073/pnas.1735528100
PNAS | November 11, 2003 | vol. 100 | no. 23 | 13225-13230


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From The Cover
Biochemistry
Histone sumoylation is associated with transcriptional repression

Yuzuru Shiio * {dagger}, and Robert N. Eisenman * {ddagger}

*Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98109-4417; and {dagger}Institute for Systems Biology, Seattle, WA 98103-8904

Contributed by Robert N. Eisenman, August 27, 2003

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.

Abbreviations: SUMO, small ubiquitin-related modifier; HDAC, histone deacetylase; HP1, heterochromatin protein 1; HA, hemagglutinin.

See Commentary on page 13118.

{ddagger} To whom correspondence should be addressed. E-mail: eisenman{at}fhcrc.org.


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Related Commentary in PNAS:

Histone modifications: Now summoning sumoylation
Dafna Nathan, David E. Sterner, and Shelley L. Berger
PNAS 2003 100: 13118-13120. [Extract] [Full Text]  



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