Open AccessHistone sumoylation is associated with transcriptional repression
Author(s) -
Yuzuru Shiio,
Robert N. Eisenman
Publication year - 2003
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.1735528100
Subject(s) - sumo protein , histone methyltransferase , histone h2a , histone code , histone modifying enzymes , histone , histone h4 , heterochromatin protein 1 , histone methylation , biology , chromatin , ezh2 , microbiology and biotechnology , histone deacetylase , histone h1 , histone deacetylase 2 , hdac11 , histone deacetylase 5 , ubiquitin , biochemistry , heterochromatin , dna methylation , gene expression , nucleosome , dna , gene
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom