Sumoylated human histone H4 prevents chromatin compaction by inhibiting long-range internucleosomal interactions.

ABSTRACT: The structure of eukaryotic chromatin directly influences gene function, and is regulated by chemical modifications of the core histone proteins. Modification of the human histone H4 N-terminal tail region by the small ubiquitin-like modifier protein, SUMO-3, is associated with transcription repression. However, the direct effect of sumoylation on chromatin structure and function remains unknown. Therefore, we employed a disulfide-directed strategy to generate H4 homogenously and site-specifically sumoylated at Lys-12 (suH4ss). Chromatin compaction and oligomerization assays with nucleosomal arrays containing suH4ss established that SUMO-3 inhibits array folding and higher order oligomerization, which underlie chromatin fiber formation. Moreover, the effect of sumoylation differed from tha

SUBMITTER: Dhall A 

PROVIDER: S-EPMC4256319 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature