Histone sumoylation and chromatin dynamics | Zendy

HongYeoul Ryu | Zendy; Mark Hochstrasser | Zendy

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Histone sumoylation and chromatin dynamics

Author(s) -

HongYeoul Ryu,

Mark Hochstrasser

Publication year - 2021

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/gkab280

Subject(s) - sumo protein , biology , chromatin , histone code , histone h2a , histone , histone methyltransferase , chromatin remodeling , microbiology and biotechnology , histone h1 , histone methylation , rna polymerase ii , genetics , histone modifying enzymes , ubiquitin , gene , dna methylation , gene expression , nucleosome , promoter

Chromatin structure and gene expression are dynamically controlled by post-translational modifications (PTMs) on histone proteins, including ubiquitylation, methylation, acetylation and small ubiquitin-like modifier (SUMO) conjugation. It was initially thought that histone sumoylation exclusively suppressed gene transcription, but recent advances in proteomics and genomics have uncovered its diverse functions in cotranscriptional processes, including chromatin remodeling, transcript elongation, and blocking cryptic initiation. Histone sumoylation is integral to complex signaling codes that prime additional histone PTMs as well as modifications of the RNA polymerase II carboxy-terminal domain (RNAPII-CTD) during transcription. In addition, sumoylation of histone variants is critical for the DNA double-strand break (DSB) response and for chromosome segregation during mitosis. This review describes recent findings on histone sumoylation and its coordination with other histone and RNAPII-CTD modifications in the regulation of chromatin dynamics.

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