Histone methyltransferase

SUMO protein

Histone methylation

Biology

Histone code

Histone H1

Promoter

Gene

Gene expression

Chromatin remodeling

DNA methylation

Ubiquitin

Histone H2A

RNA polymerase II

Histone

Nucleosome

Cell biology

Genetics

Histone-modifying enzymes

Chromatin

Nucleic Acids Research

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.

Histone sumoylation and chromatin dynamics