A Histone H2A Deubiquitinase Complex Coordinating Histone Acetylation and H1 Dissociation in Transcriptional Regulation

RESEARCH PAPER:

Reference:

Ping Z., W. Zhou., J. Wang., J. Puc., K. A. Ohgi., H. Erdjument-Bromage., P. Tempst., C. K. Glass and M. G. Rosenfeld. 2007. Mol. Cell. 27: 609-621.

The complex regulation of gene activation and expression in eukaryotes is one of most important genetic features that make possible the inheritance of traits from generation to generation. Within the tight DNA packaging strategy relies also the capability of unwinding to become active and modified.

Histones are well known proteins that interact with DNA during its packaging. Modifications among them have been described as an essential part of the chromatin remodelling and transcriptional regulation. For many years, the study of DNA and chromatin remodelling has been extensively described, especially: the acetylation and methylation while the role of the ubiquitination still remained less obvious in spite the fact that was discovered quite long ago.

The following research article highlights the finding of the histone H2A deubiquitinase complex and its importance in the coordination of the histone acetylation and Histone 1 dissociation during the transcriptional regulation.

Their work, suggest that H2A deubiquitinase (2A-DUB) regulates transcription by coordinating the histone acetylation and deubiquitination provoking the destabilization of the linker histone H1 and the nucleosome, activity that is regulated by the degree of acetylation in the nucleosome.

Finally they conclude that the H2A ubiquitinase seems to represent a widely used mechanism for many regulatory transcripcional processes; in fact, with time it’s expected that more H2A ubiquitin ligases/ deubiquitinases will be discovered for specific groups of transcriptional units.

S. Pineda.