Format

Send to

Choose Destination
See comment in PubMed Commons below
Biochemistry. 2012 Jul 31;51(30):5873-5. Epub 2012 Jul 20.

Rad26p, a transcription-coupled repair factor, promotes the eviction and prevents the reassociation of histone H2A-H2B dimer during transcriptional elongation in vivo.

Author information

1
Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL 62901, USA.

Abstract

We have recently demonstrated the formation of an atypical histone H2A-H2B dimer-enriched chromatin at the coding sequence of the active gene in the absence of Rad26p in vivo. However, the mechanisms for such a surprising observation remain unknown. Here, using a ChIP assay, we demonstrate that Rad26p promotes the eviction of histone H2A-H2B dimer and prevents the reassociation of the dimer with naked DNA in the wake of elongating RNA polymerase II at the coding sequence of the active GAL1 gene. Thus, the absence of Rad26p leads to the generation of an atypical histone H2A-H2B dimer-enriched chromatin at the active coding sequence in vivo.

PMID:
22794311
PMCID:
PMC3447996
DOI:
10.1021/bi3005768
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for American Chemical Society Icon for PubMed Central
    Loading ...
    Support Center