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

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.

SUBMITTER: Malik S

PROVIDER: S-EPMC3447996 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature

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

Malik Shivani S Bhaumik Sukesh R SR

Biochemistry 20120720 30

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. ...[more]

PMID: 22794311

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