Rad26p, a transcription-coupled repair factor, promotes the eviction and prevents the reassociation of histone H2A-H2B dimer during transcriptional elongation in vivo.
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.
Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL 62901, USA.
Shivani
S
Malik
Sukesh R
SR
Bhaumik
D000251:Adenosine Triphosphatases / Q000235:genetics*; D001426:Bacterial Proteins / Q000235:genetics / Q000502:physiology*; D002843:Chromatin / Q000235:genetics / Q000378:metabolism; D004260:DNA Repair / Q000235:genetics*; D004271:DNA, Fungal / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D006657:Histones / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D055503:Protein Multimerization; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics*; D014157:Transcription Factors / Q000235:genetics / Q000502:physiology*; D035602:Transcriptional Elongation Factors / Q000235:genetics* / Q000378:metabolism
D001426:Bacterial Proteins; D002843:Chromatin; D004271:DNA, Fungal; D006657:Histones; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D035602:Transcriptional Elongation Factors; C072103:transcription repair coupling factor protein, Bacteria; D000251:Adenosine Triphosphatases; C465758:RAD26 protein, S cerevisiae