Abstract:
:GCN5, a putative transcriptional adapter in humans and yeast, possesses histone acetyltransferase (HAT) activity which has been linked to GCN5's role in transcriptional activation in yeast. In this report, we demonstrate a functional interaction between human GCN5 (hGCN5) and the DNA-dependent protein kinase (DNA-PK) holoenzyme. Yeast two-hybrid screening detected an interaction between the bromodomain of hGCN5 and the p70 subunit of the human Ku heterodimer (p70-p80), which is the DNA-binding component of DNA-PK. Interaction between intact hGCN5 and Ku70 was shown biochemically using recombinant proteins and by coimmunoprecipitation of endogenous proteins following chromatography of HeLa nuclear extracts. We demonstrate that the catalytic subunit of DNA-PK phosphorylates hGCN5 both in vivo and in vitro and, moreover, that the phosphorylation inhibits the HAT activity of hGCN5. These findings suggest a possible regulatory mechanism of HAT activity.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Barlev NA,Poltoratsky V,Owen-Hughes T,Ying C,Liu L,Workman JL,Berger SLdoi
10.1128/mcb.18.3.1349subject
Has Abstractpub_date
1998-03-01 00:00:00pages
1349-58issue
3eissn
0270-7306issn
1098-5549journal_volume
18pub_type
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