Structure and ligand of a histone acetyltransferase bromodomain

Christophe Dhalluin, Justin E. Carlson, Lei Zeng, Cheng He, Aneel K. Aggarwal, Ming-Ming Zhou and Ming-Ming Zhou ()
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Christophe Dhalluin: Structural Biology Program, Mount Sinai School of Medicine
Justin E. Carlson: Structural Biology Program, Mount Sinai School of Medicine
Lei Zeng: Structural Biology Program, Mount Sinai School of Medicine
Cheng He: Structural Biology Program, Mount Sinai School of Medicine
Aneel K. Aggarwal: Structural Biology Program, Mount Sinai School of Medicine
Ming-Ming Zhou: Structural Biology Program, Mount Sinai School of Medicine
Ming-Ming Zhou: Structural Biology Program, Mount Sinai School of Medicine

Nature, 1999, vol. 399, issue 6735, 491-496

Abstract: Abstract Histone acetylation is important in chromatin remodelling and gene activation1,2,3,4. Nearly all known histone-acetyltransferase (HAT)-associated transcriptional co-activators contain bromodomains, which are ∼110-amino-acid modules found in many chromatin-associated proteins5,6,7,8,9. Despite the wide occurrence of these bromodomains, their three-dimensional structure and binding partners remain unknown. Here we report the solution structure of the bromodomain of the HAT co-activator P/CAF (p300/CBP-associated factor)10,11. The structure reveals an unusual left-handed up-and-down four-helix bundle. In addition, we showby a combination of structural and site-directed mutagenesis studies that bromodomains can interact specifically with acetylated lysine, making them the first known protein modules to do so. The nature of the recognition of acetyl-lysine by the P/CAF bromodomain is similar to that of acetyl-CoA by histone acetyltransferase. Thus, the bromodomain is functionally linked to the HAT activity of co-activators in the regulation of gene transcription.

Date: 1999
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DOI: 10.1038/20974

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