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| Structure and ligand of a histone acetyltransferase bromodomain |
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| Author(s): Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal AK, Zhou MM |
| Source: NATURE Volume: 399 Issue: 6735 Pages: 491-496 Published: JUN 3 1999 |
| Times Cited: 489 References: 29 |
| Abstract: Histone acetylation is important in chromatin remodelling and gene activation(1-4). Nearly all known histone-acetyltransferase (HAT)-associated transcriptional co-activators contain bromodomains, which are similar to 110-amino-acid modules found in many chromatin-associated proteins(5-9). 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 show by 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. |
| Document Type: Article |
| Language: English |
| Reprint Address: Zhou, MM (reprint author), CUNY Mt Sinai Sch Med, Dept Physiol & Biophys, Struct Biol Program, Box 1218, New York, NY 10029 USA |
Addresses:
1. CUNY Mt Sinai Sch Med, Dept Physiol & Biophys, Struct Biol Program, New York, NY 10029 USA |
| Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON N1 9XW, ENGLAND |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: 202TH |
| ISSN: 0028-0836 |
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