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| Mol. Cell. Biol. Jul (2008); 28(13):4342-53 | |
| Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109- | |
| Fillingham J, Recht J, Silva AC, Suter B, Emili A, Stagljar I, Krogan NJ, Allis CD, Keogh MC, Greenblatt JF | |
| Banting and Best Department of Medical Research, Terrence Donnelly Centre for Cellular and Biomolecular Research -CCBR-, University of Toronto, 160 College St-, Toronto, Ontario M5S 3E1, Canada- | |
| Abstract: Acetylation of Saccharomyces cerevisiae histone H3 on K56 by the histone acetyltransferase -HAT- Rtt109 is important for repairing replication-associated lesions- Rtt109 purifies from yeast in complex with the histone chaperone Vps75, which stabilizes the HAT in vivo- A whole-genome screen to identify genes whose deletions have synthetic genetic interactions with rtt109Delta suggests Rtt109 has functions in addition to DNA repair- We show that in addition to its known H3-K56 acetylation activity, Rtt109 is also an H3-K9 HAT, and we show that Rtt109 and Gcn5 are the only H3-K9 HATs in vivo- Rtt109's H3-K9 acetylation activity in vitro is enhanced strongly by Vps75- Another histone chaperone, Asf1, and Vps75 are both required for acetylation of lysine 9 on H3 -H3-K9ac- in vivo by Rtt109, whereas H3-K56ac in vivo requires only Asf1- Asf1 also physically interacts with the nuclear Hat1-Hat2-Hif1 complex that acetylates H4-K5 and H4-K12- We suggest Asf1 is capable of assembling into chromatin H3-H4 dimers diacetylated on both H4-K5-12 and H3-K9-56- | |
| [PUBMED: 18458063] |   |
| Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. |
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| BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9. |