| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1979173 | Current Opinion in Structural Biology | 2011 | 7 Pages |
Abstract
⺠Histone chaperones Vps75 and Asf1 stimulate Rtt109 acetyltransferase toward histone H3 approximately 100-fold. ⺠Rtt109-Asf1 acetylates H3 K56, while Rtt109-Vps75 acetylates H3 K9 and K27. ⺠Auto-acetylation of Rtt109 at K290 is essential and is not influenced by Vps75. ⺠Based on structural work, the stoichiometry of Vps75-Rtt109 is uncertain; it may be 2:1 or 2:2. ⺠Vps75 imports Rtt109 into the nucleus, stabilizes Rtt109, and positions H3 for acetylation by Rtt109.
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Authors
Sheena D'Arcy, Karolin Luger,