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Fillingham J, et al.  (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53

Abstract: Acetylation of S.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 additional functions to DNA repair. We show that, in addition to its known H3K56 acetylation activity, Rtt109 is also a H3-K9 HAT, and 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, as well as Vps75 are both required for 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 di-acetylated on both H4-K5,12 and H3-K9,56.

Status: Published Type: Journal Article PubMed ID: 18458063

Topics addressed in this paper

Number of different genes curated to this paper: 20

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Topics Topics not linked to Genes Genes linked to topics (#1 - 10 )
ASF1 GCN5 HAT1 HAT2 HHF1 HHF2 HHT1 HHT2 HIF1 HST3
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Topics Genes linked to topics (#11 - 20 )
HST4 HTA1 HTA2 MMS1 MMS22 PPH3 RAD53 RTT101 RTT109 VPS75
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Cell Cycle Phase Involved blue ball blue ball blue ball
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Protein Processing/Modification/Regulation blue ball blue ball blue ball blue ball
Regulatory Role blue ball
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