期刊
MOLECULAR CELL
卷 14, 期 2, 页码 195-205出版社
CELL PRESS
DOI: 10.1016/S1097-2765(04)00184-4
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资金
- NIGMS NIH HHS [R01 GM62970, R01 GM062970] Funding Source: Medline
The yeast Hat1p/Hat2p type B histone acetyltransferase complex is localized to both the cytoplasm and nucleus. We isolate the nuclear form of the Hat1p/ Hat2p complex and find that it copurifies with the product of the uncharacterized open reading frame YLL022C (named Hif1p). The functional significance of the association of Hif1p with the Hat1p/Hat2p complex is confirmed by the observation that hif1Delta and hat1Delta strains display similar defects in telomeric silencing and DNA double-strand break repair. Hif1p is a histone chaperone that selectively interacts with histones H3 and H4. Hif1p is also a chromatin assembly factor, promoting the deposition of histones in the presence of a yeast cytosolic extract. In vivo, the nuclear Hat1p/ Hat2p/Hif1p complex is bound to acetylated histone H4, as well as histone H3. The association of Hif1p with acetylated H4 requires Hat1p and Hat2p providing a link between type B histone acetyltransferases and chromatin assembly.
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