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    Mol Cell. 2004 Apr 23;14(2):195-205.

    The nuclear Hat1p/Hat2p complex: a molecular link between type B histone acetyltransferases and chromatin assembly.

    Ai X, Parthun MR.

    Department of Molecular and Cellular Biochemistry, The Ohio State University, Columbus, OH 43210, USA.

    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.

    PMID: 15099519 [PubMed - indexed for MEDLINE]

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