机构:
Penn State Univ, Howard Hughes Med Inst, Dept Biochem & Mol Biol, University Pk, PA 16802 USAPenn State Univ, Howard Hughes Med Inst, Dept Biochem & Mol Biol, University Pk, PA 16802 USA
Grant, PA
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Berger, SL
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机构:Penn State Univ, Howard Hughes Med Inst, Dept Biochem & Mol Biol, University Pk, PA 16802 USA
Berger, SL
机构:
[1] Penn State Univ, Howard Hughes Med Inst, Dept Biochem & Mol Biol, University Pk, PA 16802 USA
[2] Wistar Inst Anat & Biol, Philadelphia, PA 19104 USA
Modification of histone amino terminal tails by acetylation has long been linked to the transcriptional capacity of genes in chromatin and to various aspects of chromatin dynamics. Over the last few years a flurry of reports have described the purification and identification of a large number of histone acetyltransferases. Many of these enzymes had previously been described as transcriptional regulators and have frequently been isolated as part of larger multisubunit protein complexes. This review describes the association of acetyltransferases with partner proteins and the additional functional attributes of such complexes beyond catalytic function.