机构:
Penn State Univ, Dept Biochem & Mol Biol, Howard Hughes Med Inst, University Pk, PA 16802 USAPenn State Univ, Dept Biochem & Mol Biol, Howard Hughes Med Inst, University Pk, PA 16802 USA
Brown, CE
[1
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Lechner, T
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机构:
Penn State Univ, Dept Biochem & Mol Biol, Howard Hughes Med Inst, University Pk, PA 16802 USAPenn State Univ, Dept Biochem & Mol Biol, Howard Hughes Med Inst, University Pk, PA 16802 USA
Lechner, T
[1
]
Howe, L
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h-index: 0
机构:
Penn State Univ, Dept Biochem & Mol Biol, Howard Hughes Med Inst, University Pk, PA 16802 USAPenn State Univ, Dept Biochem & Mol Biol, Howard Hughes Med Inst, University Pk, PA 16802 USA
Howe, L
[1
]
Workman, JL
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机构:
Penn State Univ, Dept Biochem & Mol Biol, Howard Hughes Med Inst, University Pk, PA 16802 USAPenn State Univ, Dept Biochem & Mol Biol, Howard Hughes Med Inst, University Pk, PA 16802 USA
Workman, JL
[1
]
机构:
[1] Penn State Univ, Dept Biochem & Mol Biol, Howard Hughes Med Inst, University Pk, PA 16802 USA
Histone acetylation is closely linked to gene transcription. The identification of histone acetyltransferases (HATs) and the large multiprotein complexes in which they reside has yielded important insights into how these enzymes regulate transcription. The demonstration that HAT complexes interact with sequence-specific activator proteins illustrates how these complexes target specific genes. In addition to histones, some HATs can acetylate nonhistone proteins suggesting multiple roles for these enzymes.