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Related Experiment Videos

Structure and function of histone acetyltransferases.

R Marmorstein1

  • 1The Wistar Institute and the Department of Chemistry, University of Pennsylvania, Philadelphia 19104, USA. marmor@wistar.upenn.edu

Cellular and Molecular Life Sciences : CMLS
|July 5, 2001
PubMed
Summary
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Histone acetyltransferase (HAT) enzymes regulate gene transcription by acetylating histones. Structural studies reveal conserved domains for cofactor binding and variable domains for histone interaction, aiding in understanding HAT complex function.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Epigenetics

Background:

  • Histone acetyltransferase (HAT) enzymes are crucial for transcriptional activation.
  • They function as catalytic subunits within large multisubunit HAT complexes.
  • HATs catalyze the acetylation of lysine residues on histone tails.

Purpose of the Study:

  • To provide new insights into the mechanism of histone binding and acetylation by HAT proteins.
  • To establish a framework for understanding the structure and function of diverse HAT enzymes.
  • To explore how HAT proteins cooperate within complexes for transcriptional activation.

Main Methods:

  • Structural and functional studies of divergent HAT enzymes (Gcn5/PCAF, Esa1, Hat1).
  • Analysis of conserved core domains and variable N- and C-terminal domains.

Related Experiment Videos

  • Comparative analysis across different HAT protein families.

    • Main Results:

    • A structurally conserved core domain is essential for coenzyme A binding and catalysis.
    • Variable N- and C-terminal domains mediate histone substrate binding.
    • Identified conserved structural and functional roles across divergent HAT enzymes.

    Conclusions:

    • The findings provide a structural framework for understanding HAT enzyme mechanisms.
    • This framework aids in comprehending the function of more divergent HATs like TAF(II)250 and CBP/p300.
    • It offers a starting point for investigating in vivo HAT complex cooperation in transcription.