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Tat-controlled protein acetylation.

Edwige Col1, Benoit Gilquin, Cécile Caron

  • 1Laboratoire de Biologie Moléculaire et Cellulaire de la Différenciation-INSERM U309, Equipe Chromatine et Expression des Gènes, Institut Albert Bonniot, Faculté de Médecine, Domaine de la Merci, 38706 La Tronche Cedex, France.

The Journal of Biological Chemistry
|August 3, 2002
PubMed
Summary
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Human immunodeficiency virus type 1 Tat protein broadly inhibits histone acetylation by cellular enzymes. Tat specifically targets the CREB-binding protein (CBP), altering its substrate selectivity and hijacking cellular signaling pathways.

Area of Science:

  • Molecular Biology
  • Virology
  • Epigenetics

Background:

  • Human immunodeficiency virus type 1 (HIV-1) transactivator protein (Tat) interacts with nuclear histone acetyltransferases (HATs).
  • Histone acetylation plays a crucial role in regulating gene expression and cellular signaling.

Purpose of the Study:

  • To investigate the effect of HIV-1 Tat on cellular histone acetylation.
  • To determine if Tat exhibits substrate selectivity towards specific HATs.

Main Methods:

  • In vitro assays measuring histone acetylation in the presence of HIV-1 Tat.
  • Analysis of Tat's interaction with CREB-binding protein (CBP) and its effect on substrate acetylation (histones, p53, MyoD).
  • Deletion analysis of the Tat protein to identify functional domains.

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Main Results:

  • HIV-1 Tat acts as a general inhibitor of histone acetylation by cellular HATs.
  • Tat induces substrate selectivity in CREB-binding protein (CBP), significantly inhibiting histone acetylation while leaving p53 and MyoD acetylation unaffected.
  • The C-terminal domain of Tat is essential and sufficient for inhibiting histone acetylation.

Conclusions:

  • HIV-1 Tat protein can selectively modulate cellular protein acetylation mediated by nuclear HATs.
  • Tat hijacks the cellular acetylation signaling system for its own purposes, potentially impacting host cell function.
  • Understanding Tat's interaction with HATs provides insights into HIV-1 pathogenesis and epigenetic regulation.