Human immunodeficiency virus type-1 Tat/co-activator acetyltransferase interactions inhibit p53Lys-320 acetylation and p53-responsive transcription

J Biol Chem. 2003 Apr 4;278(14):12310-8. doi: 10.1074/jbc.M211167200. Epub 2002 Dec 24.

Abstract

Patients with AIDS are at increased risk for developing various neoplasms, including Hodgkin's and non-Hodgkin's lymphomas, Kaposi's sarcomas, and anal-rectal carcinomas, suggestive that human immunodeficiency virus type-1 infection might promote establishment of AIDS-related cancers. Tat, the viral trans-activator, can be endocytosed by uninfected cells and has been shown to inhibit p53 functions, providing a candidate mechanism through which the human immunodeficiency virus type-1 might contribute to malignant transformation. Because Tat has been shown to interact with histone acetyltransferase domains of p300/cAMP-responsive element-binding protein (CREB)-binding protein and p300/CREB-binding protein-associated factor, we have investigated whether Tat might alter p53 acetylation and tumor suppressor-responsive transcription. Here, we demonstrate that both Tat and p53 co-localize with p300/CREB-binding protein-associated factor and p300 in nuclei of IMR-32 human neuroblastoma cells and in PC-12 pheochromocytoma cells. Further, p53 trans-activation of the 14-3-3varsigma promoter was markedly repressed by Tat-histone acetyltransferase interactions, and p53 acetylation by p300/CREB-binding protein-associated factor on residue Lys(320) was diminished as a result of Tat-histone acetyltransferase binding in vivo and in vitro. Tat also inhibited p53 acetylation by p300 in a dosage-dependent manner in vitro. Finally, HIV-1-infected Molt-4 cells displayed reduced p53 acetylation on lysines 320 and 373 in response to UV irradiation. Our results allude to a mechanism whereby the human immunodeficiency virus type-1 trans-activator might impair tumor suppressor functions in immune/neuronal-derived cells, thus favoring the establishment of neoplasia during AIDS.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetylation / radiation effects
  • Acetyltransferases / metabolism*
  • Animals
  • Antineoplastic Agents / pharmacology
  • Cell Cycle / drug effects
  • Cell Cycle / physiology
  • Cell Cycle Proteins / metabolism*
  • Cell Nucleus / metabolism
  • Doxorubicin / pharmacology
  • Gene Products, tat / genetics
  • Gene Products, tat / metabolism*
  • HIV / metabolism*
  • HIV-1*
  • Histone Acetyltransferases
  • Humans
  • Neuroblastoma
  • PC12 Cells
  • Peptide Fragments / metabolism
  • Promoter Regions, Genetic / physiology
  • Rats
  • Trans-Activators / metabolism
  • Transcription Factors
  • Transcriptional Activation / physiology*
  • Transfection
  • Tumor Cells, Cultured
  • Tumor Suppressor Protein p53 / genetics*
  • Tumor Suppressor Protein p53 / metabolism*
  • Ultraviolet Rays
  • p300-CBP Transcription Factors
  • tat Gene Products, Human Immunodeficiency Virus

Substances

  • Antineoplastic Agents
  • Cell Cycle Proteins
  • Gene Products, tat
  • Peptide Fragments
  • Trans-Activators
  • Transcription Factors
  • Tumor Suppressor Protein p53
  • tat Gene Products, Human Immunodeficiency Virus
  • Doxorubicin
  • Acetyltransferases
  • Histone Acetyltransferases
  • p300-CBP Transcription Factors
  • p300-CBP-associated factor