A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef.
In addition to playing a crucial role in the pathogenesis of AIDS, HIV nef induces down-regulation of CD4 expression and TCR signaling and also regulates the sorting pathway in host T cells. To elucidate the Nef function in HIV progression, we searched for a cellular component which interacts with Nef. ... A human cDNA encoding a novel acyl-CoA thioesterase (hACTE-III) was isolated as an HIV nef-binding protein by yeast two-hybrid system. hACTE-III is homologous to E. coli thioesterase II but to none of the mammalian thioesterases and therefore belongs to a new type. hACTE-III exhibits enzymatic specificity for a broad range of fatty acyl-CoAs. The hACTE-III-binding region within Nef is localized in the central region (amino acids 109-152). hACTE-III greatly enhances its enzymatic activity upon direct binding to Nef. Considering that either Nef-overexpression or impaired fatty acid regulation induces alteration of subcellular morphology, the augmented hACTE-III function by Nef-binding might induce dysfunction of T cells.
Mesh Terms:
Amino Acid Sequence, Binding Sites, Cloning, Molecular, Drug Interactions, Gene Products, nef, HIV, Humans, Jurkat Cells, Molecular Sequence Data, Palmitoyl-CoA Hydrolase, Protein Binding, Recombinant Proteins, Substrate Specificity, nef Gene Products, Human Immunodeficiency Virus
Amino Acid Sequence, Binding Sites, Cloning, Molecular, Drug Interactions, Gene Products, nef, HIV, Humans, Jurkat Cells, Molecular Sequence Data, Palmitoyl-CoA Hydrolase, Protein Binding, Recombinant Proteins, Substrate Specificity, nef Gene Products, Human Immunodeficiency Virus
Biochem. Biophys. Res. Commun.
Date: Sep. 08, 1997
PubMed ID: 9299485
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