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Watanabe, H, Shiratori, T, Shoji, H, Miyatake, S, Okazaki, Y, Ikuta, K, Sato, T and Saito, T (1997) A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef. Biochem. Biophys. Res. Commun. 238:234-9

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.

PubMed Online version:10.1006/bbrc.1997.7217

Amino Acid Sequence; Binding Sites; Cloning, Molecular; Drug Interactions; Gene Products, nef/genetics; Gene Products, nef/metabolism; Gene Products, nef/physiology; HIV/enzymology; HIV/physiology; Humans; Jurkat Cells; Molecular Sequence Data; Palmitoyl-CoA Hydrolase/genetics; Palmitoyl-CoA Hydrolase/metabolism; Palmitoyl-CoA Hydrolase/physiology; Protein Binding; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Substrate Specificity; nef Gene Products, Human Immunodeficiency Virus