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A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1997 Sep 08; Vol. 238 (1), pp. 234-9. - Publication Year :
- 1997
-
Abstract
- 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.
- Subjects :
- Amino Acid Sequence
Binding Sites
Cloning, Molecular
Drug Interactions
Gene Products, nef genetics
Gene Products, nef physiology
HIV physiology
Humans
Jurkat Cells
Molecular Sequence Data
Palmitoyl-CoA Hydrolase genetics
Palmitoyl-CoA Hydrolase physiology
Protein Binding
Recombinant Proteins chemistry
Recombinant Proteins metabolism
Substrate Specificity
nef Gene Products, Human Immunodeficiency Virus
Gene Products, nef metabolism
HIV enzymology
Palmitoyl-CoA Hydrolase metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 238
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 9299485
- Full Text :
- https://doi.org/10.1006/bbrc.1997.7217