       Document 0197
 DOCN  M9610197
 TI    The human and simian immunodeficiency virus envelope glycoprotein
       transmembrane subunits are palmitoylated.
 DT    9601
 AU    Yang C; Spies CP; Compans RW; Department of Microbiology and Immunology,
       Emory University; School of Medicine, Atlanta, GA 30322, USA.
 SO    Proc Natl Acad Sci U S A. 1995 Oct 10;92(21):9871-5. Unique Identifier :
       AIDSLINE MED/96003881
 AB    The envelope proteins of human immunodeficiency virus (HIV) and simian
       immunodeficiency virus (SIV) were found to be modified by fatty
       acylation of the transmembrane protein subunit gp41. The precursor gp160
       was also palmitoylated prior to its cleavage into the gp120 and gp41
       subunits. The palmitic acid label was sensitive to treatment with
       hydroxylamine or 2-mercaptoethanol, indicating that the linkage is
       through a thioester bond. Treatment with cycloheximide did not prevent
       the incorporation of [3H]palmitic acid into the HIV envelope protein,
       indicating that palmitoylation is a posttranslation modification. In
       contrast to other glycoproteins, which are palmitoylated at cysteine
       residues within or close to the membrane-spanning hydrophobic domain,
       the palmitoylation of the HIV-1 envelope proteins occurs on two cysteine
       residues, Cys-764 and Cys-837, which are 59 and 132 amino acids,
       respectively, from the proposed membrane-spanning domain of gp41.
       Sequence comparison revealed that one of these residues (Cys-764) is
       conserved in the cytoplasmic domains of almost all HIV-1 isolates and is
       located very close to an amphipathic region which has been postulated to
       bind to the plasma membrane.
 DE    Amino Acid Sequence  Base Sequence  Comparative Study  Gene Products,
       env/GENETICS/*METABOLISM  Hela Cells  Human  HIV Envelope Protein
       gp120/GENETICS/METABOLISM  HIV Envelope Protein gp41/GENETICS/METABOLISM
       HIV-1/*METABOLISM  Membrane Fusion  Molecular Sequence Data  Palmitic
       Acids/*METABOLISM  Protein Conformation  Protein
       Precursors/GENETICS/METABOLISM  *Protein Processing, Post-Translational
       Recombinant Proteins/METABOLISM  Sequence Homology, Amino Acid  Support,
       U.S. Gov't, P.H.S.  SIV/*METABOLISM  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

