Document 0509
 DOCN  M9610509
 TI    Localization of the palmitoylation site in the transmembrane protein
       p12E of Friend murine leukaemia virus.
 DT    9601
 AU    Hensel J; Hintz M; Karas M; Linder D; Stahl B; Geyer R; Biochemisches
       Institut am Klinikum der; Justus-Liebig-Universitat, Giessen, Germany.
 SO    Eur J Biochem. 1995 Sep 1;232(2):373-80. Unique Identifier : AIDSLINE
       MED/96035869
 AB    Friend murine leukaemia virus complex was propagated on murine cells in
       the presence of [9,10-3H]palmitic acid. Virus particles were harvested
       from the culture supernatant and lysed with detergents. The viral
       transmembrane protein, p12E, was isolated from the lysates by
       size-exclusion chromatography and purified by narrowbore reverse-phase
       HPLC. Analysis of the purified product by matrix-assisted laser
       desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS)
       revealed that the protein is palmitoylated carrying one fatty acid
       residue. The radiolabelled fatty acid was released by hydroxylamine
       treatment at pH 7, indicating that acylation occurred via a thioester
       linkage. For allocation of the acylation site, p12E was digested with
       trypsin. The resulting peptides were either directly subjected to
       MALDI-TOF-MS or fractionated by microbore reverse-phase HPLC prior to
       mass spectrometry. The results revealed that p12E of Friend murine
       leukaemia virus is acylated at a cysteine residue situated at the
       C-terminal side of the putative transmembrane anchor of the polypeptide.
       Fatty acid analysis of the purified acylpeptide demonstrated that p12E
       carries almost exclusively palmitic acid.
 DE    Acylation  Amino Acid Sequence  Animal  Binding Sites  Fatty
       Acids/CHEMISTRY  Friend Virus/*CHEMISTRY/GENETICS/METABOLISM  Gene
       Products, env/*CHEMISTRY/GENETICS/METABOLISM  Mice  Molecular Sequence
       Data  Palmitic Acids/*CHEMISTRY/METABOLISM  Peptide
       Fragments/CHEMISTRY/GENETICS  Protein Processing, Post-Translational
       Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
       Support, Non-U.S. Gov't  JOURNAL ARTICLE

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