title: The Rex proteins of human T-cell leukemia virus type II differ by serine phosphorylation.
abstract: The Rex proteins of human T-cell leukemia virus types I and II (HTLV-I and HTLV-II) induce cytoplasmic expression of unspliced gag-pol mRNA and singly spliced env mRNA and are critical for virus replication. Two rex gene products, p27rex and p21rex of HTLV-I and p26rex and p24rex of HTLV-II, have been detected in HTLV-infected cells; however, the structural and biological relationship of the proteins has not been clearly elucidated. Endoproteinase digestion and phosphoamino acid analysis of HTLV-II Rex indicated that p24rex has the same amino acid backbone as p26rex and that the larger apparent molecular size of p26rex is attributable to serine phosphorylation.
authors.affiliation: Department of Medicine, University of California, Los Angeles, School of Medicine.
authors.forename: P L
authors.initials: PL
authors.lastname: Green
authors.forename: Y M
authors.initials: YM
authors.lastname: Xie
authors.forename: I S
authors.initials: IS
authors.lastname: Chen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D016370:Gene Products, rex / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification; D016355:Genes, pX; D015367:Human T-lymphotropic virus 2 / Q000502:physiology*; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D010766:Phosphorylation; D012694:Serine; D014162:Transfection
chemical_list: D016370:Gene Products, rex; D012694:Serine