       Document 0660
 DOCN  M9620660
 TI    Binding of human prothymosin alpha to the leucine-motif/activation
       domains of HTLV-I Rex and HIV-1 Rev.
 DT    9602
 AU    Kubota S; Adachi Y; Copeland TD; Oroszlan S; Laboratory of Molecular
       Virology and Carcinogenesis,; NCI-Frederick Cancer Research and
       Development Center, MD 21702,; USA.
 SO    Eur J Biochem. 1995 Oct 1;233(1):48-54. Unique Identifier : AIDSLINE
       MED/96061931
 AB    Rex of human T-cell leukemia virus type I (HTLV-I) and Rev of human
       immunodeficiency virus 1 (HIV-1) are post-transcriptional regulators of
       viral gene expression. By means of affinity chromatography, we purified
       an 18-kDa cellular protein that bound to the conserved
       leucine-motif/activation domain of HTLV-I Rex or HIV-1 Rev. The protein
       that was purified through a Rev-affinity column was found to bind to Rex
       immunoprecipitated with anti-Rex IgG from an HTLV-I-producing cell line.
       We analyzed the purified approximately 18-kDa protein biochemically and
       identified it as prothymosin alpha. The binding activity of prothymosin
       alpha to Rev or Rex was completely abolished when the epsilon-amino
       groups of its lysine residues were chemically modified by
       N-succinimidyl-3-(4-hydroxy-3,5-diodo- phenyl)propionate. The functional
       relationship between the nuclear protein prothymosin alpha and Rex-Rev
       is discussed.
 DE    Amino Acid Sequence  Binding Sites  Carrier Proteins/GENETICS/ISOLATION
       & PURIF/METABOLISM  Cell Line  Chromatography, Affinity  Gene Products,
       rev/GENETICS/ISOLATION & PURIF/*METABOLISM  Gene Products,
       rex/GENETICS/ISOLATION & PURIF/*METABOLISM  Human
       HIV-1/CHEMISTRY/GENETICS/*METABOLISM
       HTLV-I/CHEMISTRY/GENETICS/*METABOLISM  Molecular Sequence Data
       Precipitin Tests  Protein Binding  Protein Precursors/GENETICS/ISOLATION
       & PURIF/*METABOLISM  Sequence Homology, Amino Acid  Support, U.S. Gov't,
       P.H.S.  Thymosin/*ANALOGS & DERIVATIVES/GENETICS/ISOLATION & PURIF/
       METABOLISM  JOURNAL ARTICLE

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

