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1996-02-26
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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).