TY - JOUR
T1 - Binding of Human Prothymosin α to the Leucine‐Motif/activation Domains of HTLV‐I Rex and HIV‐1 Rev
AU - Kubota, Satoshi
AU - Adachi, Yoshifumi
AU - Copeland, Terry D.
AU - Oroszlan, Stephen
N1 - Copyright:
Copyright 2016 Elsevier B.V., All rights reserved.
PY - 1995/10
Y1 - 1995/10
N2 - 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 ≈ 18‐kDa protein biochemically and identified it as prothymosin α. The binding activity of prothymosin α to Rev or Rex was completely abolished when the ɛ‐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 α and Rex‐Rev is discussed.
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 ≈ 18‐kDa protein biochemically and identified it as prothymosin α. The binding activity of prothymosin α to Rev or Rex was completely abolished when the ɛ‐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 α and Rex‐Rev is discussed.
KW - Rex of human T‐cell leukemia virus type I (HTLV‐I)
KW - human immunodeficiency virus type 1 (HIV‐1)
KW - interaction with Rev and Rex
KW - prothymosin α
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U2 - 10.1111/j.1432-1033.1995.048_1.x
DO - 10.1111/j.1432-1033.1995.048_1.x
M3 - Article
C2 - 7588773
AN - SCOPUS:0028862786
SN - 0014-2956
VL - 233
SP - 48
EP - 54
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 1
ER -