Binding of human prothymosin α to the leucine-motif/activation domains of HTLV-I Rex and HIV-1 Rev

Satoshi Kubota, Y. Adachi, T. D. Copeland, S. Oroszlan

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

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 ε-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.

Original languageEnglish
Pages (from-to)48-54
Number of pages7
JournalEuropean Journal of Biochemistry
Volume233
Issue number1
Publication statusPublished - 1995
Externally publishedYes

Fingerprint

Human T-lymphotropic virus 1
T-cells
Viruses
Leucine
HIV-1
Chemical activation
Proteins
Viral Genes
Propionates
Regulator Genes
Nuclear Proteins
Affinity Chromatography
Lysine
Affinity chromatography
Immunoglobulin G
Gene Expression
Cell Line
Gene expression
Cells

Keywords

  • human immunodeficiency virus type 1 (HIV-1)
  • interaction with Rev and Rex
  • prothymosin α
  • Rex of human T-cell leukemia virus type I (HTLV-I)

ASJC Scopus subject areas

  • Biochemistry

Cite this

Binding of human prothymosin α to the leucine-motif/activation domains of HTLV-I Rex and HIV-1 Rev. / Kubota, Satoshi; Adachi, Y.; Copeland, T. D.; Oroszlan, S.

In: European Journal of Biochemistry, Vol. 233, No. 1, 1995, p. 48-54.

Research output: Contribution to journalArticle

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AU - Adachi, Y.

AU - Copeland, T. D.

AU - Oroszlan, S.

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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 ε-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 ε-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.

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