Binding of Human Prothymosin α to the Leucine‐Motif/activation Domains of HTLV‐I Rex and HIV‐1 Rev

Satoshi Kubota, Yoshifumi Adachi, Terry D. Copeland, Stephen 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 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.

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

Keywords

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

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Binding of Human Prothymosin α to the Leucine‐Motif/activation Domains of HTLV‐I Rex and HIV‐1 Rev'. Together they form a unique fingerprint.

  • Cite this