Poly(U) binding activity of hepatitis C virus NS3 protein, a putative RNA helicase

Akio Kanai, Kyoko Tanabe, Michinori Kohara

研究成果: Article査読

64 被引用数 (Scopus)

抄録

A non-structural protein of the hepatitis C virus (HCV), NS3, contains amino acid sequence motifs characteristic of serine-proteinases and RNA helicases. RNA binding activity of the NS3 protein with an apparent dissociation constant of 2 × 10-7 M was detected using a poly(U)-Sepharose resin. Competitive RNA binding analysis suggested that the NS3 protein binds preferentially to the poly(U) sequence, which is located at the 3′ end of HCV RNA. Mutational analysis of NS3 protein revealed the possibility that both the RNA helicase region and the serine-proteinase region were necessary for full RNA binding activity.

本文言語English
ページ(範囲)221-224
ページ数4
ジャーナルFEBS Letters
376
3
DOI
出版ステータスPublished - 1995 12 4
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

フィンガープリント

「Poly(U) binding activity of hepatitis C virus NS3 protein, a putative RNA helicase」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル