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

Akio Kanai, Kyoko Tanabe, Michinori Kohara

Research output: Contribution to journalArticle

64 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)221-224
Number of pages4
JournalFEBS Letters
Volume376
Issue number3
DOIs
Publication statusPublished - 1995 Dec 4
Externally publishedYes

Fingerprint

RNA Helicases
Poly U
RNA
Serine Proteases
Amino Acid Motifs
Proteins
Competitive Binding
Viruses
Hepacivirus
Amino Acid Sequence
Resins
Amino Acids
hepatitis C virus NS3 protein

Keywords

  • Helicase
  • Hepatitis C virus
  • NS3 protein
  • Poly(U)
  • RNA binding

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

Cite this

Poly(U) binding activity of hepatitis C virus NS3 protein, a putative RNA helicase. / Kanai, Akio; Tanabe, Kyoko; Kohara, Michinori.

In: FEBS Letters, Vol. 376, No. 3, 04.12.1995, p. 221-224.

Research output: Contribution to journalArticle

Kanai, Akio ; Tanabe, Kyoko ; Kohara, Michinori. / Poly(U) binding activity of hepatitis C virus NS3 protein, a putative RNA helicase. In: FEBS Letters. 1995 ; Vol. 376, No. 3. pp. 221-224.
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