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

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. Compet...

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Bibliographic Details
Published in:FEBS letters 1995-12, Vol.376 (3), p.221-224
Main Authors: Kanai, Akio, Tanabe, Kyoko, Kohara, Michinori
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Helicase
Hepatitis C virus
Molecular Sequence Data
NS3 protein
Poly U - metabolism
Poly(U)
Recombinant Proteins
RNA binding
RNA Helicases
RNA Nucleotidyltransferases - metabolism
RNA-Binding Proteins - metabolism
Sequence Deletion
Structure-Activity Relationship
Viral Nonstructural Proteins - metabolism
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)01283-X