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Poly(U) binding activity of hepatitis C virus NS3 protein, a putative RNA helicase
- Source :
- FEBS letters. 376(3)
- Publication Year :
- 1995
-
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.
- Subjects :
- Poly U
viruses
Molecular Sequence Data
Biophysics
RNA-dependent RNA polymerase
Viral Nonstructural Proteins
Biochemistry
Helicase
Structure-Activity Relationship
Structural Biology
Transcription (biology)
Genetics
NS3 protein
Amino Acid Sequence
Molecular Biology
Poly(U)
Sequence Deletion
Messenger RNA
Hepatitis C virus
Chemistry
virus diseases
RNA
RNA-Binding Proteins
RNA Nucleotidyltransferases
Cell Biology
RNA binding
biochemical phenomena, metabolism, and nutrition
Non-coding RNA
RNA Helicase A
Molecular biology
digestive system diseases
Recombinant Proteins
Post-transcriptional modification
Degradosome
RNA Helicases
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 376
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- FEBS letters
- Accession number :
- edsair.doi.dedup.....4488f1f105265e7477963d836cf707d5