A highly basic cyanogen bromide peptide from sowbane mosaic virus protein
J H Tremaine1, W P Ronald, E M Kelly
1Research Station, Agriculture Canada, 6660 N. W. Marine Drive, Vancouver, B. C. V6T 1X2 Canada.
Virology
|October 15, 1981
Summary
Sowbane mosaic virus protein cleavage revealed a highly basic peptide (sCB-1) rich in lysine and arginine. This peptide
Area of Science:
- Virology
- Molecular Biology
- Biochemistry
Background:
- Sowbane mosaic virus (SoMV) is a plant virus with a protein coat.
- Understanding the structural and functional roles of viral proteins is crucial for virology research.
Purpose of the Study:
- To isolate and characterize a specific peptide fragment from the SoMV protein.
- To investigate the potential role of this peptide in virus-RNA interactions.
Main Methods:
- Cleavage of the SoMV protein using cyanogen bromide (CNBr).
- Isolation of the peptide fragment (sCB-1) using Sephadex and ion-exchange chromatography.
- Analysis of amino acid composition and peptide size using SDS-PAGE.
Main Results:
- A highly basic peptide, sCB-1, comprising 49 amino acid residues was isolated.
- sCB-1 contains 18 basic residues, including 15 lysine and 3 arginine residues.
- sCB-1 exhibited faster migration in electrophoresis compared to a similar peptide from southern bean mosaic virus.
Conclusions:
- The high basicity of sCB-1 suggests its involvement in binding to viral RNA within SoMV particles.
- This finding provides insights into the molecular mechanisms of virus assembly and RNA packaging.
