Deletion of highly conserved arginine-rich RNA binding motif in cowpea chlorotic mottle virus capsid protein results in virion structural alterations and RNA packaging constraints.

Abstract excerpt

The N-proximal region of cowpea chlorotic mottle virus (CCMV) capsid protein (CP) contains an arginine-rich RNA binding motif (ARM) that is also found in the CPs of other members of Bromoviridae and in other RNA binding proteins such as the Tat and Rev proteins of human immunodeficiency virus. To assess the critical role played by this motif during encapsidation, a variant of CCMV RNA3 (C3) precisely lacking the...

Topics

• Amino Acid Motifs
• Amino Acid Sequence
• Blotting, Northern
• Bromovirus
• Capsid Proteins
• Electrophoretic Mobility Shift Assay
• Image Processing, Computer-Assisted
• Microscopy, Electron
• Molecular Sequence Data
• Mutation
• Protein Binding
• RNA, Viral