ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

The role of arginine-rich motif and beta-annulus in the assembly andstability of sesbania mosaic virus capsids

Satheshkumar, PS and Lokesh, GL and Murthy, MRN and Savithri, HS (2005) The role of arginine-rich motif and beta-annulus in the assembly andstability of sesbania mosaic virus capsids. In: Journal of Molecular Biology, 353 (2). pp. 447-458.

[img] PDF
av55.pdf
Restricted to Registered users only

Download (1765Kb) | Request a copy

Abstract

Sesbania mosaic virus (SeMV) capsids are stabilized by protein-protein,protein-RNA and calcium-mediated protein-protein interactions. The N-terminal random domain of SeMV coat protein (CP) controls RNA encapsidation and size of the capsids and has two important motifs, the arginine-rich motif (ARM) and the \beta-annulus structure. Here,mutational analysis of the arginine residues present in the ARM to glutamic acid was carried out. Mutation of all the arginine residues in the ARM almost completely abolished RNA encapsidation, although the assembly of T = 3 capsids was not affected. A minimum of three arginine residues was found to be essential for RNA encapsidation. The mutant capsids devoid of RNA were less. stable to thermal denaturation when compared to wild-type capsids. The results suggest that capsid assemblyis entirely mediated by CP-dependent protein-protein inter-subunit interactions and encapsidation of genomic RNA enhances the stability of the capsids. Because of the unique structural ordering of \beta-annulus segment at the icosahedral 3-folds, it has been suggested as the switch that determines the pentameric and hexameric clustering of CP subunits essential for T = 3 capsid assembly. Surprisingly, mutation of a conserved proline within the segment that forms the beta-annulus to alanine, or deletion of residues 48-53 involved in hydrogen bonding interactions with residues 54-58 of the 3-fold related subunit or deletion of all the residues (48-59) involved in the formation of \beta-annulus did not affect capsid assembly. These results suggest that the switch for assembly into T = 3 capsids is not the-annulus. The ordered \beta-annulus observed in the structures of many viruses could be a consequence of assembly to optimize inter subunit interactions.

Item Type: Journal Article
Additional Information: Copyright for this article belongs to Elsevier.
Keywords: Sesbania mosaic virus;coat protein;assembly;arginine-rich motif;beta-annulus
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Division of Biological Sciences > Biochemistry
Date Deposited: 30 Nov 2005
Last Modified: 19 Sep 2010 04:21
URI: http://eprints.iisc.ernet.in/id/eprint/4226

Actions (login required)

View Item View Item