NDLI: A structural rationale for SV40 Vp1 temperature-sensitive mutants and their complementation

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A structural rationale for SV40 Vp1 temperature-sensitive mutants and their complementation

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A structural rationale for SV40 Vp1 temperature-sensitive mutants and their complementation

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Nakamura, Akiko Tevethia, M. Judith Liddington, Robert C. Kasamatsu, Harumi Müller, Peter Woo, Jennifer
Description	Country affiliation: United States Author Affiliation: Kasamatsu H ( Molecular Biology Institute, University of California, Los Angeles, CA 90095, USA.)
Abstract	Two groups of temperature-sensitive (ts) mutants, termed ts B and ts C, have mutations in the major capsid protein of SV40, Vp1. These mutants have virion assembly defects at the nonpermissive temperature, but can complement one another when two mutants, one from each group, coinfect a cell. A third group of mutants, termed ts BC, have related phenotypes, but do not complement other mutants. We found that the mutations fall into two structural and functional classes. All ts C and one ts BC mutations map to the region close to the Ca2+ binding sites, and are predicted to disrupt the insertion of the distal part of the C-terminal invading arm (C-arm) into the receiving clamp. They share a severe defect in assembly at the nonpermissive temperature, with few capsid proteins attached to the viral minichromosome. By contrast, all ts B and most ts BC mutations map to a contiguous region including acceptor sites for the proximal part of the C-arm and intrapentamer contacts. These mutants form assembly intermediates that carry substantial capsid proteins on the minichromosome. Thus, accurate virion assembly is prevented by mutations that disrupt interactions between the receiving pentamer and both the proximal and distal parts of the C-arms, with the latter having a greater effect. The distinct spatial localization and assembly defects of the two classes of mutants provide a rationale for their intracistronic complementation and suggest models of capsid assembly.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	9
Volume Number	15
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2006-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Capsid Proteins Chemistry Mutation Structure-activity Relationship Virus Assembly Binding Sites Calcium Metabolism Genetics Chromosomes Protein Structure, Secondary Protein Structure, Tertiary Temperature Research Support, N.i.h., Extramural Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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