NDLI: Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching

Content Provider	PubMed Central
Author	Parent, Kristin N. Suhanovsky, Margaret M. Teschke, Carolyn M.
Copyright Year	2007
Abstract	Eighteen single amino acid substitutions in phage P22 coat protein cause temperature-sensitive folding defects (tsf). Three intragenic global suppressor (su) substitutions (D163G, T166I and F170L), localized to a flexible loop, rescue the folding of several tsf coat proteins. Here we investigate the su substitutions in the absence of the original tsf substitutions. None of the su variant coat proteins displayed protein folding defects. Individual su substitutions had little effect on phage production in vivo; yet double and triple combinations resulted in a cold-sensitive (cs) phenotype, consistent with a defect in assembly. During virus assembly and maturation, conformational switching of capsid subunits is required when chemically identical capsid subunits form an icosahedron. Analysis of double- and triple-su phage-infected cell lysates by negative-stain electron microscopy reveals an increase in aberrant structures at the cs temperature. In vitro assembly of F170L coat protein causes production of polyheads, never seen before in phage P22. Purified procapsids composed of all of the su coat proteins showed defects in expansion, which mimics maturation in vitro. Our results suggest that a previously identified surface-exposed loop in coat protein is critical in conformational switching of subunits during both procapsid assembly and maturation.
Related Links	http://dx.doi.org/10.1111/j.1365-2958.2007.05868.x
Ending Page	1310
Page Count	11
Starting Page	1300
File Format	PDF
ISSN	0950382X
e-ISSN	13652958
Journal	Molecular microbiology
Issue Number	5
Volume Number	65
Language	English
Publisher Date	2007-09-01
Access Restriction	Open
Subject Keyword	Molecular Biology Microbiology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

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Temperature-sensitive mutations in the phage P22 coat protein which interfere with polypeptide chain folding.

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Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching

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