NDLI: RNA-controlled polymorphism in the in vivoassembly of 180-subunit and 120-subunit virions from a singlecapsid protein

Content Provider	PubMed Central
Author	Krol, Michael A. Olson, Norman H. Tate, John Johnson, John E. Baker, Timothy S. Ahlquist, Paul
Copyright Year	1999
Abstract	Repeated, specific interactions between capsid protein (CP)subunits direct virus capsid assembly and exemplify regulatedprotein–protein interactions. The results presented here reveal astriking in vivo switch in CP assembly. Usingcryoelectron microscopy, three-dimensional image reconstruction, andmolecular modeling, we show that brome mosaic virus (BMV) CP canassemble in vivo two remarkably distinct capsids thatselectively package BMV-derived RNAs in the absence of BMV RNAreplication: a 180-subunit capsid indistinguishable from virionsproduced in natural infections and a previously unobserved BMV capsidtype with 120 subunits arranged as 60 CP dimers. Each such dimercontains two CPs in distinct, nonequivalent environments, in contrastto the quasi-equivalent CP environments throughout the 180-subunitcapsid. This 120-subunit capsid utilizes most of the CP interactions ofthe 180-subunit capsid plus nonequivalent CP–CP interactions. Thus,the CP of BMV, and perhaps other viruses, can encode CP–CPinteractions that are not apparent from mature virions and may functionin assembly or disassembly. Shared structural features suggest that the120- and 180-subunit capsids share assembly steps and that a commonpentamer of CP dimers may be an important assembly intermediate. Theability of a single CP to switch between distinct capsids by means ofalternate interactions also implies reduced evolutionary barriersbetween different capsid structures. The in vivo switchbetween alternate BMV capsids is controlled by the RNA packaged: anatural BMV genomic RNA was packaged in 180-subunit capsids, whereas anengineered mRNA containing only the BMV CP gene was packaged in120-subunit capsids. RNA features can thus direct the assembly of aribonucleoprotein complex between alternate structural pathways.
Starting Page	13650
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	24
Volume Number	96
Language	English
Publisher	National Academy of Sciences
Publisher Date	1999-11-23
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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