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Please use this identifier to cite or link to this item: http://hdl.handle.net/10373/321

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Title: A plant virus movement protein forms ringlike, complexes with the major nucleolar protein, fibrillarin, in vitro
Authors: Canetta, Elisabetta
Kim, Sang Hyon
Kalinina, Natalia O.
Shaw, Jane
Adya, Ashok K.
Gillespie, Trudi
Brown, John W. S.
Taliansky, Michael
Affiliation: University of Abertay Dundee. School of Contemporary Sciences
Keywords: Atomic force microscopy
Fibrillarin
Umbravirus
Virus movement
Protein complexes
Issue Date: 29-Feb-2008
Publisher: Elsevier Ltd
Type: Journal Article
Refereed: peer-reviewed
Rights: Published version (c)Elsevier Ltd, available from 10.1016/j.jmb.2007.12.039
Citation: Canetta, E., et al. 2008. A plant virus movement protein forms ringlike, complexes with the major nucleolar protein, fibrillarin, in vitro. Journal of Molecular Biology. 376(4): pp.932-937. Available from: DOI: 10.1016/j.jmb.2007.12.039
Abstract: Fibrillarin, one of the major proteins of the nucleolus, has methyltransferase activity directing 2′-O-ribose methylation of rRNA and snRNAs and is required for rRNA processing. The ability of the plant umbravirus, groundnut rosette virus, to move long distances through the phloem, the specialized plant vascular system, has been shown to strictly depend on the interaction of one of its proteins, the ORF3 protein (protein encoded by open reading frame 3), with fibrillarin. This interaction is essential for several stages in the groundnut rosette virus life cycle such as nucleolar import of the ORF3 protein via Cajal bodies, relocalization of some fibrillarin from the nucleolus to cytoplasm, and assembly of cytoplasmic umbraviral ribonucleoprotein particles that are themselves required for the long-distance spread of the virus and systemic infection. Here, using atomic force microscopy, we determine the architecture of these complexes as singlelayered ringlike structures with a diameter of 18–22 nm and a height of 2.0±0.4 nm, which consist of several (n=6–8) distinct protein granules. We also estimate the molar ratio of fibrillarin to ORF3 protein in the complexes as approximately 1:1. Based on these data, we propose a model of the structural organization of fibrillarin–ORF3 protein complexes and discuss potential mechanistic and functional implications that may also apply to other viruses.
URI: http://hdl.handle.net/10373/321
ISSN: 0022-2836
Appears in Collections:Science Engineering & Technology Collection

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