Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 932-937 |
| Number of pages | 6 |
| Journal | Journal of Molecular Biology |
| Volume | 376 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 29 Feb 2008 |
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A plant virus movement protein forms ringlike, complexes with the major nucleolar protein, fibrillarin, in vitro. / Canetta, Elisabetta; Kim, Sang Hyon; Kalinina, Natalia O.; Shaw, Jane; Adya, Ashok K.; Gillespie, Trudi; Brown, John W. S.; Taliansky, Michael.
In: Journal of Molecular Biology, Vol. 376, No. 4, 29.02.2008, p. 932-937.Research output: Contribution to journal › Article
TY - JOUR
T1 - A plant virus movement protein forms ringlike, complexes with the major nucleolar protein, fibrillarin, in vitro
AU - Canetta, Elisabetta
AU - Kim, Sang Hyon
AU - Kalinina, Natalia O.
AU - Shaw, Jane
AU - Adya, Ashok K.
AU - Gillespie, Trudi
AU - Brown, John W. S.
AU - Taliansky, Michael
PY - 2008/2/29
Y1 - 2008/2/29
N2 - 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.
AB - 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.
U2 - 10.1016/j.jmb.2007.12.039
DO - 10.1016/j.jmb.2007.12.039
M3 - Article
VL - 376
SP - 932
EP - 937
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 4
ER -