http://www.cnr.it/ontology/cnr/individuo/prodotto/ID56716
Cymbidium ringspot virus defective interfering RNA replication in yeast cells occurs on endoplasmic reticulum-derived membranes in the absence of peroxisomes (Articolo in rivista)
- Type
- Label
- Cymbidium ringspot virus defective interfering RNA replication in yeast cells occurs on endoplasmic reticulum-derived membranes in the absence of peroxisomes (Articolo in rivista) (literal)
- Anno
- 2007-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1099/vir.0.82729-0 (literal)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Rubino L; Navarro B.; Russo M (literal)
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- http://vir.sgmjournals.org/content/88/5/1634.long (literal)
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- Pubblicazione scientifica (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto di Virologia Vegetale del CNR, Sezione di Bari, c/o Dipartimento di Protezione delle Piante e Microbiologia Applicata, Università degli Studi, Bari, Italy (literal)
- Titolo
- Cymbidium ringspot virus defective interfering RNA replication in yeast cells occurs on endoplasmic reticulum-derived membranes in the absence of peroxisomes (literal)
- Abstract
- The replication of Cymbidium ringspot virus (CymRSV) defective interfering (DI) RNA in cells of
the yeast Saccharomyces cerevisiae normally takes place in association with the peroxisomal
membrane, thus paralleling the replication events in infected plant cells. However, previous results
with a peroxisome-deficient mutant strain of yeast had suggested that the presence of
peroxisomes is not a strict requirement for CymRSV DI RNA replication. Thus, a novel approach
was used to study the putative alternative sites of replication by using S. cerevisiae strain YPH499
which does not contain normal peroxisomes. In this strain, CymRSV p33 and p92 accumulated
over portions of the nuclear membrane and on membranous overgrowths which were identified as
endoplasmic reticulum (ER) strands, following immunofluorescence and immunoelectron
microscope observations. The proteins were not released by high-pH treatment, but were
susceptible to proteolytic digestion, thus indicating peripheral and not integrated association. ERassociated
p33 and p92 proteins supported in trans the replication of DI RNA. The capacity of
plus-strand RNA viruses to replicate in association with different types of cell membranes was
thus confirmed. (literal)
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