Analysis of sequences in the Cymbidium ringspot virus replicase protein p33 that promote targeting and anchoring with the endoplasmic reticulum membranes (Comunicazione a convegno)

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  • Analysis of sequences in the Cymbidium ringspot virus replicase protein p33 that promote targeting and anchoring with the endoplasmic reticulum membranes (Comunicazione a convegno) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
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  • Rubino, L., Vernile, P. & Russo, M. (2008)
    Analysis of sequences in the Cymbidium ringspot virus replicase protein p33 that promote targeting and anchoring with the endoplasmic reticulum membranes
    in 8th National Congress of the Italian Society of Virology, Orvieto
    (literal)
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  • Rubino, L., Vernile, P. & Russo, M. (literal)
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  • The replication of positive-stranded RNA viruses requires the association of the virus-encoded replicase proteins with intracellular membranes. Cymbidium ringspot virus (CymRSV) RNA replication occurs on the limiting membrane of peroxisomes of both plant and yeast cells when these organelles are present. In peroxisome-deficient yeast strains viral RNA replication takes place on endoplasmic reticulum (ER)-derived membranes, causing ER proliferation and deformation. Biochemical analysis suggested that a strong association of CymRSV replication protein p33 with the ER occurs, as it was not released from the membrane fraction after high-pH or high-salt treatments and was detected in the low-density membrane fractions in floatation gradient analysis. The variations in membrane affinity and intracellular localization of a number of p33 deletion mutants in yeast cells devoid of peroxisomes, was analyzed to further examine the nature of the association of CymRSV p33 with the ER membrane and the sequences involved. Confocal immunfluorescence microscopy and floatation gradient analysis of p33 mutants showed that the ER targeting signal of p33 resided in the first 189 aa, which consisted of two transmembrane domains, the N-terminal hydrophilic region upstream of the first transmembrane and a hydrophilic stretch of 35 aa downstream the second transmembrane. We suggest that in infected plant cells, targeting of p33 to ER strands is a necessary and preliminary step for p33 protein localization in peroxisomal membranes which leads to their conspicuous proliferation. In the absence of peroxisomes, as in the case of YPH499 yeast cells, the protein remains localized in the ER. (literal)
Titolo
  • Analysis of sequences in the Cymbidium ringspot virus replicase protein p33 that promote targeting and anchoring with the endoplasmic reticulum membranes (literal)
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