Plant endoplasmin supports the protein secretory pathway and has a role in proliferating tissues (Articolo in rivista)

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  • Plant endoplasmin supports the protein secretory pathway and has a role in proliferating tissues (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Alternative label
  • Klein E.M., Mascheroni L., Pompa A., Ragni L., Weimar T., Lilley K.S., Dupree P., Vitale A. (2006)
    Plant endoplasmin supports the protein secretory pathway and has a role in proliferating tissues
    in Plant journal (Print)
    (literal)
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  • Klein E.M., Mascheroni L., Pompa A., Ragni L., Weimar T., Lilley K.S., Dupree P., Vitale A. (literal)
Pagina inizio
  • 657 (literal)
Pagina fine
  • 673 (literal)
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  • 48 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
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  • IBBA-CNR 1; Department of Biochemistry, University of Cambridge, Cambridge, UK 2; Cambridge Centre for Proteomics, Department of Biochemistry, University of Cambridge, Cambridge, UK 3 (literal)
Titolo
  • Plant endoplasmin supports the protein secretory pathway and has a role in proliferating tissues (literal)
Abstract
  • Endoplasmin is the endoplasmic reticulum-located molecular chaperone of the heat-shock protein 90 class and its activity is poorly characterised in plants. We assessed the ability of endoplasmin to alleviate stress via its transient over-expression in tobacco protoplasts treated with tunicamycin, an inhibitor of glycosylation and inducer of the unfolded protein response (UPR). Endoplasmin supported the secretion of a model secretory protein but was less effective than BiP, the endoplasmic reticulum member of the heat-shock protein 70 family. Consistently, immunoprecipitation experiments of in vivo radioactively labelled proteins using an antiserum prepared against Arabidopsis endoplasmin showed that a much lower amount of newly synthesised polypeptides associated with endoplasmin compared to BiP. Synthesis of endoplasmin was enhanced by UPR inducers in tobacco seedlings but not protoplasts. As BiP synthesis was induced in both systems, we conclude that the UPR acts, at least in part, differently on the expression of the two chaperones. Endoplasmin was not detectable in extracts of leaves and stems of the Arabidopsis endoplasmin T-DNA insertion mutant shepherd. However, the chaperone is present, albeit at low levels, in shepherd mutant callus, mature roots and tunicamycin-treated seedlings, demonstrating that the mutation is leaky. Reduced endoplasmin in the shepherd mutant has no effect on BiP protein levels in callus or mature roots, leaves and stems, but is compensated by increased BiP in seedlings. This increase occurs in proliferating rather than expanding leaf cells, indicating an important role of endoplasmin in proliferating plant tissues. (literal)
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