Expression and localisation of a senescence-associated KDEL-cysteine protease from Lilium longiflorum tepals

Copyright © 2013 Elsevier Ireland Ltd. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant science : an international journal of experimental plant biology. - 1985. - 214(2014) vom: 19. Jan., Seite 38-46
1. Verfasser: Battelli, Riccardo (VerfasserIn)
Weitere Verfasser: Lombardi, Lara, Picciarelli, Piero, Lorenzi, Roberto, Frigerio, Lorenzo, Rogers, Hilary J
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2014
Zugriff auf das übergeordnete Werk:Plant science : an international journal of experimental plant biology
Schlagworte:Journal Article Cysteine proteases Endoplasmic reticulum Lilium Petal senescence Subcellular localisation Vacuole Luminescent Proteins Oligopeptides Plant Proteins mehr... Protein Sorting Signals lysyl-aspartyl-glutamyl-leucine 113516-56-6 Cysteine Proteases EC 3.4.-
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100 1 |a Battelli, Riccardo  |e verfasserin  |4 aut 
245 1 0 |a Expression and localisation of a senescence-associated KDEL-cysteine protease from Lilium longiflorum tepals 
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520 |a Copyright © 2013 Elsevier Ireland Ltd. All rights reserved. 
520 |a Senescence is a tightly regulated process and both compartmentalisation and regulated activation of degradative enzymes is critical to avoid premature cellular destruction. Proteolysis is a key process in senescent tissues, linked to disassembly of cellular contents and nutrient remobilisation. Cysteine proteases are responsible for most proteolytic activity in senescent petals, encoded by a gene family comprising both senescence-specific and senescence up-regulated genes. KDEL cysteine proteases are present in senescent petals of several species. Isoforms from endosperm tissue localise to ricinosomes: cytosol acidification following vacuole rupture results in ricinosome rupture and activation of the KDEL proteases from an inactive proform. Here data show that a Lilium longiflorum KDEL protease gene (LlCYP) is transcriptionally up-regulated, and a KDEL cysteine protease antibody reveals post-translational processing in senescent petals. Plants over-expressing LlCYP lacking the KDEL sequence show reduced growth and early senescence. Immunogold staining and confocal analyses indicate that in young tissues the protein is retained in the ER, while during floral senescence it is localised to the vacuole. Our data therefore suggest that the vacuole may be the site of action for at least this KDEL cysteine protease during tepal senescence 
650 4 |a Journal Article 
650 4 |a Cysteine proteases 
650 4 |a Endoplasmic reticulum 
650 4 |a Lilium 
650 4 |a Petal senescence 
650 4 |a Subcellular localisation 
650 4 |a Vacuole 
650 7 |a Luminescent Proteins  |2 NLM 
650 7 |a Oligopeptides  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Protein Sorting Signals  |2 NLM 
650 7 |a lysyl-aspartyl-glutamyl-leucine  |2 NLM 
650 7 |a 113516-56-6  |2 NLM 
650 7 |a Cysteine Proteases  |2 NLM 
650 7 |a EC 3.4.-  |2 NLM 
700 1 |a Lombardi, Lara  |e verfasserin  |4 aut 
700 1 |a Picciarelli, Piero  |e verfasserin  |4 aut 
700 1 |a Lorenzi, Roberto  |e verfasserin  |4 aut 
700 1 |a Frigerio, Lorenzo  |e verfasserin  |4 aut 
700 1 |a Rogers, Hilary J  |e verfasserin  |4 aut 
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