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

Battelli, Riccardo, Lombardi, Lara, Picciarelli, Piero, Lorenzi, Roberto, Frigerio, Lorenzo and Rogers, Hilary Joan 2014. Expression and localisation of a senescence-associated KDEL-cysteine protease from Lilium longiflorum tepals. Plant Science 214 , pp. 38-46. 10.1016/j.plantsci.2013.09.011

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Abstract

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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Subjects: Q Science > QK Botany
Uncontrolled Keywords: Cysteine proteases; Endoplasmic reticulum; Lilium; Petal senescence; Subcellular localisation; Vacuole
Additional Information: PDF uploaded in accordance with publisher's policies at http://www.sherpa.ac.uk/romeo/issn/0168-9452/ (accessed 11.02.16). Available online 27 September 2013
Publisher: Elsevier
ISSN: 0168-9452
Date of Acceptance: 21 September 2013
Last Modified: 03 Jul 2019 02:51
URI: http://orca.cf.ac.uk/id/eprint/52661

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