Degradome and Secretome of Pollination Drops of Ephedra

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dc.contributor.authorvon Aderkas, Patrick
dc.contributor.authorPrior, Natalie
dc.contributor.authorGagnon, Susannah
dc.contributor.authorLittle, Stefan
dc.contributor.authorCross, Tyra
dc.contributor.authorHardie, Darryl
dc.contributor.authorBorchers, Christoph
dc.contributor.authorThornburg, Robert
dc.contributor.authorHou, Chen
dc.contributor.authorLunny, Alexandra
dc.date.accessioned2016-08-17T16:24:24Z
dc.date.available2016-08-17T16:24:24Z
dc.date.copyright2015en_US
dc.date.issued2015-03
dc.description.abstractAlthough secreted proteins (a secretome) are known to occur in gymnosperm pollination drops, this study shows evidence for the presence of a protein degradome for the first time. A protein degradome is composed of protein and peptide fragments, a product of protein breakdown, whereas a secretome is composed of whole, secreted, and often biologically active extracellular proteins. Harvested Ephedra pollination drops from seven species were pooled either by collection date or, in the case of less abundant sample volumes, by species. Samples were processed by one of two methods: 1. gel electophoresis or by 2. liquid-liquid extraction, followed by chromatographic separation. Processed samples were trypsin-digested and analyzed with a Thermo Scientific LTQ Orbitrap Velos. On average, two-thirds of the detected and characterized proteins found in Ephedra spp. pollination drops were intracellular proteins, such as ubiquitin. The remaining third represent proteins known to be secreted, often involved in apoplastic processes such as defense and carbohydrate-modification, typical of known conifer pollination drop proteins. Characterized proteins detected in our comparative study of Ephedra spp drops ranged from 6 in E. monosperma to 20 in E. foeminea. We propose that the intracellular proteins detected are present as the result of nucellar tissue degeneration during pollination drop formation; previous proteomic investigations of pollination drops were in taxa that lack nucellar degeneration during drop formation Discovery of a degradome in pollination drops is novel and significant in that its presence has biological implications for pollination biology. We predict that degradomes in pollination drops are not restricted to Ephedra, but should also occur in species with nucellar tissue breakdown that coincides with pollination drop formation, such as in cycads and Ginkgo and some Pinaceae. Analysis of several collection dates of E. monosperma shows a large number of proteins that change over the course of the pollination drop secretion period, which suggests that variation in pollination drop contents over time may be important in the pollination biology of Ephdera.en_US
dc.description.reviewstatusRevieweden_US
dc.description.scholarlevelFacultyen_US
dc.description.sponsorshipThe authors would like to thank University of Victoria (UVic), UVic-Genome BC Proteomics Centre (UVic-GBCP), Genome Canada, and Genome BC for their support, as well as the Natural Sciences and Engineering Research Council of Canada (NSERC) for a Discovery Research Grant Program (PvA), and a Postgraduate Scholarship Program Grant (NAP). We acknowledge the expert assistance of B. Gowen (UVic), D. Smith (UVic) and Dr. Carol Parker (UVic-GBCP), as well as the invaluable assistance in sample collections from S. Ickert-Bond, C. Rydin, K. Bolinder, A. Rydberg, J. Jernstedt and I. Loera-Carrizales.en_US
dc.identifier.citationvon Aderkas, P., Prior, N., Gagnon, S., Little, S., Cross, T., Hardie, D., … Lunny, A. (2015). Degradome and secretome of pollination drops of Ephedra. Botanical Review, 81(1), 1-27.en_US
dc.identifier.urihttp://dx.doi.org/10.1007/s12229-014-9147-x
dc.identifier.urihttp://hdl.handle.net/1828/7444
dc.language.isoenen_US
dc.publisherBotanical Reviewen_US
dc.subjectdegradomeen_US
dc.subjectEphedraen_US
dc.subjectgymnosperm reproductionen_US
dc.subjectpollination dropen_US
dc.subjectproteomicsen_US
dc.subjectsecretomeen_US
dc.titleDegradome and Secretome of Pollination Drops of Ephedraen_US
dc.typePostprinten_US

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