Proteome analysis of Physcomitrella patens exposed to progressive dehydration and rehydration
Physcomitrella patens is an extremely dehydration-tolerant moss. However, the molecular basis of its responses to loss of cellular water remains unclear. A comprehensive proteomic analysis of dehydration- and rehydration-responsive proteins has been conducted using quantitative two-dimensional diffe...
| Publié dans: | Journal of experimental botany. - 1985. - 63(2012), 2 vom: 13. Jan., Seite 711-26 |
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| Auteur principal: | |
| Autres auteurs: | , , , , , , |
| Format: | Article en ligne |
| Langue: | English |
| Publié: |
2012
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| Accès à la collection: | Journal of experimental botany |
| Sujets: | Journal Article Research Support, Non-U.S. Gov't Plant Proteins Proteome late embryogenesis abundant protein, plant Water 059QF0KO0R |
| Résumé: | Physcomitrella patens is an extremely dehydration-tolerant moss. However, the molecular basis of its responses to loss of cellular water remains unclear. A comprehensive proteomic analysis of dehydration- and rehydration-responsive proteins has been conducted using quantitative two-dimensional difference in-gel electrophoresis (2D-DIGE), and traditional 2-D gel electrophoresis (2-DE) combined with MALDI TOF/TOF MS. Of the 216 differentially-expressed protein spots, 112 and 104 were dehydration- and rehydration-responsive proteins, respectively. The functional categories of the most differentially-expressed proteins were seed maturation, defence, protein synthesis and quality control, and energy production. Strikingly, most of the late embryogenesis abundant (LEA) proteins were expressed at a basal level under control conditions and their synthesis was strongly enhanced by dehydration, a pattern that was confirmed by RT-PCR. Actinoporins, phosphatidylethanolamine-binding protein, arabinogalactan protein, and phospholipase are the likely dominant players in the defence system. In addition, 24 proteins of unknown function were identified as novel dehydration- or rehydration-responsive proteins. Our data indicate that Physcomitrella adopts a rapid protein response mechanism to cope with dehydration in its leafy-shoot and basal expression levels of desiccation-tolerant proteins are rapidly upgraded at high levels under stress. This mechanism appears similar to that seen in angiosperm seeds |
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| Description: | Date Completed 10.01.2014 Date Revised 17.03.2022 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1460-2431 |
| DOI: | 10.1093/jxb/err296 |