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Reboot the system thanks to protein post-translational modifications and proteome diversity: How quiescent seeds restart their metabolism to prepare seedling establishment.
- Source :
-
Proteomics [Proteomics] 2011 May; Vol. 11 (9), pp. 1606-18. Date of Electronic Publication: 2011 Mar 23. - Publication Year :
- 2011
-
Abstract
- Once liberated in their environment, orthodox seeds live in a quiescent dehydrated state not totally exempt of essential molecular events as, for example, the capacity of breaking dormancy during after-ripening. Upon imbibition, if internal regulatory padlocks are released and given adequate external conditions, the quiescent seed is able to "reboot" its system and, thus, germinate. Recent studies unraveled the crucial importance of protein PTMs in seed dormancy, longevity and vigor. As compared to other plant developmental stages, the seed proteome appears quite unique and diverse. Seed proteins encompass several functional classes from primary and secondary metabolism to structural and antimicrobial defense. In the dry state, oxidative damages can occur due to reactive oxygen and nitrogen species produced by non-enzymatic reactions. These reactive species can affect proteins by the oxidation of their amino acids in a post-translational manner. The hormone abscisic acid regulates major aspects of seed life including dormancy and germination. This signaling pathway has been shown to rely on several PTMs such as protein phosphorylation or ubiquitination.<br /> (Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
- Subjects :
- Abscisic Acid metabolism
Abscisic Acid pharmacology
Gibberellins metabolism
Gibberellins pharmacology
Plant Development
Plant Growth Regulators metabolism
Plant Growth Regulators pharmacology
Plants metabolism
Seedlings metabolism
Seeds growth & development
Seeds metabolism
Signal Transduction drug effects
Plant Proteins metabolism
Protein Processing, Post-Translational
Proteome metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1615-9861
- Volume :
- 11
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- Proteomics
- Publication Type :
- Academic Journal
- Accession number :
- 21433284
- Full Text :
- https://doi.org/10.1002/pmic.201000641