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  Characterization of the Heat-Stable Proteome during Seed Germination in Arabidopsis with Special Focus on LEA Proteins

Ginsawaeng, O., Gorka, M., Erban, A., Heise, C., Brueckner, F., Hoefgen, R., et al. (2021). Characterization of the Heat-Stable Proteome during Seed Germination in Arabidopsis with Special Focus on LEA Proteins. International Journal of Molecular Sciences, 22(15): 8172. doi:10.3390/ijms22158172.

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Ginsawaeng, O.1, Author              
Gorka, M.2, Author              
Erban, A.3, Author              
Heise, C.1, Author              
Brueckner, F.4, Author              
Hoefgen, R.4, Author              
Kopka, J.3, Author              
Skirycz, A.2, Author              
Hincha, D. K.1, Author              
Zuther, E.1, Author              
Affiliations:
1Transcript Profiling, Infrastructure Groups and Service Units, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753306              
2Small-Molecule Signalling, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_2586692              
3Applied Metabolome Analysis, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753338              
4Amino Acid and Sulfur Metabolism, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753337              

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 Abstract: During seed germination, desiccation tolerance is lost in the radicle with progressing radicle protrusion and seedling establishment. This process is accompanied by comprehensive changes in the metabolome and proteome. Germination of Arabidopsis seeds was investigated over 72 h with special focus on the heat-stable proteome including late embryogenesis abundant (LEA) proteins together with changes in primary metabolites. Six metabolites in dry seeds known to be important for seed longevity decreased during germination and seedling establishment, while all other metabolites increased simultaneously with activation of growth and development. Thermo-stable proteins were associated with a multitude of biological processes. In the heat-stable proteome, a relatively similar proportion of fully ordered and fully intrinsically disordered proteins (IDP) was discovered. Highly disordered proteins were found to be associated with functional categories development, protein, RNA and stress. As expected, the majority of LEA proteins decreased during germination and seedling establishment. However, four germination-specific dehydrins were identified, not present in dry seeds. A network analysis of proteins, metabolites and amino acids generated during the course of germination revealed a highly connected LEA protein network.

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Language(s): eng - English
 Dates: 2021
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: DOI: 10.3390/ijms22158172
BibTex Citekey: ijms22158172
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Title: International Journal of Molecular Sciences
  Abbreviation : Int. J. Mol. Sci.
Source Genre: Journal
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Publ. Info: Basel, Switzerland : MDPI AG
Pages: - Volume / Issue: 22 (15) Sequence Number: 8172 Start / End Page: - Identifier: ISSN: 1422-0067
CoNE: https://pure.mpg.de/cone/journals/resource/1422-0067