Revisiting the stem proteome of Eucalyptus grandis and Eucalyptus globulus: Identification of temperature-induced changes.
Biomarkers
Label-free proteomics
Plant proteomics
Thermal stress
Journal
Biochimica et biophysica acta. Proteins and proteomics
ISSN: 1878-1454
Titre abrégé: Biochim Biophys Acta Proteins Proteom
Pays: Netherlands
ID NLM: 101731734
Informations de publication
Date de publication:
12 2020
12 2020
Historique:
received:
01
05
2020
revised:
13
08
2020
accepted:
15
08
2020
pubmed:
28
8
2020
medline:
15
12
2020
entrez:
28
8
2020
Statut:
ppublish
Résumé
Eucalyptus grandis and Eucalyptus globulus are important species for the Brazilian forestry industry. E. grandis plantations are mainly found in tropical regions, yet E. globulus plants are usually cultivated under moderate to low temperature conditions. As temperature seems to be a key factor for the planting of these species, we revisited our previously generated shotgun proteomics dataset to identify the main patterns of proteome regulation induced by thermal stimulus and to pinpoint specific proteins involved in the environmental response. Large-scale analysis has pointed out the different proteomic responses of E. grandis and E. globulus under temperature stimulus, with 296 proteins considered to be differentially regulated in the stems of Eucalyptus spp. grown at different temperatures. A stringent filtering approach was used to identify the most differentially regulated proteins. Through the stringent criteria, 66 proteins were found to be enriched in the plant species. Cultivation of E. globulus plants in low-temperature conditions induced the highest number of differentially regulated proteins. Additionally, metabolic proteins were mostly down-regulated, while stress-related proteins were majorly up-regulated in both species. Finally, the subset of the most differentially regulated proteins comprised new candidates of protein markers of temperature stress.
Identifiants
pubmed: 32853770
pii: S1570-9639(20)30177-1
doi: 10.1016/j.bbapap.2020.140530
pii:
doi:
Substances chimiques
Proteome
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
140530Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.