Functional analysis of the Chloroplast GrpE (CGE) proteins from Arabidopsis thaliana

Copyright © 2019 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 139(2019) vom: 02. Juni, Seite 293-306
1. Verfasser: de Luna-Valdez, L A (VerfasserIn)
Weitere Verfasser: Villaseñor-Salmerón, C I, Cordoba, E, Vera-Estrella, R, León-Mejía, P, Guevara-García, A A
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2019
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Arabidopsis Chaperones Chloroplast Cochaperones GrpE Hsp70 Chloroplast Proteins HSP70 Heat-Shock Proteins Molecular Chaperones Plant Proteins
Beschreibung
Zusammenfassung:Copyright © 2019 Elsevier Masson SAS. All rights reserved.
The function of proteins depends on specific partners that regulate protein folding, degradation and protein-protein interactions, such partners are the chaperones and cochaperones. In chloroplasts, proteins belonging to several families of chaperones have been identified: chaperonins (Cpn60s), Hsp90s (Hsp90-5/Hsp90C), Hsp100s (Hsp93/ClpC) and Hsp70s (cpHsc70s). Several lines of evidence have demonstrated that cpHsc70 chaperones are involved in molecular processes like protein import, protein folding and oligomer formation that impact important physiological aspects in plants such as thermotolerance and thylakoid biogenesis. Despite the vast amount of data existing around the function of cpHcp70s chaperones, very little attention has been paid to the roles of DnaJ and GrpE cochaperones in the chloroplast. In this study, we performed a phylogenetic analysis of the chloroplastic GrpE (CGE) proteins from 71 species. Based on their phylogenetic relationships and on a motif enrichment analysis, we propose a classification system for land plants' CGEs, which include two independent groups with specific primary structure traits. Furthermore, using in vivo assays we determined that the two CGEs from A. thaliana (AtCGEs) complement the mutant phenotype displayed by a knockout E. coli strain defective in the bacterial grpE gene. Moreover, we determined in planta that the two AtCGEs are bona fide chloroplastic proteins, which form the essential homodimers needed to establish direct physical interactions with the cpHsc70-1 chaperone. Finally, we found evidence suggesting that AtCGE1 is involved in specific physiological phenomena in A. thaliana, such as the chloroplastic response to heat stress, and the correct oligomerization of the photosynthesis-related LHCII complex
Beschreibung:Date Completed 26.06.2019
Date Revised 30.09.2020
published: Print-Electronic
Citation Status MEDLINE
ISSN:1873-2690
DOI:10.1016/j.plaphy.2019.03.027