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Presence of a Mitovirus Is Associated with Alteration of the Mitochondrial Proteome, as Revealed by Protein-Protein Interaction (PPI) and Co-Expression Network Models in Chenopodium quinoa Plants.
Di Silvestre, Dario; Passignani, Giulia; Rossi, Rossana; Ciuffo, Marina; Turina, Massimo; Vigani, Gianpiero; Mauri, Pier Luigi.
Afiliação
  • Di Silvestre D; Laboratory of Proteomics and Metabolomics, Institute for Biomedical Technologies (ITB), Department of Biomedical Sciences, National Research Council (CNR), 20054 Milan, Italy.
  • Passignani G; Laboratory of Proteomics and Metabolomics, Institute for Biomedical Technologies (ITB), Department of Biomedical Sciences, National Research Council (CNR), 20054 Milan, Italy.
  • Rossi R; Laboratory of Proteomics and Metabolomics, Institute for Biomedical Technologies (ITB), Department of Biomedical Sciences, National Research Council (CNR), 20054 Milan, Italy.
  • Ciuffo M; Institute for Sustainable Plant Protection, Department of Bio-Food Sciences, National Research Council (CNR), 10135 Turin, Italy.
  • Turina M; Institute for Sustainable Plant Protection, Department of Bio-Food Sciences, National Research Council (CNR), 10135 Turin, Italy.
  • Vigani G; Plant Physiology Unit, Department of Life Sciences and Systems Biology, University of Turin, 10135 Turin, Italy.
  • Mauri PL; Laboratory of Proteomics and Metabolomics, Institute for Biomedical Technologies (ITB), Department of Biomedical Sciences, National Research Council (CNR), 20054 Milan, Italy.
Biology (Basel) ; 11(1)2022 Jan 08.
Article em En | MEDLINE | ID: mdl-35053093
ABSTRACT
Plant mitoviruses belong to Mitoviridae family and consist of positive single-stranded RNA genomes replicating exclusively in host mitochondria. We previously reported the biological characterization of a replicating plant mitovirus, designated Chenopodium quinoa mitovirus 1 (CqMV1), in some Chenopodium quinoa accessions. In this study, we analyzed the mitochondrial proteome from leaves of quinoa, infected and not infected by CqMV1. Furthermore, by protein-protein interaction and co-expression network models, we provided a system perspective of how CqMV1 affects mitochondrial functionality. We found that CqMV1 is associated with changes in mitochondrial protein expression in a mild but well-defined way. In quinoa-infected plants, we observed up-regulation of functional modules involved in amino acid catabolism, mitochondrial respiratory chain, proteolysis, folding/stress response and redox homeostasis. In this context, some proteins, including BCE2 (lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex), DELTA-OAT (ornithine aminotransferase) and GR-RBP2 (glycine-rich RNA-binding protein 2) were interesting because all up-regulated and network hubs in infected plants; together with other hubs, including CAT (catalase) and APX3 (L-ascorbate peroxidase 3), they play a role in stress response and redox homeostasis. These proteins could be related to the higher tolerance degree to drought we observed in CqMV1-infected plants. Although a specific causative link could not be established by our experimental approach at this stage, the results suggest a new mechanistic hypothesis that demands further in-depth functional studies.
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Texto completo: 1 Base de dados: MEDLINE Tipo de estudo: Risk_factors_studies Idioma: En Revista: Biology (Basel) Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Itália

Texto completo: 1 Base de dados: MEDLINE Tipo de estudo: Risk_factors_studies Idioma: En Revista: Biology (Basel) Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Itália