Specific Hsp100 Chaperones Determine the Fate of the First Enzyme of the Plastidial Isoprenoid Pathway for Either Refolding or Degradation by the Stromal Clp Protease in Arabidopsis

• Published in: PLoS genetics Vol. 12; no. 1; p. e1005824
• Main Authors: Pulido, Pablo, Llamas, Ernesto, Llorente, Briardo, Ventura, Salvador, Wright, Louwrance P., Rodríguez-Concepción, Manuel
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 01.01.2016; Public Library of Science (PLoS)
• Subjects: Analysis; Arabidopsis; Arabidopsis Proteins - genetics; Arabidopsis thaliana; Biology and Life Sciences; Chloroplasts; Chloroplasts - genetics; Chloroplasts - metabolism; Endopeptidase Clp - genetics; Endopeptidase Clp - metabolism; Enzymes; Experiments; Gene expression; Genetic aspects; Heat shock proteins; Heat-Shock Proteins - genetics; Heat-Shock Proteins - metabolism; Metabolic Networks and Pathways - genetics; Metabolism; Metabolites; Molecular Chaperones - genetics; Observations; Physiological aspects; Plastids; Plastids - genetics; Plastids - metabolism; Proteases; Protein Folding; Proteolysis; Quality control; Research and Analysis Methods; Terpenes - metabolism; Transferases - genetics

The lifespan and activity of proteins depend on protein quality control systems formed by chaperones and proteases that ensure correct protein folding and prevent the formation of toxic aggregates. We previously found that the Arabidopsis thaliana J-protein J20 delivers inactive (misfolded) forms of...