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19 p, 1.6 MB 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 / Pulido, Pablo (Centre de Recerca en Agrigenòmica) ; Llamas, Ernesto (Centre de Recerca en Agrigenòmica) ; Llorente, Briardo (Centre de Recerca en Agrigenòmica) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Wright, Louwrance P. (Max Planck Institute for Chemical Ecology) ; Rodríguez Concepción, Manuel (Centre de Recerca en Agrigenòmica) ; Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí"
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 the plastidial enzyme deoxyxylulose 5-phosphate synthase (DXS) to the Hsp70 chaperone for either proper folding or degradation. [...]
2016 - 10.1371/journal.pgen.1005824
PLoS Genetics, Vol. 12, issue 1 (Jan. 2016) , e1005824  
Detailed record - Creative Commons

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