Journal
FEBS LETTERS
Volume 580, Issue 15, Pages 3671-3676Publisher
WILEY
DOI: 10.1016/j.febslet.2006.05.054
Keywords
immunophilin; FKBP; cyclophilin; peptidyl-prolyl isomerase; thylakoid lumen; Arabidopsis thaliana
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Proteomic, enzymatic, and mutant analyses revealed that peptidyl-prolyl isomerase (PPIase) activity in the chloroplast thylakoid lumen of Arabidopsis is determined by two immunophilins: AtCYP20-2 and AtFKBP13. These two enzymes are responsible for PPIase activity in both soluble and membrane-associated fractions of thylakoid lumen suggesting that other lumenal immunophilins are not active towards the peptide substrates. In thiol-reducing conditions PPIase activity of the isolated AtFKBP13 and of the total thylakoid lumen is suppressed several fold. Profound redox-dependence of PPIase activity implies oxidative activation of protein folding catalysis under oxidative stress and photosynthetic oxygen production in the thylakoid lumen of plant chloroplasts. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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