Profound redox sensitivity of peptidyl‐prolyl isomerase activity in Arabidopsis thylakoid lumen
- 5 June 2006
- journal article
- Published by Wiley in FEBS Letters
- Vol. 580 (15), 3671-3676
- https://doi.org/10.1016/j.febslet.2006.05.054
Abstract
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 chloroplastsKeywords
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