Profound redox sensitivity of peptidyl-prolyl isomerase activity in Arabidopsis thylakoid lumen |
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Authors: | Shapiguzov Alexey Edvardsson Anna Vener Alexander V |
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Institution: | Division of Cell Biology, Link?ping University, SE-581 85 Link?ping, Sweden. |
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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 chloroplasts. |
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Keywords: | FKBP FK506 binding protein PPIase peptidyl-prolyl cis/trans isomerase |
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