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Profound redox sensitivity of peptidyl‐prolyl isomerase activity in Arabidopsis thylakoid lumen
Author(s) -
Shapiguzov Alexey,
Edvardsson Anna,
Vener Alexander V.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.05.054
Subject(s) - thylakoid , biochemistry , arabidopsis , chloroplast , biology , isomerase , chemistry , enzyme , mutant , gene
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.