Profound redox sensitivity of peptidyl-prolyl isomerase activity in Arabidopsis thylakoid lumen
2006 (English)In: FEBS Letters, ISSN 0014-5793, Vol. 580, no 15, 3671-3676 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2006. Vol. 580, no 15, 3671-3676 p.
Immunophilin; FKBP; Cyclophilin; Peptidyl-prolyl isomerase; Thylakoid lumen; Arabidopsis thaliana
National CategoryMedical and Health Sciences
IdentifiersURN: urn:nbn:se:liu:diva-14357DOI: 10.1016/j.febslet.2006.05.054OAI: oai:DiVA.org:liu-14357DiVA: diva2:23308