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Published on December 24, 2008; 10.1104/pp.108.128314

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Received August 22, 2008
Accepted December 22, 2008

A SMALL FAMILY OF CHLOROPLAST ATYPICAL THIOREDOXINS

Inbal Dangoor , Hadas Peled-Zehavi , Alexander Levitan , Ohad Pasand , and Avihai Danon *

Department of Plant Sciences, Weizmann Institute of Science, Rehovot, 76100, Israel

* Corresponding author; email: Avihai.Danon{at}weizmann.ac.il.

The reduction and the formation of regulatory disulfide bonds serve as a key signaling element in chloroplasts. Members of the thioredoxins superfamily of oxidoreductases play a major role in these processes. We have characterized a small family of plant specific thioredoxins in Arabidopsis thaliana that are rich in cysteine and histidine residues, and are typified by a variable non-canonical redox active site. We found that the redox midpoint potential of three selected family members is significantly less reducing than that of the classic thioredoxins. Assays of subcellular localization demonstrated that all proteins are localized to the chloroplast. Selected members showed high activity, contingent on a dithiol electron donor, towards the chloroplast 2-Cys peroxiredoxin A, and poor activity towards the chloroplast NADP-malate dehydrogenase. The expression profile of the family members suggests that they have distinct roles. The intermediate redox midpoint potential value of the atypical thioredoxins might imply adaptability to function in modulating the redox state of chloroplast proteins with regulatory disulfides.






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