New thioredoxin targets in the unicellular photosynthetic eukaryote Chlamydomonas reinhardtii.

Abstract:

:Proteomics were used to identify the proteins from the eukaryotic unicellular green alga Chlamydomonas reinhardtii that can be reduced by thioredoxin. These proteins were retained specifically on a thioredoxin affinity column made of a monocysteinic thioredoxin mutant able to form mixed disulfides with its targets. Of a total of 55 identified targets, 29 had been found previously in higher plants or Synechocystis, but 26 were new targets. Biochemical tests were performed on three of them, showing a thioredoxin-dependent activation of isocitrate lyase and isopropylmalate dehydrogenase and a thioredoxin-dependent deactivation of catalase that is redox insensitive in Arabidopsis. In addition, we identified a Ran protein, a previously uncharacterized nuclear target in a photosynthetic organism. The metabolic and evolutionary implications of these findings are discussed.

authors

Lemaire SD,Guillon B,Le Maréchal P,Keryer E,Miginiac-Maslow M,Decottignies P

doi

10.1073/pnas.0402221101

keywords:

subject

Has Abstract

pub_date

2004-05-11 00:00:00

pages

7475-80

issue

19

eissn

0027-8424

issn

1091-6490

pii

0402221101

journal_volume

101

pub_type

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