4.5 Article

Characterization of thioredoxin y, a new type of thioredoxin identified in the genome of Chlamydomonas reinhardtii

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FEBS LETTERS
卷 543, 期 1-3, 页码 87-92

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ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(03)00416-2

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fructose-1,6-bisphosphate phosphatase; NADP-malate dehydrogenase; peroxiredoxin; thioredoxin; Chlamydomonas reinhardtii

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The sequencing of the Arabidopsis genome revealed a multiplicity of thioredoxins (TRX), ubiquitous protein disulfide oxido-reductases. We have analyzed the TRX family in the genome of the unicellular green alga Chlamydomonas reinhardtii and identified eight different thioredoxins for which we have cloned and sequenced the corresponding cDNAs. One of these TRXs represents a new type that we named TRX y. This most probably chloroplastic TRX is highly conserved in photosynthetic organisms. The biochemical characterization of the recombinant protein shows that it exhibits a thermal stability profile and specificity toward target enzymes completely different from those of TRXs characterized so far. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

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