Lemaire S D, Collin V, Keryer E, Quesada A, Miginiac-Maslow M
Institut de Biotechnologie des Plantes, UMR 8618 CNRS, Université Paris-Sud, Bâtiment 630, 91405 Cedex, Orsay, France.
FEBS Lett. 2003 May 22;543(1-3):87-92. doi: 10.1016/s0014-5793(03)00416-2.
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.
拟南芥基因组测序揭示了多种硫氧还蛋白（TRX），即普遍存在的蛋白质二硫键氧化还原酶。我们分析了单细胞绿藻莱茵衣藻基因组中的TRX家族，鉴定出8种不同的硫氧还蛋白，并克隆和测序了相应的cDNA。其中一种TRX代表一种新型，我们将其命名为TRX y。这种很可能存在于叶绿体中的TRX在光合生物中高度保守。重组蛋白的生化特性表明，它具有与迄今所表征的TRX完全不同的热稳定性特征和对靶酶的特异性。
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