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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Proteomics gives insight into the regulatory function of chloroplast thioredoxins
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Proteomics gives insight into the regulatory function of chloroplast thioredoxins

机译：蛋白质组学深入了解叶绿体硫氧还蛋白的调节功能

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摘要

Thioredoxins are small multifunctional redox active proteins widely if not universally distributed among living organisms. In chloroplasts, two types of thioredoxins (f and m) coexist and play central roles in regulating enzyme activity. Reduction of thioredoxins in chloroplasts is catalyzed by an iron-sulfur disulfide enzyme, ferredoxin-thioredoxin reductase, that receives photosynthetic electrons from ferredoxin, thereby providing a link between light and enzyme activity. Chloroplast thioredoxins function in the regulation of the Calvin cycle and associated processes. However, the relatively small number of known thioredoxin-linked proteins (about 16) raised the possibility that others remain to be identified. To pursue this opportunity, we have mutated thioredoxins f and m, such that the buried cysteine of the active disulfide has been replaced by serine or alanine, and bound them to affinity columns to trap target proteins of chloroplast stroma. The covalently linked proteins were eluted with DTT, separated on gels, and identified by mass spectrometry. This approach led to the identification of 15 potential targets that function in 10 chloroplast processes not known to be thioredoxin linked. Included are proteins that seem to function in plastid-to-nucleus signaling and in a previously unrecognized type of oxidative regulation. Approximately two-thirds of these targets contained conserved cysteines. We also identified 11 previously unknown and 9 confirmed target proteins that are members of pathways known to be regulated by thioredoxin. in contrast to results with individual enzyme assays, specificity for thioredoxin f or m was not observed on affinity chromatography. [References: 56]
机译：硫氧还蛋白是一种小型的多功能氧化还原活性蛋白，如果不能在生物体内广泛分布的话。在叶绿体中，两种类型的硫氧还蛋白（f和m）共存并在调节酶活性中起核心作用。叶绿体中硫氧还蛋白的还原是由铁硫二硫化酶铁氧还蛋白-硫氧还蛋白还原酶催化的，该酶从铁氧还蛋白接收光合电子，从而在光和酶活性之间建立联系。叶绿体硫氧还蛋白在加尔文循环和相关过程的调节中起作用。但是，相对较少的已知硫氧还蛋白连接蛋白（约16种）增加了仍有待鉴定的可能性。为了抓住这个机会，我们对硫氧还蛋白f和m进行了突变，以使活性二硫键的掩埋半胱氨酸被丝氨酸或丙氨酸取代，并将它们结合到亲和柱上，以捕获叶绿体基质的目标蛋白。共价连接的蛋白质用DTT洗脱，在凝胶上分离，并通过质谱鉴定。该方法导致鉴定出在10个叶绿体过程中起作用的15个潜在靶标，这些过程未知与硫氧还蛋白相关。其中包括似乎在质体至细胞核信号转导以及以前无法识别的氧化调节中起作用的蛋白质。这些靶标中大约三分之二包含保守的半胱氨酸。我们还确定了11种先前未知的蛋白和9种已确认的靶蛋白，它们是已知受硫氧还蛋白调节的途径的成员。与单个酶分析的结果相反，在亲和色谱上未观察到对硫氧还蛋白f或m的特异性。 [参考：56]

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