Photosynthetic Regulation of the Cyanobacterium Synechocystis sp. PCC 6803 Thioredoxin System and Functional Analysis of TrxB （Trx x） and TrxQ （Trx y） Thioredoxins
Photosynthetic Regulation of the Cyanobacterium Synechocystis sp. PCC 6803 Thioredoxin System and Functional Analysis of TrxB （Trx x） and TrxQ （Trx y） Thioredoxins作者机构：Instituto de Bioquimica Vegetal y Fotosintesis Universidad de Sevilla-CSIC Avda Americo Vespucio 49 41092-Sevilla Spain
出 版 物：《Molecular Plant》 (分子植物（英文版）)
年 卷 期：2009年第2卷第2期
页 面：270-283页
核心收录：
学科分类：0710[理学-生物学] 09[农学] 0903[农学-农业资源与环境] 0901[农学-作物学] 090302[农学-植物营养学] 0902[农学-园艺学]
基 金：the Ministry of Science and Education F.J.F., and Junta de Andalucia
主 题：Cyanobacteria photosynthetic electron transport Synechocystis oxidative stress thioredoxin.
摘 要：The expression of the genes encoding the ferredoxin-thioredoxin system including the ferredoxin-thioredoxin reductase （FTR） genes ftrC and ftrV and the four different thioredoxin genes trxA （m-type; sir0623）, trxB （x-type; sir1139）, trxC （sll1057） and trxQ （y-type; sir0233） of the cyanobacterium Synechocystis sp. PCC 6803 has been studied according to changes in the photosynthetic conditions. Experiments of light-dark transition indicate that the expression of all these genes except trxQ decreases in the dark in the absence of glucose in the growth medium. The use of two electron transport inhibitors, 3-（3,4-dichlorophenyl）-1,1-dimethylurea （DCMU） and 2,5-dibromo-3-methyl-6-isopropyl-p- benzoquinone （DBMIB）, reveals a differential effect on thioredoxin genes expression being trxC and trxQ almost unaffected, whereas trxA, trxB, and the ftr genes are down-regulated. In the presence of glucose, DCMU does not affect gene expression but DBMIB still does. Analysis of the single TrxB or TrxQ and the double TrxB TrxQ Synechocystis mutant strains reveal different functions for each of these thioredoxins under different growth conditions. Finally, a Synechocystis strain was generated containing a mutated version of TrxB （TrxBC34S）, which was used to identify the potential in-vivo targets of this thioredoxin by a proteomic analysis.
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