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
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DOI：
10.1093/mp/ssn070
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发表时间：
2009-03-01
期刊：
影响因子：
27.5
通讯作者：
Florencio, Francisco J.
中科院分区：
文献类型：
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作者：
Esther Perez-Perez, M.;Martin-Figueroa, Eugenio;Florencio, Francisco J.
编码铁氧还蛋白-硫氧还蛋白系统的基因包括铁氧还蛋白-硫氧还蛋白还原酶(FTR)基因ftrC和ftrV，以及聚球藻的四个不同的硫氧还蛋白基因trxA(m型；slr0623)、trxB(x型；slr1139)、trxC(Sll1057)和trxQ(y型；slr0233)。根据光合作用条件的变化，对PCC6803进行了研究。明暗转换实验表明，除trxQ基因外，其余基因的表达均在无葡萄糖的条件下在黑暗中降低。两种电子传递抑制剂3-(3，4-二氯苯基)-1，1-二甲基脲(DCMU)和2，5-dibromo-3-methyl-6-isopropyl-p-benzoquinone(DBMIB)对硫氧还蛋白基因的表达有不同的影响，TrxC和trxQ几乎不受影响，而trxA、trxB和FTR基因表达下调。在葡萄糖存在下，DCMU不影响基因表达，但DBMIB仍然影响基因表达。对单个TrxB或TrxQ突变株和双TrxB TrxQ合胞菌突变株的分析表明，这些硫氧还蛋白在不同的生长条件下具有不同的功能。最后，产生了一株含有TrxB突变版本(TrxBC34S)的集胞藻菌株，用于通过蛋白质组学分析鉴定这种硫氧还蛋白的潜在体内靶点。
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; slr0623), trxB (x-type; slr1139), trxC (sll1057) and trxQ (y-type; slr0233) 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.