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ABCC subfamily vacuolar transporters are involved in Pb (lead) detoxification in Saccharomyces cerevisiae

机译:ABCC亚家族液泡转运蛋白与酿酒酵母中的Pb(铅)解毒有关

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摘要

The present work has as objective to contribute for the elucidation of the mechanism associated with Pb detoxification, using the yeast Saccharomyces cerevisiae as a model organism. The deletion of GTT1 or GTT2 genes, coding for functional glutathione transferases (GST) enzymes in S. cerevisiae, caused an increased susceptibility to high Pb concentrations (5001000 mol L1). These results suggest that the formation of glutathione-Pb conjugate (GS-Pb), dependent of GSTs, is important in Pb detoxification. The involvement of ATP-binding cassette (ABC) vacuolar transporters, belonging to class C subfamily (ABCC) in vacuolar compartmentalization of Pb, was evaluated. For this purpose, mutant strains disrupted in YCF1, VMR1, YBT1 or BPT 1 genes were used. All mutants tested, without vacuolar ABCC transporters, presented an increased sensitivity to 5001000 mol L1 Pb comparative to wild-type strain. Taken together, the obtained results suggest that Pb detoxification, by vacuolar compartmentalization, can occur as a result of the concerted action of GSTs and vacuolar ABCC transporters. Pb is conjugated with glutathione, catalysed by glutathione transferases and followed to the transport of GS-Pb conjugate to the vacuole by ABCC transporters.
机译:本工作的目标是使用酵母酿酒酵母作为模型生物,为阐明与Pb解毒相关的机制做出贡献。酿酒酵母中编码功能性谷胱甘肽转移酶(GST)酶的GTT1或GTT2基因的缺失导致对高Pb浓度(5001000 mol L1)的敏感性增加。这些结果表明,依赖于GST的谷胱甘肽-Pb共轭物(GS-Pb)的形成在Pb排毒中很重要。评估了ATP结合盒(ABC)液泡转运蛋白(属于C类亚家族(ABCC))在Pb液泡分隔中的参与。为此,使用了在YCF1,VMR1,YBT1或BPT 1基因中被破坏的突变菌株。与野生型菌株相比,没有液泡ABCC转运蛋白的所有测试突变体对5001000 mol L1 Pb的敏感性都提高了。两者合计,获得的结果表明,由于GST和液泡ABCC转运蛋白的协同作用,可以通过液泡隔室进行Pb解毒。 Pb与谷胱甘肽偶联,由谷胱甘肽转移酶催化,然后由ABCC转运蛋白将GS-Pb偶联物转运至液泡。

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