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首页> 外文期刊>Applied and Environmental Microbiology >Identification and Characterization of a Bacteroid-Specific Dehydrogenase Complex in Rhizobium leguminosarum PRE
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Identification and Characterization of a Bacteroid-Specific Dehydrogenase Complex in Rhizobium leguminosarum PRE

机译:豆根瘤菌中细菌特异性脱氢酶复合物的鉴定与表征

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In membranes of Rhizobium leguminosarum bacteroids isolated from nitrogen-fixing pea root nodules, two different protein complexes with NADH dehydrogenase activity were detected. One of these complexes, with a molecular mass of 110 kilodaltons, was also found in membranes of free-living rhizobia, but the other, with a molecular mass of 550 kilodaltons, appeared to be present only in bacteroids. The bacteroid-specific complex, referred to as DH1, probably consists of at least four different subunits. Using antibodies raised against the separate polypeptides, we found that a 35,000-molecular-weight polypeptide (35K polypeptide) in the DH1 complex is bacteroid specific, while the other proposed subunits were also detectable in cytoplasmic membranes of free-living bacteria. Dehydrogenase complex DH1 is also present in bacteroids of a R. leguminosarum nifA mutant, indicating that the synthesis of the dehydrogenase is not dependent on the gene product of this nif-regulatory gene. A possible involvement of the bacteroid-specific DH1 complex in electron transport to nitrogenase is discussed.
机译:在从固氮豌豆根瘤分离的豆根瘤菌菌膜中,检测到两种具有NADH脱氢酶活性的蛋白复合物。在自由生活的根瘤菌膜中也发现了一种分子量为110道尔顿的复合物,而另一种分子量为550道尔顿的络合物似乎仅存在于类细菌中。称为DH1的类细菌特异性复合物可能由至少四个不同的亚基组成。使用针对单独多肽的抗体,我们发现DH1复合物中35,000分子量的多肽(35K多肽)是类细菌特异性的,而其他提议的亚基也可以在自由生存细菌的细胞质膜中检测到。脱氢酶复合物DH1也存在于豆科念珠菌nifA突变体的类杆菌中,这表明脱氢酶的合成不依赖于该nif调控基因的基因产物。讨论了类细菌特异性DH1复合物可能参与电子转移到固氮酶的过程。

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