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首页> 外文期刊>Archives of microbiology >Localization of Mn(II)-oxidizing activity and the putative multicopper oxidase, MnxG, to the exosporium of the marine Bacillus sp strain SG-1
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Localization of Mn(II)-oxidizing activity and the putative multicopper oxidase, MnxG, to the exosporium of the marine Bacillus sp strain SG-1

机译：Mn（II）氧化活性和假定的多铜氧化酶MnxG在海洋芽孢杆菌属菌株SG-1的外孢子中的定位

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摘要

Dormant spores of the marine Bacillus sp. strain SG-1 catalyze the oxidation of manganese(II), thereby becoming encrusted with insoluble Mn(III,IV) oxides. In this study, it was found that the Mn(II)-oxidizing activity could be removed from SG-1 spores using a French press and recovered in the supernatant following centrifugation of the spores. Transmission electron microscopy of thin sections of SG-1 spores revealed that the ridged outermost layer was removed by passage through the French press, leaving the remainder of the spore intact. Comparative chemical analysis of this layer with the underlying spore coats suggested that this outer layer is chemically distinct from the spore coat. Taken together, these results indicate that this outer layer is an exosporium. Previous genetic analysis of strain SG-1 identified a cluster of genes involved in Mn(H) oxidation, the mnx genes. The product of the most downstream gene in this cluster, MnxG, appears to be a multicopper oxidase and is essential for Mn(II) oxidation. In this study, MnxG was overexpressed in Escherichia coli and used to generate polyclonal antibodies. Western blot analysis demonstrated that MnxG is localized to the exosporium of wild-type spores but is absent in the non-oxidizing spores of transposon mutants within the mnx gene cluster. To our knowledge, Mn(II) oxidation is the first oxidase activity, and MnxG one of the first gene products, ever shown to be associated with an exosporium. [References: 31]
机译：海洋芽孢杆菌的休眠孢子。菌株SG-1催化锰（II）的氧化，从而被不溶的Mn（III，IV）氧化物包裹。在这项研究中，发现可以使用法国压力机从SG-1孢子中去除Mn（II）氧化活性，并在离心孢子后在上清液中将其回收。 SG-1孢子薄片的透射电子显微镜显示，通过法式压滤机除去了最脊的外层，剩下的孢子则完好无损。对该层与下面的孢子涂层的比较化学分析表明，该外层在化学上不同于孢子涂层。总而言之，这些结果表明该外层是外孢子。先前对SG-1菌株进行的遗传分析确定了与Mn（H）氧化有关的一组基因，即mnx基因。此簇中最下游基因的产物MnxG似乎是一种多铜氧化酶，对于Mn（II）氧化至关重要。在这项研究中，MnxG在大肠杆菌中过表达，并用于产生多克隆抗体。蛋白质印迹分析表明，MnxG位于野生型孢子的孢子囊外，但在mnx基因簇内的转座子突变体的非氧化孢子中不存在。据我们所知，Mn（II）氧化是第一种氧化酶活性，而MnxG是最早的基因产物之一，曾经证明与外孢子菌有关。 [参考：31]

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