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ATP合酶是微菌素H47抗生素发挥作用所必需的。

ATP synthase is necessary for microcin H47 antibiotic action.

作者信息

Trujillo M, Rodríguez E, Laviña M

机构信息

Sección de Fisiología y Genética Bacterianas, Facultad de Ciencias, Iguá 4225, Montevideo 11.400, Uruguay.

出版信息

Antimicrob Agents Chemother. 2001 Nov;45(11):3128-31. doi: 10.1128/AAC.45.11.3128-3131.2001.

Abstract

Microcin H47 is a gene-encoded peptide antibiotic produced by a natural Escherichia coli strain isolated in Uruguay. In order to identify cellular components necessary for its antibiotic action, microcin H47-resistant mutants isolated in this work, as well as previously described mutants affected in membrane proteins, were analyzed. These studies indicated that (i) receptor outer membrane proteins for ferric-catechol siderophores would be involved in microcin-specific binding to the cell surface, (ii) the TonB pathway is needed for microcin H47 uptake, and (iii) the presence of the ATP synthase complex is necessary for microcin action. The possibility that this last structure contains the antibiotic target is discussed.

摘要

微菌素H47是由在乌拉圭分离出的一株天然大肠杆菌菌株产生的一种基因编码的肽抗生素。为了鉴定其抗生素作用所必需的细胞成分,对本研究中分离出的耐微菌素H47突变体以及先前描述的膜蛋白受影响的突变体进行了分析。这些研究表明:(i)铁-儿茶酚铁载体的受体外膜蛋白会参与微菌素与细胞表面的特异性结合;(ii)微菌素H47的摄取需要TonB途径;(iii)ATP合酶复合体的存在是微菌素发挥作用所必需的。文中还讨论了最后一种结构含有抗生素靶点的可能性。

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J Bacteriol. 1993 Sep;175(17):5420-7. doi: 10.1128/jb.175.17.5420-5427.1993.
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