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首页> 外文期刊>Antibiotics >The Oligopeptide Permease Opp Mediates Illicit Transport of the Bacterial P-site Decoding Inhibitor GE81112 ?
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The Oligopeptide Permease Opp Mediates Illicit Transport of the Bacterial P-site Decoding Inhibitor GE81112 ?

机译：寡肽渗透酶Opp介导细菌P位点编码抑制剂GE81112的非法转运。

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摘要

GE81112 is a tetrapeptide antibiotic that binds to the 30S ribosomal subunit and specifically inhibits P-site decoding of the mRNA initiation codon by the fMet-tRNA anticodon. GE81112 displays excellent microbiological activity against some Gram-positive and Gram-negative bacteria in both minimal and complete, chemically defined, broth, but is essentially inactive in complete complex media. This is due to the presence of peptides that compete with the antibiotic for the oligopeptide permease system (Opp) responsible for its illicit transport into the bacterial cells as demonstrated in the cases of Escherichia coli and Bacillus subtilis . Mutations that inactivate the Opp system and confer GE81112 resistance arise spontaneously with a frequency of ca. 1 × 10 ?6 , similar to that of the mutants resistant to tri- l -ornithine, a known Opp substrate. On the contrary, cells expressing extrachromosomal copies of the opp genes are extremely sensitive to GE81112 in rich medium and GE81112-resistant mutations affecting the molecular target of the antibiotic were not detected upon examining >10 9 cells of this type. However, some mutations introduced in the 16S rRNA to confer kasugamycin resistance were found to reduce the sensitivity of the cells to GE81112.
机译：GE81112是一种四肽抗生素，可与30S核糖体亚基结合，并特异性抑制fMet-tRNA反密码子对mRNA起始密码子的P位解码。 GE81112在极少量和完整的化学成分明确的肉汤中均显示出对某些革兰氏阳性和革兰氏阴性细菌极好的微生物活性，但在完全复杂的培养基中基本上没有活性。这是由于存在与抗生素竞争的肽，该寡肽渗透酶系统（Opp）负责将其非法运输到细菌细胞中，如大肠杆菌和枯草芽孢杆菌的情况所示。使Opp系统失活并赋予GE81112电阻的突变会自发出现，频率约为ca。 1×10？6，类似于对已知的Opp底物Tril -ornithine有抗性的突变体。相反，表达opp基因的染色体外拷贝的细胞在丰富的培养基中对GE81112极为敏感，并且在检查> 10 9个此类细胞后未检测到影响抗生素分子靶标的GE81112抗性突变。然而，发现在16S rRNA中引入的赋予春黄霉素抗性的某些突变降低了细胞对GE81112的敏感性。

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