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首页> 外文期刊>Journal of bacteriology >Multicopy suppression: an approach to understanding intracellular functioning of the protein export system.
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Multicopy suppression: an approach to understanding intracellular functioning of the protein export system.

机译：多拷贝抑制：了解蛋白质输出系统细胞内功能的一种方法。

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摘要

Escherichia coli genes were cloned onto a multicopy plasmid and selected by the ability to restore growth and protein export defects caused by a temperature-sensitive secY or secA mutation. When secA51 was used as the primary mutation, only clones carrying groE, which specifies the chaperonin class of heat shock protein, were obtained. Selection using secY24 yielded three major classes of genes. The first class encodes another heat shock protein, HtpG; the most frequently obtained second class encodes a neutral histonelike protein, H-NS; and the third class, msyB, encodes a 124-residue protein of which 38 residues are acidic amino acids. Possible mechanisms of suppression as well as the significance and limitations of the multicopy suppression approach are discussed.
机译：将大肠杆菌基因克隆到多拷贝质粒上，并根据恢复由于温度敏感的secY或secA突变引起的生长和蛋白质输出缺陷的能力进行选择。当将secA51用作主要突变时，仅获得带有groE的克隆，该克隆指定了伴侣蛋白类的热休克蛋白。使用secY24的选择产生了三大类基因。第一类编码另一种热激蛋白HtpG。最常获得的第二类编码中性的组蛋白样蛋白H-NS。第三类msyB编码124个残基的蛋白质，其中38个残基为酸性氨基酸。讨论了可能的抑制机制以及多拷贝抑制方法的重要性和局限性。

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