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首页> 外文期刊>Journal of bacteriology >Role of primary structure and disulfide bond formation in beta-lactamase secretion.
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Role of primary structure and disulfide bond formation in beta-lactamase secretion.

机译：一级结构和二硫键形成在β-内酰胺酶分泌中的作用。

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摘要

Plasmid pBR322-encoded beta-lactamase was shown to contain a single disulfide bond, which caused the protein to migrate faster in sodium dodecyl sulfate-polyacrylamide gels than the fully reduced form. A similar difference in mobility of the in vitro synthesized precursor before and after reduction indicates that it also contained a disulfide bond. Formation of the disulfide bond in vivo, however, occurred concomitant with processing. In vivo accumulation of the precursor by inhibition of secretion did not allow disulfide bond formation to occur. This result is consistent with post-translational translocation of the precursor. Synthesis of a fragment of beta-lactamase lacking the carboxy terminus was obtained by insertion of a foreign DNA segment into the PstI site of bla. Processing and secretion of the protein did not appear to be greatly affected, indicating that the carboxy terminus is not required for secretion.
机译：已显示质粒pBR322编码的β-内酰胺酶含有单个二硫键，这导致蛋白质在十二烷基硫酸钠-聚丙烯酰胺凝胶中的迁移速度比完全还原的形式要快。还原前后体外合成的前体在迁移率上的相似差异表明它还含有二硫键。然而，体内二硫键的形成与加工同时发生。通过抑制分泌在体内积累前体不允许发生二硫键的形成。该结果与前体的翻译后移位一致。通过将外源DNA片段插入bla的PstI位点，获得了缺乏羧基末端的β-内酰胺酶片段的合成。蛋白质的加工和分泌似乎没有受到很大的影响，表明分泌不需要羧基末端。

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