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首页> 外文期刊>Journal of bacteriology >Genetic Dissection of the Outer Membrane Secretin PulD: Are There Distinct Domains for Multimerization and Secretion Specificity?
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Genetic Dissection of the Outer Membrane Secretin PulD: Are There Distinct Domains for Multimerization and Secretion Specificity?

机译：外膜促胰液素PulD的遗传解剖：是否有不同的域的多聚化和分泌特异性？

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Linker and deletion mutagenesis and gene fusions were used to probe the possible domain structure of the dodecameric outer membrane secretin PulD from the pullulanase secretion pathway ofKlebsiella oxytoca. Insertions of 24 amino acids close to or within strongly predicted and highly conserved amphipathic β strands in the C-terminal half of the polypeptide (the β domain) abolished sodium dodecyl sulfate (SDS)-resistant multimer formation that is characteristic of this protein, whereas insertions elsewhere generally had less dramatic effects on multimer formation. However, the β domain alone did not form SDS-resistant multimers unless part of the N-terminal region of the protein (the N domain) was produced intrans. All of the insertions except one, close to the C terminus of the protein, abolished function. The N domain alone was highly unstable and did not form SDS-resistant multimers even when the β domain was present in trans. We conclude that the β domain is a major determinant of multimer stability and that the N domain contributes to multimer formation. The entire or part of the N domain of PulD could be replaced by the corresponding region of the OutD secretin from the pectate lyase secretion pathway of Erwinia chrysanthemi without abolishing pullulanase secretion. This suggests that the N domain of PulD is not involved in substrate recognition, contrary to the role proposed for the N domain of OutD, which binds specifically to pectate lyase secreted by E. chrysanthemi (V. E. Shevchik, J. Robert-Badouy, and G. Condemine, EMBO J. 16:3007–3016, 1997).
机译：利用连接子和缺失诱变以及基因融合，从产酸克雷伯菌的支链淀粉酶分泌途径探究十二聚体外膜分泌蛋白PulD的可能结构域。在多肽的C末端一半（β结构域）中，在强预测和高度保守的两亲性β链附近或之内插入24个氨基酸消除了该蛋白的十二烷基硫酸钠（SDS）抗性多聚体形成，而插入其他地方通常对多聚体形成的影响较小。但是，除非在 trans 中产生了蛋白质N端区域的一部分（N域），否则单独的β结构域不会形成SDS抗性多聚体。除一个外，所有接近蛋白质C末端的插入都丧失了功能。单独的N结构域非常不稳定，即使 trans 中存在β结构域，也不会形成抗SDS的多聚体。我们得出的结论是，β结构域是决定多聚体稳定性的主要因素，而N结构域则有助于形成多聚体。 PulD的N结构域的全部或部分可以被 Erwinia chrysanthemi 的果胶酸裂解酶分泌途径中的OutD分泌素的相应区域取代，而不会消除支链淀粉酶的分泌。这表明PulD的N结构域不参与底物识别，这与针对OutD的N结构域所提议的作用相反，后者的作用与 E分泌的果胶酸裂合酶特异性结合。 chrysanthemi （V. E. Shevchik，J. Robert-Badouy，and G. Condemine，EMBO J. 16：3007-3016，1997）。

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