中山醫學大學機構典藏 CSMUIR:Item 310902500/11610
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    题名: A reversibly dissociable ternary complex formed by XpsL, XpsM and XpsN of the Xanthomonas campestris pv. campestris type II secretion apparatus
    作者: Tsai, Rong-Tzong
    Leu, Wei-Ming
    Chen, Ling-Yun
    Hu, Nien-Tai
    贡献者: 中山醫學大學
    日期: 2002
    上传时间: 2015-07-23T10:28:23Z (UTC)
    ISSN: 0264-6021
    摘要: The cytoplasmic membrane proteins XpsL, XpsM and XpsN are components required for type II secretion in Xanthomonas campestris pv. campestris. We performed metal-chelating chromatography to partially purify the His(6)-tagged XpsM (XpsMh)-containing complex. Immunoblot analysis revealed that both XpsL and XpsN co-eluted with XpsMh. The co-fractionated XpsL and XpsN proteins co-immune precipitated with each other, suggesting the existence of an XpsL-XpsM-XpsN complex. Ternary complex formation does not require other Xps protein components of the type II secretion apparatus. Further purification upon size-exclusion chromatography revealed that XpsN is prone to dissociate from the complex. Reassociation of XpsN with the XpsL-XpsMh complex immobilized on a nickel column is more effective than with XpsMh alone. Membrane-mixing experiments suggested that the XpsL-XpsMh complex and XpsN probably dissociate and reassociate in the membrane vesicles. Comparison of the half-lives of the XpsL-XpsMh-XpsN and XpsL-XpsMh complexes revealed that XpsL dissociates from the latter at a faster rate than from the former. Dissociation and reassociation between XpsL and XpsM were also demonstrated with membrane-mixing experiments. A dynamic model is proposed for the XpsL-XpsM-XpsN complex.
    URI: https://ir.csmu.edu.tw:8080/ir/handle/310902500/11610
    http://dx.doi.org/10.1042/BJ20020909
    關聯: Biochem J. 2002 Nov 1; 367(Pt 3): 865–871.
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