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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Glutathione import in Haemophilus influenzae Rd is primed by the periplasmic heme-binding protein HbpA
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Glutathione import in Haemophilus influenzae Rd is primed by the periplasmic heme-binding protein HbpA

机译：流感嗜血杆菌Rd中谷胱甘肽的进口是由周质血红素结合蛋白HbpA引发的

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摘要

Glutathione (GSH) is a vital intracellular cysteine-containing tripep-tide across all kingdoms of life and assumes a plethora of cellular roles. Such pleiotropic behavior relies on a finely tuned spatiotem-poral distribution of glutathione and its conjugates, which is not only controlled by synthesis and breakdown, but also by transport. Here, we show that import of glutathione in the obligate human pathogen Haemophilus influenzae, a glutathione auxotrophe, is mediated by the ATP-binding cassette (ABC)-like dipeptide transporter DppBCDF, which is primed for glutathione transport by a dedicated periplasmic-binding protein (PBP). We have identified the periplasmic lipoprotein HbpA, a protein hitherto implicated in heme acquisition, as the cognate PBP that specifically binds reduced (GSH) and oxidized glutathione (GSSG) forms of glutathione with physiologically relevant affinity, while it exhibits marginal binding to hemin. Dissection of the ligand preferences of HbpA showed that HbpA does not recognize bulky glutathione S conjugates or glutathione derivatives with C-terminal modifications, consistent with the need for selective import of useful forms of glutathione and the concomitant exclusion of potentially toxic glutathione adducts. Structural studies of the highly homologous HbpA from Haemophilus parasuis in complex with GSSG have revealed the structural basis of the proposed novel function for HbpA-like proteins, thus allowing a delineation of highly conserved structure-sequence fingerprints for the entire family of HbpA proteins. Taken together, our studies unmask the main physiological role of HbpA and establish a paradigm for glutathione import in bacteria. Accordingly, we propose a name change for HbpA to glutathione-binding protein A.
机译：谷胱甘肽（GSH）是整个生命王国中至关重要的细胞内含半胱氨酸的三肽，它具有多种细胞作用。这种多效性行为依赖于谷胱甘肽及其结合物的时空分布的微调，这不仅受到合成和分解的控制，而且还受到运输的控制。在这里，我们显示，谷胱甘肽在专心的人类病原体流感嗜血杆菌（一种谷胱甘肽营养缺陷型）中的导入是由ATP结合盒（ABC）样二肽转运蛋白DppBCDF介导的，它通过专用的周质结合蛋白被用于谷胱甘肽的转运（PBP）。我们已经确定了迄今为止与血红素获得有关的周质脂蛋白HbpA，它是与生理性亲和力特异性结合还原型（GSH）和氧化型谷胱甘肽（GSSG）形式的同源PBP，并具有生理相关亲和力，同时表现出与血红素的边缘结合。对HbpA配体偏好的解剖表明，HbpA无法识别具有C末端修饰的庞大的谷胱甘肽S共轭物或谷胱甘肽衍生物，这与选择性输入有用形式的谷胱甘肽的需要以及随之而来的潜在毒性谷胱甘肽加合物的排除相一致。猪副嗜血杆菌高度同源的HbpA与GSSG的复合结构研究表明，拟议的HbpA样蛋白新功能具有结构基础，因此可以勾画整个HbpA蛋白家族的高度保守的结构序列指纹图谱。综上所述，我们的研究揭示了HbpA的主要生理作用，并建立了细菌中谷胱甘肽输入的范例。因此，我们提议将HbpA更改为谷胱甘肽结合蛋白A。

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  • 作者

    Bjorn Vergauwen; rnJonathan Elegheert; rnAnn Dansercoer; rnBart Devreese; rnSavvas N. Savvides;

  • 作者单位

    Laboratory for Protein Biochemistry and Biomolecular Engineering (L-ProBE), Department of Biochemistry and Microbiology, Ghent University, 9000 Ghent, Belgium;

    rnLaboratory for Protein Biochemistry and Biomolecular Engineering (L-ProBE), Department of Biochemistry and Microbiology, Ghent University, 9000 Ghent, Belgium;

    rnLaboratory for Protein Biochemistry and Biomolecular Engineering (L-ProBE), Department of Biochemistry and Microbiology, Ghent University, 9000 Ghent, Belgium;

    rnLaboratory for Protein Biochemistry and Biomolecular Engineering (L-ProBE), Department of Biochemistry and Microbiology, Ghent University, 9000 Ghent, Belgium;

    rnLaboratory for Protein Biochemistry and Biomolecular Engineering (L-ProBE), Department of Biochemistry and Microbiology, Ghent University, 9000 Ghent, Belgium;

  • 收录信息 美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    dipeptide permease; solute binding protein; GbpA; DppA;

    机译：二肽通透酶溶质结合蛋白GbpA;丙二醛;

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