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首页> 外文期刊>Journal of Molecular Biology >Mycobacterium tuberculosis GroEL homologues unusually exist as lower oligomers and retain the ability to suppress aggregation of substrate proteins
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Mycobacterium tuberculosis GroEL homologues unusually exist as lower oligomers and retain the ability to suppress aggregation of substrate proteins

机译：结核分枝杆菌GroEL同源物以低聚物形式异常存在，并保留抑制底物蛋白聚集的能力

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Chaperonin-60s are large double ring oligomeric proteins with a central cavity where unfolded polypeptides undergo productive folding. In conjunction with their co-chaperonin, Chaperonin-60s bind non-native polypeptides and facilitate their refolding in an ATP-dependent manner. The ATPase activity of Chaperonin-60 is tightly regulated by the 10 kDa co-chaperonin. In contrast to most other bacterial species, Mycobacterium tuberculosis genome carries a duplicate set of cpn60 genes, one of which occurs on the groESL operon (cpn60.1), while the other is separately arranged on the chromosome (cpn60.2). Biophysical characterization of the mycobacterial proteins showed that these proteins exist as lower oligomers and not tetradecamers, an unexpected property much different from the other known Chaperonin-60s. Failure of the M. tuberculosis chaperonins to oligomerize can be attributed to amino acid mutations at the oligomeric interface. Rates of ATP hydrolysis of the M. tuberculosis chaperonins showed that these proteins possess a very weak ATPase activity. Both the M. tuberculosis chaperonins were partially active in refolding substrate proteins. Interestingly, their refolding activity was seen to be independent of the co-chaperonin and ATP. We hypothesize that the ATP independent chaperones might offer benefit to the pathogen by promoting its existence in the latent phase of its life cycle. (C) 2004 Elsevier Ltd. All rights reserved.
机译：伴侣蛋白60s是具有中心腔的大的双环寡聚蛋白，未折叠的多肽在此处进行生产性折叠。伴侣蛋白60s与它们的伴侣蛋白结合，结合非天然多肽，并以ATP依赖的方式促进它们的折叠。伴侣蛋白60的ATPase活性受到10 kDa伴侣蛋白的严格调控。与大多数其他细菌物种相反，结核分枝杆菌基因组携带一组重复的cpn60基因，其中一个出现在groESL操纵子（cpn60.1）上，另一个出现在染色体上（cpn60.2）。分枝杆菌蛋白的生物物理特征表明，这些蛋白以较低的低聚物而不是四聚体的形式存在，这是与其他已知的伴侣蛋白60s出乎意料的特性。结核分枝杆菌伴侣蛋白未能寡聚可归因于寡聚体界面处的氨基酸突变。结核分枝杆菌伴侣蛋白的ATP水解速率表明这些蛋白具有非常弱的ATPase活性。两种结核分枝杆菌伴侣蛋白都在重折叠底物蛋白上部分活性。有趣的是，它们的重折叠活性被认为独立于伴侣蛋白和ATP。我们假设ATP独立的伴侣可能通过促进其生命周期潜伏期的存在而为病原体提供好处。 （C）2004 Elsevier Ltd.保留所有权利。

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