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斯莱德金属沙佩龙向铁硫生物发生路径和TCA循环

Milica Denic^1,2, Evelyne Turlin¹, Deborah B Zamble^3,4

¹Unité Pathogenèse de Helicobacter, Département de Microbiologie, UMR CNRS 6047, Institut Pasteur, Université Paris Cité , Paris, France.

|August 16, 2023

概括

这项研究确定了SlyD,一种蛋白质折叠伴侣的新细菌蛋白质点. SlyD调节参与新陈代谢和辅助因子形成的酶,影响细胞应激反应.

科学领域:

生物化学生物化学
分子生物学分子生物学
微生物学微生物学

背景情况:

蛋白质折叠对于细胞功能至关重要,像SlyD这样的基基-基异相酶 (PPIases) 起着关键作用.
已知很少有细菌PPIase点,这限制了我们对它们在细胞过程中的作用的理解.
SlyD是一种具有金属沙佩龙活性的独特PPIase,表明其功能多样化.

研究的目的:

为了确定SlyD PPIase-metallochaperone从大肠杆菌和杆菌的新型蛋白质标.
在细菌生理学中研究SlyD-蛋白相互作用的功能影响.
阐明SlyD在调节代谢途径和辅因子生物合成中的作用.

主要方法:

大规模的酵母双混合选,以识别SlyD相互作用蛋白质.
*大肠杆菌*和*H. pylori ∆slyD*突变体的构造和表型分析.
生物化学分析测量细胞内ATP,质子动力和酶活性.

主要成果:

SlyD与参与金属辅因子利用,三碳酸 (TCA) 循环和铁硫 (Fe-S) 集群形成的酶相互作用.
*∆slyD*突变体对抗生素和氧化压力的敏感性降低.
在*H. pylori*中,SlyD调节TCA循环酶,可能通过控制Fe-S集群生物发生.

结论:

SlyD针对一系列重要的酶,包括中央代谢和辅因子合成中的酶.
SlyD对Fe-S集群形成的调节会影响细菌的抗压力和代谢活动.
这项工作扩展了细菌中PPIases已知的功能,突出了SlyD的关键作用.

关键词:

埃舍里希亚大肠杆菌 (Escherichia coli) 是一个大肠杆菌.在Fe-S集群中.在Helicobacter Pylori的研究中,这是一个PPIase.对于ROS的敏感性在TCA循环中,TCA循环是抗生素敏感性抗生素敏感性一个是金属的chaperone.蛋白质的陪伴者是一个人.

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