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Efficient interaction between two GTPases allows the chloroplast SRP pathway to bypass the requirement for an SRP RNA

机译:两个GTPases之间的有效相互作用使叶绿体SRP途径绕过了对SRP RNA的需求

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摘要

Cotranslational protein targeting to membranes is regulated by two GTPases in the signal recognition particle (SRP) and the SRP receptor; association between the two GTPases is slow and is accelerated 400-fold by the SRP RNA. Intriguingly, the otherwise universally conserved SRP RNA is missing in a novel chloroplast SRP pathway. We found that even in the absence of an SRP RNA, the chloroplast SRP and receptor GTPases can interact efficiently with one another; the kinetics of interaction between the chloroplast GTPases is 400-fold faster than their bacterial homologues, and matches the rate at which the bacterial SRP and receptor interact with the help of SRP RNA. Biochemical analyses further suggest that the chloroplast SRP receptor is pre-organized in a conformation that allows optimal interaction with its binding partner, so that conformational changes during complex formation are minimized. Our results highlight intriguing differences between the classical and chloroplast SRP and SRP receptor GTPases, and help explain how the chloroplast SRP pathway can mediate efficient targeting of proteins to the thylakoid membrane in the absence of the SRP RNA, which plays an indispensable role in all the other SRP pathways.
机译:靶向膜的共翻译蛋白受信号识别颗粒(SRP)和SRP受体中的两个GTPases调控。两个GTPases之间的关联很慢,并且被SRP RNA加速了400倍。有趣的是,在新的叶绿体SRP途径中缺少了原本被普遍保存的SRP RNA。我们发现,即使在没有SRP RNA的情况下,叶绿体SRP和受体GTPases也可以彼此有效地相互作用。叶绿体GTPases之间相互作用的动力学比它们的细菌同源物快400倍,并且与细菌SRP和受体在SRP RNA的帮助下相互作用的速率相匹配。生化分析进一步表明,叶绿体SRP受体的构象是预先组织的,可以与其结合配偶体进行最佳相互作用,从而使复合物形成过程中的构象变化降至最低。我们的研究结果突显了经典与叶绿体SRP和SRP受体GTPases之间有趣的差异,并有助于解释在没有SRP RNA的情况下叶绿体SRP途径如何介导蛋白质对类囊体膜的有效靶向,这在所有SRP RNA中都起着不可或缺的作用。其他SRP途径。

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