Evolutionarily conserved mechanism for membrane recognition from bacteria to mitochondria,FEBS Letters

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Evolutionarily conserved mechanism for membrane recognition from bacteria to mitochondria
FEBS Letters ( IF 3.0 ) Pub Date : 2021-10-13 , DOI: 10.1002/1873-3468.14203
Tamar Szoke ₁ , Anat Nussbaum-Shochat ₁ , Orna Amster-Choder ₁

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The mechanisms controlling membrane recognition by proteins with one hydrophobic stretch at their carboxyl terminus (tail anchor, TA) are poorly defined. The Escherichia coli TAs of ElaB and YqjD, which share sequential and structural similarity with the Saccharomyces cerevisiae TA of Fis1, were shown to localize to mitochondria. We show that YqjD and ElaB are directed by their TAs to bacterial cell poles. Fis1(TA) expressed in E. coli localizes like the endogenous TAs. The yeast and bacterial TAs are inserted in the E. coli inner membrane, and they all show affiliation to phosphatidic acid (PA), found in the membrane of the bacterial cell poles and of the yeast mitochondria. Our results suggest a mechanism for TA membrane recognition conserved from bacteria to mitochondria and raise the possibility that through their interaction with PA, and TAs play a role across prokaryotes and eukaryotes in controlling cell/organelle fate.

中文翻译：

从细菌到线粒体的膜识别的进化保守机制

在其羧基末端（尾锚，TA）具有一个疏水段的蛋白质控制膜识别的机制尚不清楚。的大肠杆菌ELAB和YqjD，其份额顺序的和结构相似性与的TA的酿酒酵母FIS1的TA，显示出定位于线粒体。我们表明 YqjD 和 ElaB 被它们的 TA 引导到细菌细胞极。在大肠杆菌中表达的 Fis1(TA)与内源性 TA 一样定位。酵母和细菌 TA 被插入到大肠杆菌中内膜，它们都显示出与磷脂酸 (PA) 的关系，磷脂酸存在于细菌细胞极和酵母线粒体的膜中。我们的结果表明了一种从细菌到线粒体保守的 TA 膜识别机制，并提高了通过它们与 PA 相互作用的可能性，TA 和 TA 在原核生物和真核生物中在控制细胞/细胞器命运方面发挥作用。

更新日期：2021-11-22

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