阴道毛滴虫氢酶体中磷酸果糖激酶n端不依赖于序列的输入。

Eukaryotic Cell Pub Date : 2015-12-01 Epub Date: 2015-10-16 DOI:10.1128/EC.00104-15
Petr Rada, Abhijith Radhakrishna Makki, Verena Zimorski, Sriram Garg, Vladimír Hampl, Ivan Hrdý, Sven B Gould, Jan Tachezy
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引用次数: 20

摘要

线粒体进化涉及蛋白质输入机制的起源,该机制允许核编码蛋白质靶向细胞器,以及可切割n端靶向序列(NTS)的起源,该序列允许基质蛋白质的有效分类和输入。在氢酶体和有丝体中,线粒体的减少形式与蛋白质组的减少,已知不依赖于nts的基质蛋白靶向。本文研究了厌氧病原菌阴道毛滴虫中两种糖酵解酶的细胞定位:ppi依赖性磷酸果糖激酶(TvPPi-PFK)和atp依赖性PFK (TvATP-PFK),前者是其糖酵解PFK活性的主要来源,而前者的功能尚不清楚。正如预期的那样,TvPPi-PFK主要在细胞质中检测到,而所有四个TvATP-PFK同源物都被输入到阴道T.氢酶体中,尽管它们都不具有NTS。TvATP-PFK在酿酒酵母中的异源表达表明,该蛋白具有被识别并导入酵母线粒体的内在能力,而酵母ATP-PFK则存在于细胞质中。TvATP-PFK仅由一个催化结构域组成,类似于“短”细菌酶,而scap - pfk包括一个n端延伸、一个催化结构域和一个c端调控结构域。sccat - pfk和短型大肠杆菌ATP-PFK催化结构域在阴道t细胞中的表达导致它们部分递送到氢酶体。这些结果表明,TvATP-PFK和同源的atp - pfk具有被氢酶体输入机制识别的内部结构靶向信息。从进化的角度来看,古代ATP-PFK被识别并导入氢酶体的倾向可能是细胞器进化早期阶段的遗留物。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

N-Terminal Presequence-Independent Import of Phosphofructokinase into Hydrogenosomes of Trichomonas vaginalis.

N-Terminal Presequence-Independent Import of Phosphofructokinase into Hydrogenosomes of Trichomonas vaginalis.

N-Terminal Presequence-Independent Import of Phosphofructokinase into Hydrogenosomes of Trichomonas vaginalis.

N-Terminal Presequence-Independent Import of Phosphofructokinase into Hydrogenosomes of Trichomonas vaginalis.

Mitochondrial evolution entailed the origin of protein import machinery that allows nuclear-encoded proteins to be targeted to the organelle, as well as the origin of cleavable N-terminal targeting sequences (NTS) that allow efficient sorting and import of matrix proteins. In hydrogenosomes and mitosomes, reduced forms of mitochondria with reduced proteomes, NTS-independent targeting of matrix proteins is known. Here, we studied the cellular localization of two glycolytic enzymes in the anaerobic pathogen Trichomonas vaginalis: PPi-dependent phosphofructokinase (TvPPi-PFK), which is the main glycolytic PFK activity of the protist, and ATP-dependent PFK (TvATP-PFK), the function of which is less clear. TvPPi-PFK was detected predominantly in the cytosol, as expected, while all four TvATP-PFK paralogues were imported into T. vaginalis hydrogenosomes, although none of them possesses an NTS. The heterologous expression of TvATP-PFK in Saccharomyces cerevisiae revealed an intrinsic capability of the protein to be recognized and imported into yeast mitochondria, whereas yeast ATP-PFK resides in the cytosol. TvATP-PFK consists of only a catalytic domain, similarly to "short" bacterial enzymes, while ScATP-PFK includes an N-terminal extension, a catalytic domain, and a C-terminal regulatory domain. Expression of the catalytic domain of ScATP-PFK and short Escherichia coli ATP-PFK in T. vaginalis resulted in their partial delivery to hydrogenosomes. These results indicate that TvATP-PFK and the homologous ATP-PFKs possess internal structural targeting information that is recognized by the hydrogenosomal import machinery. From an evolutionary perspective, the predisposition of ancient ATP-PFK to be recognized and imported into hydrogenosomes might be a relict from the early phases of organelle evolution.

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来源期刊
Eukaryotic Cell
Eukaryotic Cell 生物-微生物学
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期刊介绍: Eukaryotic Cell (EC) focuses on eukaryotic microbiology and presents reports of basic research on simple eukaryotic microorganisms, such as yeasts, fungi, algae, protozoa, and social amoebae. The journal also covers viruses of these organisms and their organelles and their interactions with other living systems, where the focus is on the eukaryotic cell. Topics include: - Basic biology - Molecular and cellular biology - Mechanisms, and control, of developmental pathways - Structure and form inherent in basic biological processes - Cellular architecture - Metabolic physiology - Comparative genomics, biochemistry, and evolution - Population dynamics - Ecology
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