气候变化领域集成服务门户(CCPortal): Determinism and contingencies shaped the evolution of mitochondrial protein import

CCPortal

DOI	10.1073/pnas.2017774118
	Determinism and contingencies shaped the evolution of mitochondrial protein import
	Rout S.; Oeljeklaus S.; Makki A.; Tachezy J.; Warscheid B.; Schneider A.
发表日期	2021
ISSN	00278424
卷号	118 期号:6
英文摘要	Mitochondrial protein import requires outer membrane receptors that evolved independently in different lineages. Here we used quantitative proteomics and in vitro binding assays to investigate the substrate preferences of ATOM46 and ATOM69, the two mitochondrial import receptors of Trypanosoma brucei. The results show that ATOM46 prefers presequence-containing, hydrophilic proteins that lack transmembrane domains (TMDs), whereas ATOM69 prefers presequence-lacking, hydrophobic substrates that have TMDs. Thus, the ATOM46/yeast Tom20 and the ATOM69/yeast Tom70 pairs have similar substrate preferences. However, ATOM46 mainly uses electrostatic, and Tom20 hydrophobic, interactions for substrate binding. In vivo replacement of T. brucei ATOM46 by yeast Tom20 did not restore import. However, replacement of ATOM69 by the recently discovered Tom36 receptor of Trichomonas hydrogenosomes, while not allowing for growth, restored import of a large subset of trypanosomal proteins that lack TMDs. Thus, even though ATOM69 and Tom36 share the same domain structure and topology, they have different substrate preferences. The study establishes complementation experiments, combined with quantitative proteomics, as a highly versatile and sensitive method to compare in vivo preferences of protein import receptors. Moreover, it illustrates the role determinism and contingencies played in the evolution of mitochondrial protein import receptors. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Mitochondria; Protein import; Receptors; Trichomonas; Trypanosoma
语种	英语
scopus关键词	mitochondrial protein; Article; binding assay; controlled study; enzyme specificity; enzyme substrate complex; hydrophilicity; hydrophobicity; in vitro study; molecular evolution; nonhuman; physical chemistry; priority journal; protein domain; protein expression; protein transport; proteomics; RNA interference; transmembrane domain; Trypanosoma brucei
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/180719
作者单位	Department of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern, Bern, CH-3012, Switzerland; Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology, University of Freiburg, Freiburg, 79104, Germany; Signalling Research Centres BIOSS and CIBSS, University of Freiburg, Freiburg, 79104, Germany; Department of Parasitology, Faculty of Science, Charles University, BIOCEV, Prague, 12843, Czech Republic
推荐引用方式 GB/T 7714	Rout S.,Oeljeklaus S.,Makki A.,et al. Determinism and contingencies shaped the evolution of mitochondrial protein import[J],2021,118(6).
APA	Rout S.,Oeljeklaus S.,Makki A.,Tachezy J.,Warscheid B.,&Schneider A..(2021).Determinism and contingencies shaped the evolution of mitochondrial protein import.Proceedings of the National Academy of Sciences of the United States of America,118(6).
MLA	Rout S.,et al."Determinism and contingencies shaped the evolution of mitochondrial protein import".Proceedings of the National Academy of Sciences of the United States of America 118.6(2021).