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Vestiges of the Bacterial Signal Recognition Particle-Based Protein Targeting in Mitochondria
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SYSNO ASEP 0554900 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Vestiges of the Bacterial Signal Recognition Particle-Based Protein Targeting in Mitochondria Author(s) Pyrih, Jan (BC-A) ORCID
Pánek, T. (CZ)
Durante, Ignacio Miguel (BC-A) RID, ORCID
Rašková, Vendula (BC-A) ORCID, RID
Cimrhanzlová, Kristýna (BC-A) SAI
Kriegová, Eva (BC-A) SAI
Tsaousis, A. (GB)
Eliáš, M. (CZ)
Lukeš, Julius (BC-A) RID, ORCIDNumber of authors 9 Source Title Molecular Biology and Evolution. - : Oxford University Press - ISSN 0737-4038
Roč. 38, č. 8 (2021), s. 3170-3187Number of pages 18 s. Publication form Print - P Language eng - English Country US - United States Keywords trypanosoma-brucei ; naegleria-gruberi ; in-situ ; rna ; genome ; prediction ; evolution ; generation ; eukaryotes ; platform ; evolution ; Ffh ; FtsY ; leca ; mitochondrion ; protein targeting ; protists ; signal recognition particle Subject RIV EE - Microbiology, Virology OECD category Microbiology R&D Projects GA18-15962S GA ČR - Czech Science Foundation (CSF) LL1601 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) EF16_019/0000759 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support BC-A - RVO:60077344 UT WOS 000693740300010 EID SCOPUS 85112480878 DOI 10.1093/molbev/msab090 Annotation The main bacterial pathway for inserting proteins into the plasma membrane relies on the signal recognition particle (SRP), composed of the Ffh protein and an associated RNA component, and the SRP-docking protein FtsY. Eukaryotes use an equivalent system of archaeal origin to deliver proteins into the endoplasmic reticulum, whereas a bacteria-derived SRP and FtsY function in the plastid. Here we report on the presence of homologs of the bacterial Ffh and FtsY proteins in various unrelated plastid-lacking unicellular eukaryotes, namely Heterolobosea, Alveida, Goniomonas, and Hemimastigophora. The monophyly of novel eukaryotic Ffh and FtsY groups, predicted mitochondrial localization experimentally confirmed for Naegleria gruberi, and a strong alphaproteobacterial affinity of the Ffh group, collectively suggest that they constitute parts of an ancestral mitochondrial signal peptide-based protein-targeting system inherited from the last eukaryotic common ancestor, but lost from the majority of extant eukaryotes. The ability of putative signal peptides, predicted in a subset of mitochondrial-encoded N. gruberi proteins, to target a reporter fluorescent protein into the endoplasmic reticulum of Trypanosoma brucei, likely through their interaction with the cytosolic SRP, provided further support for this notion. We also illustrate that known mitochondrial ribosome-interacting proteins implicated in membrane protein targeting in opisthokonts (Mbal, Mdm38, and Mrx15) are broadly conserved in eukaryotes and nonredundant with the mitochondrial SRP system. Finally, we identified a novel mitochondrial protein (MAP67) present in diverse eukaryotes and related to the signal peptide-binding domain of Ffh, which may well be a hitherto unrecognized component of the mitochondrial membrane protein-targeting machinery. Workplace Biology Centre (since 2006) Contact Dana Hypšová, eje@eje.cz, Tel.: 387 775 214 Year of Publishing 2022 Electronic address https://academic.oup.com/mbe/article/38/8/3170/6219958?login=false
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