Vestiges of the Bacterial Signal Recognition Particle-Based Protein Targeting in Mitochondria

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F21%3A43903361" target="_blank" >RIV/60076658:12310/21:43903361 - isvavai.cz</a>

Alternative codes found

RIV/61988987:17310/21:A2202BSN RIV/60077344:_____/21:00554900 RIV/00216208:11310/21:10432743

Result on the web

<a href="https://academic.oup.com/mbe/article/38/8/3170/6219958" target="_blank" >https://academic.oup.com/mbe/article/38/8/3170/6219958</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/molbev/msab090" target="_blank" >10.1093/molbev/msab090</a>

Result language

angličtina

Original language name

Vestiges of the Bacterial Signal Recognition Particle-Based Protein Targeting in Mitochondria

Original language description

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.

Czech name

—

Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2021

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Molecular Biology and Evolution

ISSN

0737-4038

e-ISSN

—

Volume of the periodical

38

Issue of the periodical within the volume

8

Country of publishing house

GB - UNITED KINGDOM

Number of pages

18

Pages from-to

3170-3187

UT code for WoS article

000693740300010

EID of the result in the Scopus database

2-s2.0-85112480878