ZapE/Afg1 interacts with Oxa1 and its depletion causes a multifaceted phenotype

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61988987%3A17310%2F20%3AA21027BC" target="_blank" >RIV/61988987:17310/20:A21027BC - isvavai.cz</a>

Alternative codes found

RIV/60077344:_____/20:00540053 RIV/60076658:12310/20:43901332

Result on the web

<a href="https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0234918" target="_blank" >https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0234918</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1371/journal.pone.0234918" target="_blank" >10.1371/journal.pone.0234918</a>

Result language

angličtina

Original language name

ZapE/Afg1 interacts with Oxa1 and its depletion causes a multifaceted phenotype

Original language description

ZapE/Afg1 is a component of the inner cell membrane of some eubacteria and the inner mitochondrial membrane of eukaryotes. This protein is involved in FtsZ-dependent division of eubacteria. In the yeast and human mitochondrion, ZapE/Afg1 likely interacts with Oxa1 and facilitates the degradation of mitochondrion-encoded subunits of respiratory complexes. Furthermore, the depletion of ZapE increases resistance to apoptosis, decreases oxidative stress tolerance, and impacts mitochondrial protein homeostasis. It remains unclear whether ZapE is a multifunctional protein, or whether some of the described effects are just secondary phenotypes. Here, we have analyzed the functions of ZapE inTrypanosoma brucei, a parasitic protist, and an important model organism. Using a newly developed proximity-dependent biotinylation approach (BioID2), we have identified the inner mitochondrial membrane insertase Oxa1 among three putative interacting partners of ZapE, which is present in two paralogs. RNAi-mediated depletion of both ZapE paralogs likely affected the function of respiratory complexes I and IV. Consistently, we show that the distribution of mitochondrial ZapE is restricted only to organisms with Oxa1, respiratory complexes, and a mitochondrial genome. We propose that the evolutionarily conserved interaction of ZapE with Oxa1, which is required for proper insertion of many inner mitochondrial membrane proteins, is behind the multifaceted phenotype caused by the ablation of ZapE

Czech name

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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

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OECD FORD branch

10601 - Cell biology

Project

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

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2020

Confidentiality

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

Name of the periodical

PLOS ONE

ISSN

1932-6203

e-ISSN

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Volume of the periodical

15

Issue of the periodical within the volume

6

Country of publishing house

US - UNITED STATES

Number of pages

21

Pages from-to

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UT code for WoS article

000545646600019

EID of the result in the Scopus database

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