In Vivo Structure-Function Analysis and Redox Interactomes of Leishmania tarentolae Erv-Reference-Cited by-同舟云学术

In Vivo Structure-Function Analysis and Redox Interactomes of Leishmania tarentolae Erv

Published:2021-10-31 Issue:2 Volume:9 Page:
ISSN:2165-0497
Container-title:Microbiology Spectrum
language:en
Short-container-title:Microbiol Spectr

Author:

Turra Gino L.¹²,Liedgens Linda¹²,Sommer Frederik³,Schneider Luzia²,Zimmer David⁴,Vilurbina Perez Jordi²,Koncarevic Sasa⁵,Schroda Michael³^ORCID,Mühlhaus Timo⁴,Deponte Marcel¹²^ORCID

Affiliation:

1. Department of Parasitology, Ruprecht-Karls University, Heidelberg, Germany

2. Faculty of Chemistry, TU Kaiserslautern, Kaiserslautern, Germany

3. Molecular Biotechnology & Systems Biology, TU Kaiserslautern, Kaiserslautern, Germany

4. Computational Systems Biology, TU Kaiserslautern, Kaiserslautern, Germany

5. Proteome Sciences R&D GmbH & Co. KG, Frankfurt, Germany

Abstract

The discovery of the redox proteins Mia40/CHCHD4 and Erv1/ALR, as well as the elucidation of their relevance for oxidative protein folding in the mitochondrial intermembrane space of yeast and mammals, founded a new research topic in redox biology and mitochondrial protein import. The lack of Mia40/CHCHD4 in protist lineages raises fundamental and controversial questions regarding the conservation and evolution of this essential pathway.

Funder

Deutsche Forschungsgemeinschaft

Deutscher Akademischer Austauschdienst

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Cell Biology,Microbiology (medical),Genetics,General Immunology and Microbiology,Ecology,Physiology

Link

https://journals.asm.org/doi/pdf/10.1128/Spectrum.00809-21

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2. Mitochondrial protein import pathways are functionally conserved among eukaryotes despite compositional diversity of the import machineries