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Cited by 235Mitochondrial Function and PathologyFungal and yeast genetics researchAutophagy in Disease and Therapy

The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.

Erv1 Mediates the Mia40-dependent Protein Import Pathway and Provides a Functional Link to the Respiratory Chain by Shuttling Electrons to Cytochrome c

Allen, Scott, Balabanidou, Vassilia, Sideris, Dionisia P., Lisowsky, Thomas, Tokatlidis, Kostas·2005·Journal of Molecular Biology
DOI 10.1016/j.jmb.2005.08.049
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Abstract

Unlike matrix-targeted or inner membrane proteins, those that are targeted to the mitochondrial intermembrane space (IMS) do not require ATP or the inner membrane electrochemical potential. Their import is mediated primarily by the essential IMS protein Mia40/Tim40. Here, we show that the mitochondrial flavin adenine dinucleotide (FAD)-linked sulfhydryl oxidase Erv1 (essential for respiration and vegetative growth 1) plays a central role in the biogenesis of small, cysteine proteins of the IMS that are import substrates for Mia40. In a temperature-sensitive strain of Erv1, steady-state levels of small translocases of the inner membrane (Tims) are specifically affected when cells are grown at the non-permissive temperature. Furthermore, mitochondria isolated from the erv1-ts show a specific import and assembly defect for the small Tims but not in any other protein import pathway. Erv1 does not directly oxidise the small Tims, as thiol trapping assays show that the small Tims can still be oxidised in erv1-ts cells grown at the non-permissive temperature and in isolated mitochondria from this strain. Moreover, addition of pure Erv1 into erv1-ts mitochondria lacking the endogenous protein restores import and assembly of the small Tims only to an extent, arguing for a cascade of interactions with Erv1 rather than for a direct interaction of Erv1 with the small Tims. Cytochrome c (cyt c) is the in vivo oxidase for Erv1, as yeast cells mutated in cyt c cannot grow under anaerobic conditions. Therefore, Erv1 functionally links the Mia40-dependent import pathway to the Mia40-independent cyt c import pathway transferring electrons from the incoming precursors to cyt c as an acceptor. In this context, the protein import process is linked to the respiratory chain via the communication of Erv1 with cyt c.

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Metadata

Authors
Allen, S., Balabanidou, V., Sideris, D. P., Lisowsky, T., & Tokatlidis, K.
Affiliations
  • University of Manchester (GB)
  • University of Crete (GR)
Corresponding author
Tokatlidis, Kostas
ORCID
Venue
Journal of Molecular Biology
Publisher
Elsevier BV
Published
2005-11
Volume
353
Issue
5
Pages
937-944
ISSN
0022-2836 (ISSN-L)
DOI
10.1016/j.jmb.2005.08.049
OpenAlex
W2019250081
Cited by
235
References
40
Citations by year
2026: 4 · 2025: 6 · 2024: 7 · 2023: 2 · 2022: 4 · 2021: 13 · 2020: 7 · 2019: 7 · 2018: 2 · 2017: 15 · 2016: 11 · 2015: 11 · 2014: 12 · 2013: 9 · 2012: 18
FWCI
7.28
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • Journal of Molecular Biology (publishedVersion)
  • PubMed (publishedVersion)
  • ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
Funders
University of Crete
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords
Erv1, Mia40, Tim23, Tim17, electron transfer, mitochondrial protein biogenesis, temperature-sensitive mutants, yeast mitochondria, electron transport chain
MeSH terms
Mitochondrial Precursor Protein Import Complex Proteins, Electron Transport, Fungal Proteins, Membrane Proteins, Mitochondria, Temperature, Protein Transport, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins, Mitochondrial Membrane Transport Proteins, Cytochromes c, Oxidoreductases Acting on Sulfur Group Donors, Mitochondrial Membranes

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