ArticleNature structural & molecular biology2020
Structure of the Bcs1 AAA-ATPase suggests an airlock-like translocation mechanism for folded proteins.
Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 43 citations in OpenAlex.
- The complexities of respiratory chain biogenesis and maintenance in yeast mitochondria.Protein science : a publication of the Protein Society · 2026Review
- Molecular machineries and pathways of mitochondrial protein transport.Nature reviews. Molecular cell biology · 2025Review
- Pathological variants in nuclear genes causing mitochondrial complex III deficiency: An update.Journal of inherited metabolic disease · 2024Review
- Conformations of Bcs1L undergoing ATP hydrolysis suggest a concerted translocation mechanism for folded iron-sulfur protein substrate.Nature communications · 2024Article
- OMA1 protease eliminates arrested protein import intermediates upon mitochondrial depolarization.The Journal of cell biology · 2024Article
- Only One of Three Bcs1 Homologs inJournal of fungi (Basel, Switzerland) · 2023Article
- A concerted ATPase cycle of the protein transporter AAA-ATPase Bcs1.Nature communications · 2023Article
- The unfolded protein response of the endoplasmic reticulum supports mitochondrial biogenesis by buffering nonimported proteins.Molecular biology of the cell · 2023Article
- Article
- Bcs1, a novel target for fungicide.Frontiers in chemistry · 2023Review
- Yeast as a tool for membrane protein production and structure determination.FEMS yeast research · 2022Article
- Crystal structure and biochemical analysis suggest that YjoB ATPase is a putative substrate-specific molecular chaperone.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Visualizing maturation factor extraction from the nascent ribosome by the AAA-ATPase Drg1.Nature structural & molecular biology · 2022Article
- Cryo-EM structure of transmembrane AAA+ protease FtsH in the ADP state.Communications biology · 2022Article
- Cytosolic Quality Control of Mitochondrial Protein Precursors-The Early Stages of the Organelle Biogenesis.International journal of molecular sciences · 2021Review
- Modelling of BCS1L-related human mitochondrial disease in Drosophila melanogaster.Journal of molecular medicine (Berlin, Germany) · 2021Article
- Interplay between Mitochondrial Protein Import and Respiratory Complexes Assembly in Neuronal Health and Degeneration.Life (Basel, Switzerland) · 2021Review
- Structural snapshots of the cellular folded protein translocation machinery Bcs1.The FEBS journal · 2021Article
- The mitochondrial intermembrane space: the most constricted mitochondrial sub-compartment with the largest variety of protein import pathways.Open biology · 2021Review
- AAA+ ATPases: structural insertions under the magnifying glass.Current opinion in structural biology · 2021Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Some proteins require completion of folding before translocation across a membrane into another cellular compartment. Yet the permeability barrier of the membrane should not be compromised and mechanisms have remained mostly elusive. Here, we present the structure of Saccharomyces cerevisiae Bcs1, an AAA-ATPase of the inner mitochondrial membrane. Bcs1 facilitates the translocation of the Rieske protein, Rip1, which requires folding and incorporation of a 2Fe-2S cluster before translocation and subsequent integration into the bc1 complex. Surprisingly, Bcs1 assembles into exclusively heptameric homo-oligomers, with each protomer consisting of an amphipathic transmembrane helix, a middle domain and an ATPase domain. Together they form two aqueous vestibules, the first being accessible from the mitochondrial matrix and the second positioned in the inner membrane, with both separated by the seal-forming middle domain. On the basis of this unique architecture, we propose an airlock-like translocation mechanism for folded Rip1.
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