ArticleNature structural & molecular biology2020
Structures of AAA protein translocase Bcs1 suggest translocation mechanism of a folded protein.
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 30 papers.
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Who cites it
30 citing papers in PubMed, 54 citations in OpenAlex.
- The complexities of respiratory chain biogenesis and maintenance in yeast mitochondria.Protein science : a publication of the Protein Society · 2026Review
- Splice-switching of the oncogenic BCS1L isoform suppresses ovarian cancer progression by disrupting mitochondrial function.Cell death & disease · 2026Article
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- 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
- The mitochondrial protein Bcs1A regulates antifungal drug tolerance by affecting efflux pump expression in the filamentous pathogenic fungusMicrobiology spectrum · 2024Article
- Conformations of Bcs1L undergoing ATP hydrolysis suggest a concerted translocation mechanism for folded iron-sulfur protein substrate.Nature communications · 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
- 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
- The Finnish genetic heritage in 2022 - from diagnosis to translational research.Disease models & mechanisms · 2022Review
- ncRNAs-mediated high expression of TIMM8A correlates with poor prognosis and act as an oncogene in breast cancer.Cancer cell international · 2022Article
- AAA+ proteins: one motor, multiple ways to work.Biochemical Society transactions · 2022Review
- Ovarian carcinoma immunoreactive antigen-like protein 2 (OCIAD2) is a novel complex III-specific assembly factor in mitochondria.Molecular biology of the cell · 2022Article
- Cryo-EM structure of transmembrane AAA+ protease FtsH in the ADP state.Communications biology · 2022Article
- The assembly, regulation and function of the mitochondrial respiratory chain.Nature reviews. Molecular cell biology · 2022Review
- Expanding the phenotypic spectrum of BCS1L-related mitochondrial disease.Annals of clinical and translational neurology · 2021Article
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7 authors at 1 institution in 1 country.
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Abstract
The mitochondrial membrane-bound AAA protein Bcs1 translocate substrates across the mitochondrial inner membrane without previous unfolding. One substrate of Bcs1 is the iron-sulfur protein (ISP), a subunit of the respiratory Complex III. How Bcs1 translocates ISP across the membrane is unknown. Here we report structures of mouse Bcs1 in two different conformations, representing three nucleotide states. The apo and ADP-bound structures reveal a homo-heptamer and show a large putative substrate-binding cavity accessible to the matrix space. ATP binding drives a contraction of the cavity by concerted motion of the ATPase domains, which could push substrate across the membrane. Our findings shed light on the potential mechanism of translocating folded proteins across a membrane, offer insights into the assembly process of Complex III and allow mapping of human disease-associated mutations onto the Bcs1 structure.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.