ArticleScience (New York, N.Y.)2017
Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing.
Article in Science (New York, N.Y.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers.
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Who cites it
150 citing papers in PubMed.
- Regulation of cellular proteostasis via mitochondrial protein import.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Disruption of mitonuclear coadaptation and compensatory evolution after an extreme dietary shift in carnivorous butterflies.Molecular biology and evolution · 2026Article
- Cryo-EM Structure of the FtsH Periplasmic Domain Reveals Functional Dynamics.ACS chemical biology · 2026Article
- Structural plasticity of the membrane-bound protein degradation assembly supports bacterial adaptation to stress.Cell reports · 2026Article
- Deposition of CENP-ACse4 is enhanced by mutations in the AAA+ ATPase domain of ATAD2Yta7.Genetics · 2026Article
- Cryo-EM Structure of Human ATAD2B Reveals a Hexameric Organization Contributes to ATPase Activity and Substrate Coordination.bioRxiv : the preprint server for biology · 2026Article
- A novel AAA+ ATPase required for sporulation and stress response inJournal of bacteriology · 2026Article
- Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026Review
- Recognition of small Tim chaperones by the mitochondrial Yme1 protease.Protein science : a publication of the Protein Society · 2026Article
- Cryo-EM structures of human ClpXP reveal mechanisms of assembly and proteolytic activation.Nature communications · 2026Article
- A stochastic mechanism drives fast substrate translocation in the AAA+ machine ClpB.Nature communications · 2026Article
- Linked dimers of the AAA+ ATPase Msp1 reveal energetic demands and mechanistic plasticity for substrate extraction from lipid bilayers.FEBS letters · 2026Article
- PCNA is a nucleotide exchange factor for the clamp loader ATPase complex.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Substrate-dependent activation of LONP1 informs on proteolytic regulation and ATPase motor function.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structure of the central Staphylococcus aureus AAA+ protease MecA/ClpC/ClpP.Communications biology · 2025Article
- Elastic analysis bridges structure and dynamics of an AAA+ molecular motor.PLoS computational biology · 2025Article
- Recent Advances in the Structural Studies of the Proteolytic ClpP/ClpX Molecular Machine.Biomolecules · 2025Review
- Structural Plasticity of the Membrane-Bound Protein Degradation Assembly Supports Bacterial Adaptation to Stress.bioRxiv : the preprint server for biology · 2025Article
- PCNA is a Nucleotide Exchange Factor for the Clamp Loader ATPase Complex.bioRxiv : the preprint server for biology · 2025Article
- Transforming an ATP-dependent enzyme into a dissipative, self-assembling system.Nature chemical biology · 2025Article
90 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors.
Funding
Abstract
We present an atomic model of a substrate-bound inner mitochondrial membrane AAA+ quality control protease in yeast, YME1. Our ~3.4-angstrom cryo-electron microscopy structure reveals how the adenosine triphosphatases (ATPases) form a closed spiral staircase encircling an unfolded substrate, directing it toward the flat, symmetric protease ring. Three coexisting nucleotide states allosterically induce distinct positioning of tyrosines in the central channel, resulting in substrate engagement and translocation to the negatively charged proteolytic chamber. This tight coordination by a network of conserved residues defines a sequential, around-the-ring adenosine triphosphate hydrolysis cycle that results in stepwise substrate translocation. A hingelike linker accommodates the large-scale nucleotide-driven motions of the ATPase spiral relative to the planar proteolytic base. The translocation mechanism is likely conserved for other AAA+ ATPases.
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Registered trials
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.