ArticleMolecular and cellular biology2007
Substrate recognition by AAA+ ATPases: distinct substrate binding modes in ATP-dependent protease Yme1 of the mitochondrial intermembrane space.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 72 citations in OpenAlex.
- The complexities of respiratory chain biogenesis and maintenance in yeast mitochondria.Protein science : a publication of the Protein Society · 2026Review
- Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026Review
- Membrane-embedded polar residues target membrane proteins for degradation by the quality control protease FtsH.Nature communications · 2026Article
- Recognition of small Tim chaperones by the mitochondrial Yme1 protease.Protein science : a publication of the Protein Society · 2026Article
- YME1L1 Dysfunction Associated With 3-Methylglutaconic Aciduria.Journal of inherited metabolic disease · 2025Article
- Recent Advances in Understanding the Structural and Functional Evolution of FtsH Proteases.Frontiers in plant science · 2022Review
- Current Understanding of Temperature Stress-Responsive Chloroplast FtsH Metalloproteases.International journal of molecular sciences · 2021Review
- Protein import in mitochondria biogenesis: guided by targeting signals and sustained by dedicated chaperones.RSC advances · 2021Review
- AAA+ ATPases in Protein Degradation: Structures, Functions and Mechanisms.Biomolecules · 2020Review
- Proteolytic Control of Lipid Metabolism.ACS chemical biology · 2019Review
- Unique Structural Features of the Mitochondrial AAA+ Protease AFG3L2 Reveal the Molecular Basis for Activity in Health and Disease.Molecular cell · 2019Article
- Insertion Defects of Mitochondrially Encoded Proteins Burden the Mitochondrial Quality Control System.Cells · 2018Article
- m-AAA proteases, mitochondrial calcium homeostasis and neurodegeneration.Cell research · 2018Review
- Mitochondrial inner-membrane protease Yme1 degrades outer-membrane proteins Tom22 and Om45.The Journal of cell biology · 2018Article
- Molecular insights into theThe Journal of biological chemistry · 2017Article
- Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing.Science (New York, N.Y.) · 2017Article
- Metalloproteases of the Inner Mitochondrial Membrane.Biochemistry · 2017Review
- Msp1 Is a Membrane Protein Dislocase for Tail-Anchored Proteins.Molecular cell · 2017Article
- Multifunctional Mitochondrial AAA Proteases.Frontiers in molecular biosciences · 2017Review
- Mitochondrial Quality Control Proteases in Neuronal Welfare.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2016Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The energy-dependent proteolysis of cellular proteins is mediated by conserved proteolytic AAA(+) complexes. Two such machines, the m- and i-AAA proteases, are present in the mitochondrial inner membrane. They exert chaperone-like properties and specifically degrade nonnative membrane proteins. However, molecular mechanisms of substrate engagement by AAA proteases remained elusive. Here, we define initial steps of substrate recognition and identify two distinct substrate binding sites in the i-AAA protease subunit Yme1. Misfolded polypeptides are recognized by conserved helices in proteolytic and AAA domains. Structural modeling reveals a lattice-like arrangement of these helices at the surface of hexameric AAA protease ring complexes. While helices within the AAA domain apparently play a general role for substrate binding, the requirement for binding to surface-exposed helices within the proteolytic domain is determined by the folding and membrane association of substrates. Moreover, an assembly factor of cytochrome c oxidase, Cox20, serves as a substrate-specific cofactor during proteolysis and modulates the initial interaction of nonassembled Cox2 with the protease. Our findings therefore reveal the existence of alternative substrate recognition pathways within AAA proteases and shed new light on molecular mechanisms ensuring the specificity of proteolysis by energy-dependent proteases.
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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.