ArticleeLife2021
Molecular insights into substrate recognition and discrimination by the N-terminal domain of Lon AAA+ protease.
Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Structural basis for the allosteric activation of Lon by the heat shock protein LarA.Nature communications · 2025Article
- Coordinated DNA polymerization by Polγ and the region of LonP1 regulated proteolysis.Nucleic acids research · 2024Article
- Polyphosphate and tyrosine phosphorylation in the N-terminal domain of the human mitochondrial Lon protease disrupts its functions.Scientific reports · 2024Article
- The heat shock protein LarA activates the Lon protease in response to proteotoxic stress.Nature communications · 2023Article
- Lon degrades stable substrates slowly but with enhanced processivity, redefining the attributes of a successful AAA+ protease.Cell reports · 2023Article
- LONRF2 is a gatekeeper against protein aggregation in aging neurons.Nature aging · 2023Article
- Insights into the Structure and Function of the Pex1/Pex6 AAA-ATPase in Peroxisome Homeostasis.Cells · 2022Review
- Structure and the Mode of Activity of Lon Proteases from Diverse Organisms.Journal of molecular biology · 2022Review
- Antimicrobial resistance patterns and genetic elements associated with the antibiotic resistance of Helicobacter pylori strains from Shanghai.Gut pathogens · 2022Article
- In vivo, in vitro and in silico: an open space for the development of microbe-based applications of synthetic biology.Microbial biotechnology · 2022Article
- Cryo-EM structure of the full-length Lon protease from Thermus thermophilus.FEBS letters · 2021Article
- Complete three-dimensional structures of the Lon protease translocating a protein substrate.Science advances · 2021Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Lon AAA+ protease (LonA) is a ubiquitous ATP-dependent proteolytic machine, which selectively degrades damaged proteins or native proteins carrying exposed motifs (degrons). Here we characterize the structural basis for substrate recognition and discrimination by the N-terminal domain (NTD) of LonA. The results reveal that the six NTDs are attached to the hexameric LonA chamber by flexible linkers such that the formers tumble independently of the latter. Further spectral analyses show that the NTD selectively interacts with unfolded proteins, protein aggregates, and degron-tagged proteins by two hydrophobic patches of its N-lobe, but not intrinsically disordered substrate, α-casein. Moreover, the NTD selectively binds to protein substrates when they are thermally induced to adopt unfolded conformations. Collectively, our findings demonstrate that NTDs enable LonA to perform protein quality control to selectively degrade proteins in damaged states and suggest that substrate discrimination and selective degradation by LonA are mediated by multiple NTD interactions.
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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.