ArticleProtein science : a publication of the Protein Society2019
N domain of the Lon AAA+ protease controls assembly and substrate choice.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Bacteria encode post-mortem protein catabolism that enables altruistic nutrient recycling.Nature communications · 2025Article
- Roles of LonP1 in Oral-Maxillofacial Developmental Defects and Tumors: A Novel Insight.International journal of molecular sciences · 2022Review
- Structure and the Mode of Activity of Lon Proteases from Diverse Organisms.Journal of molecular biology · 2022Review
- Cryo-EM structure of the full-length Lon protease from Thermus thermophilus.FEBS letters · 2021Article
- Cargo competition for a dimerization interface restricts and stabilizes a bacterial protease adaptor.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Crystal structure of XCC3289 from Xanthomonas campestris: homology with the N-terminal substrate-binding domain of Lon peptidase.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Cryo-EM structure of substrate-freeCurrent research in structural biology · 2019Article
- A Mechanistic Perspective on PEX1 and PEX6, Two AAA+ Proteins of the Peroxisomal Protein Import Machinery.International journal of molecular sciences · 2019Review
- Omnipresent Maxwell's demons orchestrate information management in living cells.Microbial biotechnology · 2019Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The protein quality control network (pQC) plays critical roles in maintaining protein and cellular homeostasis, especially during stress. Lon is a major pQC AAA+ protease, conserved from bacteria to human mitochondria. It is the principal enzyme that degrades most unfolded or damaged proteins. Degradation by Lon also controls cellular levels of several key regulatory proteins. Recently, our group determined that Escherichia coli Lon, previously thought to be an obligate homo-hexamer, also forms a dodecamer. This larger assembly has decreased ATPase activity and displays substrate-specific alterations in degradation compared with the hexamer. Here we experimentally probe the physical hexamer-hexamer interactions and the biological roles of the Lon dodecamer. Using structure prediction methods coupled with mutagenesis, we identified a key interface and specific residues within the Lon N domain that participates in an intermolecular coiled coil unique to the dodecamer. With this knowledge, we made a Lon variant (Lon
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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.