ArticleActa biochimica Polonica2008
Limited proteolysis of E. coli ATP-dependent protease Lon - a unified view of the subunit architecture and characterization of isolated enzyme fragments.
Article in Acta biochimica Polonica, 2008. 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, 23 citations in OpenAlex.
- Investigation of a cryptic ligand binding site on Plasmodium falciparum Hsp90.Bioorganic & medicinal chemistry · 2025Article
- Unique Structural Fold of LonBA Protease fromInternational journal of molecular sciences · 2022Article
- Structure and the Mode of Activity of Lon Proteases from Diverse Organisms.Journal of molecular biology · 2022Review
- Article
- Cryo-EM structure of substrate-freeCurrent research in structural biology · 2019Article
- New insights into structural and functional relationships between LonA proteases and ClpB chaperones.FEBS open bio · 2019Article
- Defining the crucial domain and amino acid residues in bacterial Lon protease for DNA binding and processing of DNA-interacting substrates.The Journal of biological chemistry · 2017Article
- Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity.Molecular microbiology · 2014Article
- A mutation in the N domain of Escherichia coli lon stabilizes dodecamers and selectively alters degradation of model substrates.Journal of bacteriology · 2013Article
- Distinct quaternary structures of the AAA+ Lon protease control substrate degradation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Biological roles of the Podospora anserina mitochondrial Lon protease and the importance of its N-domain.PloS one · 2012Article
- Structure of the N-terminal fragment of Escherichia coli Lon protease.Acta crystallographica. Section D, Biological crystallography · 2010Article
- Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
We carried out chymotryptic digestion of multimeric ATP-dependent Lon protease from Escherichia coli. Four regions sensitive to proteolytic digestion were located in the enzyme and several fragments corresponding to the individual structural domains of the enzyme or their combinations were isolated. It was shown that (i) unlike the known AAA(+) proteins, the ATPase fragment (A) of Lon has no ATPase activity in spite of its ability to bind nucleotides, and it is monomeric in solution regardless of the presence of any effectors; (ii) the monomeric proteolytic domain (P) does not display proteolytic activity; (iii) in contrast to the inactive counterparts, the AP fragment is an oligomer and exhibits both the ATPase and proteolytic activities. However, unlike the full-length Lon, its AP fragment oligomerizes into a dimer or a tetramer only, exhibits the properties of a non-processive protease, and undergoes self-degradation upon ATP hydrolysis. These results reveal the crucial role played by the non-catalytic N fragment of Lon (including its coiled-coil region), as well as the contribution of individual domains to creation of the quaternary structure of the full-length enzyme, empowering its function as a processive protease.
Indexed as
Identifiers
18506223PMC7355814W2168603821What OpenQuestion holds
Registered trials
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