ArticleJournal of bacteriology2002
A membrane-bound archaeal Lon protease displays ATP-independent proteolytic activity towards unfolded proteins and ATP-dependent activity for folded proteins.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 59 citations in OpenAlex.
- Lon-dependent proteolysis in oxidative stress responses.Journal of bacteriology · 2025Review
- The Role of Lonp1 on Mitochondrial Functions during Cardiovascular and Muscular Diseases.Antioxidants (Basel, Switzerland) · 2023Review
- Activator of one protease transforms into inhibitor of another in response to nutritional signals.Genes & development · 2019Article
- Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.Emerging topics in life sciences · 2018Article
- Characterization of the ATP-Dependent Lon-Like Protease in Methanobrevibacter smithii.Archaea (Vancouver, B.C.) · 2016Article
- Structural basis for the ATP-independent proteolytic activity of LonB proteases and reclassification of their AAA+ modules.Journal of microbiology (Seoul, Korea) · 2015Article
- Proteomic Insights into Sulfur Metabolism in the Hydrogen-Producing Hyperthermophilic Archaeon Thermococcus onnurineus NA1.International journal of molecular sciences · 2015Article
- Archaeal membrane-associated proteases: insights on Haloferax volcanii and other haloarchaea.Frontiers in microbiology · 2015Review
- Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs).Chemical reviews · 2014Review
- OMICS in ecology: systems level analyses of Halobacterium salinarum reveal large-scale temperature-mediated changes and a requirement of CctA for thermotolerance.Omics : a journal of integrative biology · 2014Article
- Structural and biochemical analysis of a thermostable membrane-bound stomatin-specific protease.Journal of synchrotron radiation · 2013Article
- Crystallization and preliminary X-ray diffraction analysis of the α subdomain of Lon protease from Brevibacillus thermoruber.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Archaeal proteasomes and sampylation.Sub-cellular biochemistry · 2013Review
- A Lon-like protease with no ATP-powered unfolding activity.PloS one · 2012Article
- Chaperone role for proteins p618 and p892 in the extracellular tail development of Acidianus two-tailed virus.Journal of virology · 2011Article
- Histone and TK0471/TrmBL2 form a novel heterogeneous genome architecture in the hyperthermophilic archaeon Thermococcus kodakarensis.Molecular biology of the cell · 2011Article
- Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber.The EMBO journal · 2010Article
- Crystallization and preliminary X-ray crystallographic analysis of Lon from Thermococcus onnurineus NA1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Thermodynamic characterization of specific interactions between the human Lon protease and G-quartet DNA.Nucleic acids research · 2008Article
- Cross genome comparisons of serine proteases in Arabidopsis and rice.BMC genomics · 2006Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In contrast to the eucaryal 26S proteasome and the bacterial ATP-dependent proteases, little is known about the energy-dependent proteolysis in members of the third domain, Archae. We cloned a gene homologous to ATP-dependent Lon protease from a hyperthermophilic archaeon and observed the unique properties of the archaeal Lon. Lon from Thermococcus kodakaraensis KOD1 (Lon(Tk)) is a 70-kDa protein with an N-terminal ATPase domain belonging to the AAA(+) superfamily and a C-terminal protease domain including a putative catalytic triad. Interestingly, a secondary structure prediction suggested the presence of two transmembrane helices within the ATPase domain and Western blot analysis using specific antiserum against the recombinant protein clearly indicated that Lon(Tk) was actually a membrane-bound protein. The recombinant Lon(Tk) possessed thermostable ATPase activity and peptide cleavage activity toward fluorogenic peptides with optimum temperatures of 95 and 70 degrees C, respectively. Unlike the enzyme from Escherichia coli, we found that Lon(Tk) showed higher peptide cleavage activity in the absence of ATP than it did in the presence of ATP. When three kinds of proteins with different thermostabilities were examined as substrates, it was found that Lon(Tk) required ATP for degradation of folded proteins, probably due to a chaperone-like function of the ATPase domain, along with ATP hydrolysis. In contrast, Lon(Tk) degraded unfolded proteins in an ATP-independent manner, suggesting a mode of action in Lon(Tk) different from that of its bacterial counterpart.
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