The Lon ATP-dependent protease plays a major role in protein quality control. An increasing number of regulatory proteins, however, are being identified as Lon substrates, thus indicating that in addition to its housekeeping function, Lon plays an important role in regulating many biological processes in bacteria. This review presents and discusses the involvement of Lon in different aspects of bacterial physiology, including cell differentiation, sporulation, pathogenicity and survival under starvation conditions.
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Expression of Multiple Copies of the Lon Protease Gene Resulted in Increased Antibiotic Production, Osmotic and UV Stress Resistance in Streptomyces coelicolor A3(2).
Curr Microbiol
December 2024
Faculty of Science, Molecular Biology and Genetics Department, Gebze Technical University, Gebze, 41400, Kocaeli, Türkiye.
The genus Streptomyces is a group of gram-positive bacteria that exhibit a distinctive growth pattern characterised by elongated, branched hyphae. Streptomyces coelicolor A3(2), which produces at least five different antibiotics, is a model organism that is widely used in genetic studies. There are very few studies in Streptomyces on the ATP-dependent Lon protease, which has very important functions in every organism and is particularly responsible for protein homeostasis.
View Article and Find Full Text PDFAllosteric modulation of the Lon protease via ssDNA binding and local charge changes.
J Biol Chem
November 2024
Department of Biochemistry and Molecular Biology, Molecular and Cellular Biology Program, University of Massachusetts, Amherst, USA. Electronic address:
The ATPase Associated with diverse cellular Activities (AAA+) family of proteases play crucial roles in cellular proteolysis and stress responses. Like other AAA + proteases, the Lon protease is known to be allosterically regulated by nucleotide and substrate binding. Although it was originally classified as a DNA binding protein, the impact of DNA binding on Lon activity is unclear.
View Article and Find Full Text PDFGlobal impacts of peroxisome and pexophagy dysfunction revealed through multi-omics analyses of lon2 and atg2 mutants.
Plant J
December 2024
Department of Biosciences, Rice University, Houston, Texas, 77005, USA.
Peroxisomes house diverse metabolic pathways that are essential for plant and animal survival, including enzymes that produce or inactivate toxic byproducts. Despite the importance of peroxisomes and their collaborations with other organelles, the mechanisms that trigger or prevent peroxisome turnover and the cellular impacts of impaired peroxisomes are incompletely understood. When Arabidopsis thaliana LON2, a peroxisomal protein with chaperone and protease capacity, is disrupted, metabolic dysfunction and protein instability in peroxisomes ensue.
View Article and Find Full Text PDFAssociation of LONP1 gene with epilepsy and the sub-regional effect.
Sci Rep
October 2024
Key Laboratory of Neurogenetics and Channelopathies of Guangdong Province, Department of Neurology of the Second Affiliated Hospital, Institute of Neuroscience, Guangzhou Medical University, Ministry of Education of China, Guangzhou, China.
The LONP1 gene encodes Lon protease, which is responsible for degrading damaged or misfolded proteins and binding mitochondrial DNA. Previously, LONP1 variants have been identified in patients with cerebral, ocular, dental, auricular, and skeletal anomalies (CODAS syndrome) and mitochondrial diseases. Seizures were occasionally observed.
View Article and Find Full Text PDFReaddressing the Localization of Apolipoprotein E (APOE) in Mitochondria-Associated Endoplasmic Reticulum (ER) Membranes (MAMs): An Investigation of the Hepatic Protein-Protein Interactions of APOE with the Mitochondrial Proteins Lon Protease (LONP1), Mitochondrial Import Receptor Subunit TOM40 (TOMM40) and Voltage-Dependent Anion-Selective Channel 1 (VDAC1).
Int J Mol Sci
October 2024
Institute of Human Nutrition and Food Science, University of Kiel, Hermann-Rodewald-Strasse 6, 24118 Kiel, Germany.
As a component of circulating lipoproteins, APOE binds to cell surface receptors mediating lipoprotein metabolism and cholesterol transport. A growing body of evidence, including the identification of a broad variety of cellular proteins interacting with APOE, suggests additional independent functions. Investigating cellular localization and protein-protein interactions in cultured human hepatocytes, we aimed to contribute to the elucidation of hitherto unnoted cellular functions of APOE.
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