| Divergent Roles of Escherichia Coli Encoded Lon Protease in Imparting Resistance to Uncouplers of Oxidative Phosphorylation: Roles of marA, rob, soxS and acrB. | Divergent Roles of Escherichia Coli Encoded Lon Protease in Imparting Resistance to Uncouplers of Oxidative Phosphorylation: Roles of marA, rob, soxS and acrB.
Verma T, Nandini SS, Singh V, Raghavan A, Annappa H, Bhaskarla C, Dubey AK, Nandi D. | 02/29/2024 |
| A 5+1 assemble-to-activate mechanism of the Lon proteolytic machine. | A 5+1 assemble-to-activate mechanism of the Lon proteolytic machine.
Li S, Hsieh KY, Kuo CI, Lin TC, Lee SH, Chen YR, Wang CH, Ho MR, Ting SY, Zhang K, Chang CI., Free PMC Article | 11/29/2023 |
| Lon Protease Removes Excess Signal Recognition Particle Protein in Escherichia coli. | Lon Protease Removes Excess Signal Recognition Particle Protein in Escherichia coli.
Sauerbrei B, Arends J, Schünemann D, Narberhaus F., Free PMC Article | 02/13/2021 |
| Escherichia coli, the ATP-dependent Lon protease is crucial for protein quality control and regulatory processes; data suggests previously unrecognized fundamental functions of Lon in sulfur assimilation, nucleotide biosynthesis, amino acid and central energy metabolism. | An Integrated Proteomic Approach Uncovers Novel Substrates and Functions of the Lon Protease in Escherichia coli.
Arends J, Griego M, Thomanek N, Lindemann C, Kutscher B, Meyer HE, Narberhaus F. | 07/20/2019 |
| the ability of Lon to bind DNA is determined by its ATPase domain, that this binding is required for processing protein substrates in nucleoprotein complexes, and that Lon may help regulate DNA replication in response to growth conditions. | Defining the crucial domain and amino acid residues in bacterial Lon protease for DNA binding and processing of DNA-interacting substrates.
Karlowicz A, Wegrzyn K, Gross M, Kaczynska D, Ropelewska M, Siemiątkowska M, Bujnicki JM, Konieczny I., Free PMC Article | 06/10/2017 |
| These mutant rpoB RNA polymerases affect rcsA transcription, but per se are not defective either at rcsA or at cps promoters ande hence lead to increased capsular polysaccharide synthesis in Deltalon strains of Escherichia coli. | Suppression of capsule expression in Δlon strains of Escherichia coli by two novel rpoB mutations in concert with HNS: possible role for DNA bending at rcsA promoter.
Meenakshi S, Munavar MH., Free PMC Article | 07/30/2016 |
| (p)ppGpp and Lon protease contribute to the robustness of the cell division. | Inactivation of Cell Division Protein FtsZ by SulA Makes Lon Indispensable for the Viability of a ppGpp0 Strain of Escherichia coli.
Nazir A, Harinarayanan R., Free PMC Article | 06/11/2016 |
| Ec-Lon-protease was found to form complexes with the previously obtained thrombin aptamers whose molecules comprise the duplex domains and G-quadruplex region. | [Interaction of DNA Aptamers with the ATP-Dependent Lon Protease from Escherichia coli].
Spiridonova VA, Kudzhaev AM, Melnichuk AV, Gainutdinov AA, Andrianova AG, Rotanova TV. | 05/21/2016 |
| Role of mutation of alpha-helical domains in the functioning of ATP-dependent Lon protease of Escherichia coli. | [The Effect of Mutations in the Inserted Domain of ATP-Dependent Lon Protease from E. coli on the Enzyme Function].
Kudzhaev AM, Andrianova AG, Serova OV, Arkhipova VA, Dubovtseva ES, Rotanova TV. | 04/30/2016 |
| The participation of HI(CC) domain in formation of the spatial structures of LonA proteases and/or formation of their complexes with DNA is suggested. | [Role of the α-helical domains in the functioning of ATP-dependent Lon protease of Escherichia coli].
Andrianova AG, Kudzhaev AM, Serova OV, Dergousova NI, Rotanova TV. | 05/9/2015 |
| Here we show that the cysteine residues act as a redox switch of Lon | A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis.
Nishii W, Kukimoto-Niino M, Terada T, Shirouzu M, Muramatsu T, Kojima M, Kihara H, Yokoyama S. | 02/28/2015 |
| Immature TorA (apoTorA) is degraded in vivo and in vitro by the Lon protease. Lon interacts with apoTorA but not with holoTorA. | Quality control of a molybdoenzyme by the Lon protease.
Redelberger D, Genest O, Arabet D, Méjean V, Ilbert M, Iobbi-Nivol C. | 02/22/2014 |
| Lon(E240K) exists almost exclusively as a dodecamer, whereas wild-type Lon equilibrates between hexamers and dodecamers. | A mutation in the N domain of Escherichia coli lon stabilizes dodecamers and selectively alters degradation of model substrates.
Wohlever ML, Baker TA, Sauer RT., Free PMC Article | 01/25/2014 |
| Results augget that the cleavage of multiple peptide bonds awaits the "almost complete" delivery of all the scissile sites in Lon protease (lambdaN) to the proteolytic site in an ATP-dependent manner. | Processive degradation of unstructured protein by Escherichia coli Lon occurs via the slow, sequential delivery of multiple scissile sites followed by rapid and synchronized peptide bond cleavage events.
Mikita N, Cheng I, Fishovitz J, Huang J, Lee I. | 11/30/2013 |
| Here, we demonstrate that Lon catalyzes robust unfolding and degradation of circularly permuted variants of GFP | Engineering fluorescent protein substrates for the AAA+ Lon protease.
Wohlever ML, Nager AR, Baker TA, Sauer RT., Free PMC Article | 09/7/2013 |
| Protein unfolding and degradation by the AAA+ Lon protease. | Protein unfolding and degradation by the AAA+ Lon protease.
Gur E, Vishkautzan M, Sauer RT., Free PMC Article | 06/2/2012 |
| CspD is subject to growth-regulated degradation by the Lon protease. | The Escherichia coli replication inhibitor CspD is subject to growth-regulated degradation by the Lon protease.
Langklotz S, Narberhaus F. | 09/24/2011 |
| These results suggest that Lon interacts with cardiolipin in biological membranes, which may regulate the functions of Lon as a protein-degrading centre in accordance with environmental changes inside cells. | Regulatory role of cardiolipin in the activity of an ATP-dependent protease, Lon, from Escherichia coli.
Minami N, Yasuda T, Ishii Y, Fujimori K, Amano F. | 09/24/2011 |
| The authors report that IbpA and IbpB, the sHSPs of Escherichia coli, are substrates for the AAA+ Lon protease. | The IbpA and IbpB small heat-shock proteins are substrates of the AAA+ Lon protease.
Bissonnette SA, Rivera-Rivera I, Sauer RT, Baker TA., Free PMC Article | 10/23/2010 |
| Using synthetic peptides constituting different regions of the endogenous protein substrate lambdaN, the study demonstrates that the proteolytic site of Escherichia coli Lon exhibits a certain level of localized sequence specificity. | Utilization of synthetic peptides to evaluate the importance of substrate interaction at the proteolytic site of Escherichia coli Lon protease.
Patterson-Ward J, Tedesco J, Hudak J, Fishovitz J, Becker J, Frase H, McNamara K, Lee I., Free PMC Article | 01/21/2010 |
| Besides many members of the RcsA regulon (which validates our approach as RcsA is a known Lon substrate), many genes of the sigmaS-dependent general stress response were upregulated in the lon mutant. | A role for Lon protease in the control of the acid resistance genes of Escherichia coli.
Heuveling J, Possling A, Hengge R. | 01/21/2010 |
| Detection and characterization of two ATP-dependent conformational changes in proteolytically inactive Escherichia coli lon mutants | Detection and characterization of two ATP-dependent conformational changes in proteolytically inactive Escherichia coli Lon mutants by stopped flow kinetic techniques.
Patterson-Ward J, Huang J, Lee I., Free PMC Article | 01/21/2010 |
| N-terminus verified by Edman degradation on complete protein | See all PubMed (2) articles | 11/5/2007 |
| We conclude that Lon protease participates directly in the degradation of tmRNA-tagged proteins. | Lon protease degrades transfer-messenger RNA-tagged proteins.
Choy JS, Aung LL, Karzai AW., Free PMC Article | 01/21/2010 |
| the main ATP-dependent proteases Lon and ClpP participate in the physiological disintegration of cytoplasmic inclusion bodies, their absence minimizing the protein removal up to 40% | Lon and ClpP proteases participate in the physiological disintegration of bacterial inclusion bodies.
Vera A, Arís A, Carrió M, González-Montalbán N, Villaverde A. | 01/21/2010 |