lon Antibody

1. 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. PMID: 28292931
2. 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. PMID: 26403574
3. (p)ppGpp and Lon protease contribute to the robustness of the cell division. PMID: 26644431
4. Ec-Lon-protease was found to form complexes with the previously obtained thrombin aptamers whose molecules comprise the duplex domains and G-quadruplex region. PMID: 27125023
5. Role of mutation of alpha-helical domains in the functioning of ATP-dependent Lon protease of Escherichia coli. PMID: 26762095
6. 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. PMID: 25895363
7. Here we show that the cysteine residues act as a redox switch of Lon PMID: 25383757
8. Immature TorA (apoTorA) is degraded in vivo and in vitro by the Lon protease. Lon interacts with apoTorA but not with holoTorA. PMID: 24211448
9. Lon(E240K) exists almost exclusively as a dodecamer, whereas wild-type Lon equilibrates between hexamers and dodecamers. PMID: 24123818
10. 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. PMID: 23822859
11. Here, we demonstrate that Lon catalyzes robust unfolding and degradation of circularly permuted variants of GFP PMID: 23359718
12. Protein unfolding and degradation by the AAA+ Lon protease. PMID: 22162032
13. CspD is subject to growth-regulated degradation by the Lon protease. PMID: 21435040
14. 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. PMID: 21436141
15. The authors report that IbpA and IbpB, the sHSPs of Escherichia coli, are substrates for the AAA+ Lon protease. PMID: 20158612
16. Detailed comparison with the structures of 11 similar domains established the putative location of the nucleotide-binding site in this first fragment of Lon for which a crystal structure has become available. PMID: 15037242
17. Three dimensional structure of the N-terminal domain of E. coli Lon protease. PMID: 16199667
18. formation of a complex then enables Lon to degrade free ribosomal proteins PMID: 16495646
19. results indicate that Lon has a hexameric ring-shaped structure with a central cavity, and that the establishment of this configuration requires Mg(2+), but not ATP PMID: 16511355
20. We found that the addition of soxbox DNA or RNA polymerase to an in vitro degradation system decreases the rate of SoxS proteolysis by Lon protease. PMID: 16556231
21. Because of the differing affinities for ATP, we were able to monitor the activities of the high- and low-affinity ATPase sites of lon separately and determine that they were noninteracting. PMID: 16584195
22. A revised kinetic model is presented for ATPase activity in Lon protease in both the absence and presence of the model peptide substrate PMID: 16981703
23. We survey some recent developments in the mechanistic characterization of Lon with an emphasis on the utilization of pre-steady-state enzyme kinetic techniques to determine the timing of the ATPase and peptidase activities of the enzyme. PMID: 17216028
24. We conclude that Lon protease participates directly in the degradation of tmRNA-tagged proteins. PMID: 17616591
25. Detection and characterization of two ATP-dependent conformational changes in proteolytically inactive Escherichia coli lon mutants PMID: 17975895
26. 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. PMID: 18630346
27. 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. PMID: 19285157

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KEGG: ecj:JW0429

STRING: 316385.ECDH10B_0395