| Non-canonical LexA proteins regulate the SOS response in the Bacteroidetes. | Non-canonical LexA proteins regulate the SOS response in the Bacteroidetes.
Sánchez-Osuna M, Cortés P, Lee M, Smith AT, Barbé J, Erill I., Free PMC Article | 12/25/2021 |
| Single-molecule imaging of LexA degradation in Escherichia coli elucidates regulatory mechanisms and heterogeneity of the SOS response. | Single-molecule imaging of LexA degradation in Escherichia coli elucidates regulatory mechanisms and heterogeneity of the SOS response.
Jones EC, Uphoff S., Free PMC Article | 09/18/2021 |
| The Parameter-Fitness Landscape of lexA Autoregulation in Escherichia coli. | The Parameter-Fitness Landscape of lexA Autoregulation in Escherichia coli.
Kozuch BC, Shaffer MG, Culyba MJ., Free PMC Article | 07/24/2021 |
| Two components of DNA replication-dependent LexA cleavage. | Two components of DNA replication-dependent LexA cleavage.
Myka KK, Marians KJ., Free PMC Article | 01/16/2021 |
| YbiB from Escherichia coli, the defining member of the novel Trpd2 family of prokaryotic DNA-binding proteins, forms an operon with the DNA helicase gene dinG and is under LexA control. | YbiB from Escherichia coli, the Defining Member of the Novel TrpD2 Family of Prokaryotic DNA-binding Proteins.
Schneider D, Kaiser W, Stutz C, Holinski A, Mayans O, Babinger P., Free PMC Article | 11/7/2015 |
| Like the self-cleaving serine proteases LexA and UmuD in Escherichia coli, UmuDAb required RecA for cleavage. | The Acinetobacter regulatory UmuDAb protein cleaves in response to DNA damage with chimeric LexA/UmuD characteristics.
Hare JM, Adhikari S, Lambert KV, Hare AE, Grice AN., Free PMC Article | 07/6/2013 |
| These results suggest that, IscR stabilizes LexA at the cka promoter after DNA damage thus, preventing its cleavage and inactivation, and this cooperation ensures that suicidal colicin K production is switched on only as a last resort. | Double locking of an Escherichia coli promoter by two repressors prevents premature colicin expression and cell lysis.
Butala M, Sonjak S, Kamenšek S, Hodošček M, Browning DF, Žgur-Bertok D, Busby SJ. | 02/2/2013 |
| These results reveal specific amino acid determinants of the RecA-LexA interaction and suggest that LexA binds RecA and RecAi+6 at a composite site on the RecA filament, which could explain the role of the active filament during LexA cleavage. | Separation of recombination and SOS response in Escherichia coli RecA suggests LexA interaction sites.
Adikesavan AK, Katsonis P, Marciano DC, Lua R, Herman C, Lichtarge O., Free PMC Article | 01/14/2012 |
| The conformational flexibility of unbound LexA is the key element in establishing a co-ordinated SOS response. | Interconversion between bound and free conformations of LexA orchestrates the bacterial SOS response.
Butala M, Klose D, Hodnik V, Rems A, Podlesek Z, Klare JP, Anderluh G, Busby SJ, Steinhoff HJ, Zgur-Bertok D., Free PMC Article | 11/5/2011 |
| LexA regulated genes exhibit phenotypic heterogeneity as high level expression is observed in only a small subpopulation. | Genes regulated by the Escherichia coli SOS repressor LexA exhibit heterogeneous expression.
Kamenšek S, Podlesek Z, Gillor O, Zgur-Bertok D., Free PMC Article | 02/26/2011 |
| Uropathogenic Escherichia coli strains defective in regulation of the SOS response mediated by RecA and LexA display attenuated virulence in immunocompetent mice within the first 6 h post infection. | SOS regulatory elements are essential for UPEC pathogenesis.
Li B, Smith P, Horvath DJ Jr, Romesberg FE, Justice SS. | 11/6/2010 |
| RecA stimulates the transition of LexA from its noncleavable to its cleavable conformation and therefore operates, at least in part, by an allosteric mechanism. | RecA-dependent cleavage of LexA dimers.
Giese KC, Michalowski CB, Little JW., Free PMC Article | 01/21/2010 |
| LexA binds to and represses the promoter of antC of coliphage N15. | The antirepressor needed for induction of linear plasmid-prophage N15 belongs to the SOS regulon.
Mardanov AV, Ravin NV., Free PMC Article | 01/21/2010 |
| oligomerization of LexA is proposed to be a possible regulation mechanism of the Escherichia coli SOS regulon in response to environmental conditions resulting in acidic intracellular pH. Structural changes on LexA repressor promoted by acidic pH. | Tetramerization of the LexA repressor in solution: implications for gene regulation of the E.coli SOS system at acidic pH.
Sousa FJ, Lima LM, Pacheco AB, Oliveira CL, Torriani I, Almeida DF, Foguel D, Silva JL, Mohana-Borges R. | 01/21/2010 |
| NMR analysis of LexA catalytic domain in its active conformation | Backbone chemical shift assignments of the LexA catalytic domain in its active conformation.
Okon M, Pfuetzner RA, Vuckovic M, Little JW, Strynadka NC, McIntosh LP. | 01/21/2010 |