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-Structure paper
タイトル | Snapshots of SOS response reveal structural requisites for LexA autoproteolysis. |
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ジャーナル・号・ページ | iScience, Vol. 28, Issue 2, Page 111726, Year 2025 |
掲載日 | 2025年2月21日 |
![]() | Filippo Vascon / Sofia De Felice / Matteo Gasparotto / Stefan T Huber / Claudio Catalano / Monica Chinellato / Riccardo Mezzetti / Alessandro Grinzato / Francesco Filippini / Lorenzo Maso / Arjen J Jakobi / Laura Cendron / ![]() ![]() ![]() ![]() ![]() |
PubMed 要旨 | Antimicrobial resistance poses a severe threat to human health and stands out among the pathogens responsible for this emergency. The SOS response to DNA damage is crucial in bacterial evolution, ...Antimicrobial resistance poses a severe threat to human health and stands out among the pathogens responsible for this emergency. The SOS response to DNA damage is crucial in bacterial evolution, influencing resistance development and adaptability in challenging environments, especially under antibiotic exposure. Recombinase A (RecA) and the transcriptional repressor LexA are the key players that orchestrate this process, determining either the silencing or the active transcription of the genes under their control. By integrating state-of-the-art structural approaches with binding and functional assays, we elucidated the molecular events activating the SOS response in , focusing on the RecA-LexA interaction. Our findings identify the conserved determinants and strength of the interactions that allow RecA to trigger LexA autocleavage and inactivation. These results provide the groundwork for designing novel antimicrobial strategies and exploring the potential translation of -derived approaches, to address the implications of infections. |
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手法 | EM (らせん対称) / EM (単粒子) |
解像度 | 3.43 - 4.2 Å |
構造データ | EMDB-19761, PDB-8s70: EMDB-19771, PDB-8s7g: |
化合物 | ![]() ChemComp-MG: ![]() ChemComp-AGS: |
由来 |
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![]() | DNA BINDING PROTEIN / recombinase / co-protease activator / TRANSCRIPTION / protease / antibiotic resistance / SOS response |