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TitleSnapshots of SOS response reveal structural requisites for LexA autoproteolysis.
Journal, issue, pagesiScience, Vol. 28, Issue 2, Page 111726, Year 2025
Publish dateFeb 21, 2025
AuthorsFilippo 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 AbstractAntimicrobial 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.
External linksiScience / PubMed:39898034 / PubMed Central
MethodsEM (helical sym.) / EM (single particle)
Resolution3.43 - 4.2 Å
Structure data

19761

8s70

EMDB-19761, PDB-8s70:
Cryo-EM structure of Pseudomonas aeruginosa recombinase A (RecA) in complex with ssDNA 72mer and ATPgS
Method: EM (helical sym.) / Resolution: 4.2 Å

19771

8s7g

EMDB-19771, PDB-8s7g:
Cryo-EM structure of Pseudomonas aeruginosa Recombinase A (RecA) in complex with LexAS125A mutant
Method: EM (single particle) / Resolution: 3.43 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

Source
  • Pseudomonas aeruginosa PAO1 (bacteria)
  • synthetic construct (others)
  • pseudomonas aeruginosa (bacteria)
KeywordsDNA BINDING PROTEIN / recombinase / co-protease activator / TRANSCRIPTION / protease / antibiotic resistance / SOS response

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