Gabija restricts phages that antagonize a conserved host DNA repair complex.

ABSTRACT: Anti-bacteriophage systems like restriction-modification and CRISPR-Cas have DNA substrate specificity mechanisms that enable identification of invaders. How Gabija, a highly prevalent nuclease-helicase anti-phage system, executes self- vs. non-self-discrimination remains unknown. Here, we propose that phage-encoded DNA end-binding proteins that antagonize host RecBCD sensitize phages to Gabija. When targeting a temperate Lambda-like phage in Pseudomonas aeruginosa, Gabija protects the cell by preventing phage genome circularization and subsequent replication. Phage and plasmid sensitivity to Gabija is licensed by DNA end-binding complexes such as a phage exonuclease together with a ssDNA-annealing protein or Gam_Mu dimers, which prevent loading of host repair complex RecB

SUBMITTER: Hong A 

PROVIDER: S-EPMC12407980 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature