Mutational Analysis of Residues in PriA and PriC Affecting Their Ability To Interact with SSB in Escherichia coli K-12.

PriA and PriC recognize abandoned replication forks and direct reloading of the DnaB replicative helicase onto the lagging-strand template coated with single-stranded DNA-binding protein (SSB). Both PriA and PriC have been shown by biochemical and structural studies to physically interact with the C terminus of SSB. , these interactions trigger remodeling of the SSB on ssDNA.

An Epistasis Analysis of and in K-12.

RecA is essential for double-strand-break repair (DSBR) and the SOS response in K-12. RecN is an SOS protein and a member of the Structural Maintenance of Chromosomes family of proteins thought to play a role in sister chromatid cohesion/interactions during DSBR. Previous studies have shown that a plasmid-encoded (Q300R) mutant had a phenotype similar to ∆ (mitomycin C sensitive and UV resistant).

Protease-deficient SOS constitutive cells have RecN-dependent cell division phenotypes.

In Escherichia coli, after DNA damage, the SOS response increases the transcription (and protein levels) of approximately 50 genes. As DNA repair ensues, the level of transcription returns to homeostatic levels. ClpXP and other proteases return the high levels of several SOS proteins to homeostasis.