Induction of prophage lambda by γ-rays, mitomycin C and tif; Repressor cleavage studied by immunoprecipitation

Suppression of tif-mediated induction of SOS functions in Escherichia coli by an altered dnaB protein

“…The recA product purified from recA+ or tif-1 strains has been shown to cleave purified A repressor in vitro (26). The tifpromoted in vivo reaction takes place even if chloramphenicol is added before the temperature shift (30); tif-induced synthesis of the recA protein is known to be inhibited by chloramphenicol (18), suggesting that the tif protein acquires protease activity at high temperature through modification of the preexisting recA (tif) product. It is commonly hypothesized that the wild-type recA protein similarly undergoes a conformational change (activation) after inducing treatments (6,11,19).…”

T4-likeEscherichia coliphages from the environment carryblaCTX-M

“…The transductants thus obtained were further subject to prophage induction using mitomycin C at 1 μ g ml −1 and phage re‐isolation was experimented to determine if the event was due to specialized transduction (Shinagawa et al . ; Banks et al . ; Chen et al .…”

“…The resistors were tested for the CTX-M gene to confirm the transduction. The transductants thus obtained were further subject to prophage induction using mitomycin C at 1 lg ml À1 and phage re-isolation was experimented to determine if the event was due to specialized transduction (Shinagawa et al 1977;Banks et al 2003;Chen et al 2006). Plasmid was extracted from the transductants and PCR for the bla CTX-M gene was performed.…”

RecA protein-dependent cleavage of UmuD protein and SOS mutagenesis.

“…Portions of the sample were taken at different times after the addition and immediately chilled in an ice bath. Cell lysates were prepared, and the protein(s) that reacts with the antiserum was precipitated as described before (27) except that protein A-Sepharose (Sigma) was used instead of the second antibody and the antigen-antibody complexes adsorbed to the protein A-Sepharose were washed several times with RIPA buffer (10%o Triton X-100/1% sodium deoxycholate/0.1% NaDodSO4/0.15 M NaCl/0.05 M Tris'HCI, pH 7.2) and then with Hepes buffer (10% glycerol/20 mM Hepes, pH 7.5). The labeled proteins were separated by NadDodSO4/PAGE and visualized by autoradiography.…”