Additional file 1: of Activity of Vsr endonucleases encoded by Neisseria gonorrhoeae FA1090 is influenced by MutL and MutS proteins

Table S1. Primers used in the work. Table S2. Plasmids used in the work. Table S3. DNA substrates used in the work for the study the activity of gonococcal Vsr endonucleases. Table S4. The mutations occurred in the rpoB gene in the gonococcal mutants with disrupted vsr genes. Table S5. The activity of gonococcal Vsr endonucleases in the presence of the gonococcal MutL protein. The kst values for all DNA substrates recognized by Vsr endonucleases that were used for plotting the graphs in Fig. 4C. Table S6. The activity of gonococcal Vsr endonucleases in the presence of MutL protein of E. coli. The kst values for all DNA substrates recognized by Vsr endonucleases that were used to plot the graphs in Fig. 6. Table S7. The activity of gonococcal Vsr endonucleases in the presence of the gonococcal MutS protein. The kst values for all DNA substrates recognized by Vsr endonucleases that were used to plot the graphs in Fig. 7C. Figure S1. Spontaneous mutation frequency in N. gonorrhoeae mutants with disrupted ngoAXIIIV, ngoAXIVV, mutLNgo or mutS genes assayed by nalidixic acid resistance. Figure S2. The presence of the MutLNgo protein decreases amount of Vsr endonuclease required to complete DNA digestion. The results for DNA substrates that are not presented in Fig. 5. Figure S3. Comparison of the increase in mutation frequency in different bacterial species with disrupted mutL, mutS or vsr genes. Figure S4. Purification of the V.NgoAXIII endonuclease, V.NgoAXIV endonuclease, MutLNgoand MutS protein of N. gonorrhoeae FA1090 and the MutL protein of E. coli. Figure S5. Construction of DNA substrates containing two T:G mismatches and principle of an assay to demonstrate the activity of Vsr endonuclease. Figure S6. Construction of DNA substrates containing one T:G mismatch and principle of an assay to demonstrate the activity of Vsr endonuclease. (PDF 2718 kb