SEARCH

SEARCH BY CITATION

FilenameFormatSizeDescription
fml12476-sup-0001-FigS1-4-TableS1.pdfapplication/PDF588K

Fig. S1. The amino acid substitutions HrpS(I26N)/(R90H)/(R185H)/(H251Q) on the structural model of HrpS, based on the AAA+ domain of PspF.

Fig. S2. Transcription activity in vivo of HrpS variants, within HrpRS complexes, that escapes negative regulation by HrpV.

Fig. S3. Binding interactions between the HrpS variants I26, R90, R185 and H251 fused to T18 AC fragment and assayed in the presence of: (a) HrpV fused to T25 AC fragment, (b) HrpR fused to T25 AC fragment, (c) HrpS fused to T25 AC fragment.

Fig. S4. Western blotting of the Hrp proteins expressed in the BACTH system recognized by corresponding antibody.

Table S1. Bacterial strains and plasmids used in this study.

Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.