E N D
A B Amino acid sequence comparison and alignment of various bacterial FlgM proteins color-coded according to different physico-chemical properties. Sequence alignments were performed using ClustalW2 (Larkin et al., 2007); the alignment was color-coded and depicted using the software GeneDoc (Nicholas et al., 1997). A) alignment of FlgM of different Campylobacterales species which all possess short N-termini; B) alignment of FlgM of diverse eubacteria. Rust et al., Figure S1
Amino acid sequence alignment and comparison of H. pylori FliA and FlhA (C-terminal cytoplasmic domain only). Alignment was color-coded according to different physico-chemical properties. The sequence alignment was performed using ClustalW2 (Larkin et al., 2007); the alignment was color-coded and depicted using the software GeneDoc (Nicholas et al., 1997). Rust et al., Figure S2
FlgM T18 FlhAC T25 pCJ1001+pUT18 pCJ1001+pCJ1004 pKNT25+pUT18 pKNT25-ZIP+pUT18-ZIP BamHI BamHI B A BamHI BamHI EcoRI EcoRI flgM flgM long long flhAc flhAc T18 T18 pCJ1004 pCJ1004 pCJ1001 pCJ1001 4603 4603 bps bps 3239 3239 bps bps EcoRI EcoRI T25 T25 BACTH plasmid constructs coding for HPFlhAC-T25 (A) and HPFlgM-T18 (B) fusion proteins in plasmids pKNT25 and pUT18, respectively. C C) Screening of transformants containing BACTH plasmids in E. coli BTH101 on LB-IPTG-x-Gal plates. pCJ1001+pCJ1004 are transformants expressing both FlhAC-T25 and FlgM-T18 fusion proteins. pCJ1001+pUT18 and pKNT25+pUT18 represent two different negative controls (see also table 3). pKNT25-ZIP+pUT18-ZIP are the positive control transformants expressing two leucin zipper domain fusions (for the latter see Karimova et al., Proc.Natl.Acad.Sci. 1998, and BACTH manual). Rust et al., Figure S3