Structural and Functional Analysis of the C-terminal Cytoplasmic Domain of FlhA, an Integral Membrane Component of the Type III Flagellar Protein Export Apparatus in Salmonella

Distinct Roles of Highly Conserved Charged Residues at the MotA-FliG Interface in Bacterial Flagellar Motor Rotation

“…P22-mediated transduction was carried out as described by Yamaguchi et al (33). Procedures for DNA manipulations were carried out as described previously (38). QuikChange site-directed mutagenesis was performed as described in the manufacturer's instructions (Stratagene).…”

Evidence for symmetry in the elementary process of bidirectional torque generation by the bacterial flagellar motor

“…To carry out resurrection experiments, we used a plasmid, pYC20, which encodes MotA and MotB on pBAD24 (24). DNA manipulation was carried out as previously described (38). Luria broth and motility medium were also prepared as previously described (28).…”

Crystal structure of the C‐terminal domain of the Salmonella type III secretion system export apparatus protein InvA

“…It has been shown to interact with several soluble flagellar apparatus proteins including the ATPase FliI (InvC/YscN), its regulator FliH (OrgB/YscL), and FliJ (InvI/YscO); and is associated with a dominant-negative multicopy effect, inhibiting flagellar action by sequestering soluble components of the assembly apparatus in non-productive complexes. 1,[5][6][7][8] It is proposed that the C-terminal domain of FlhA provides one of the main sites of interaction at the base of the F-T3SS for the soluble assembly complex before subsequent substrate insertion into the inner membrane portal of the F-T3SS. 7 Structural data for the conserved core inner membrane components of the T3SS export apparatus is limited to the C-terminal cytoplasmic domain of SpaS/ YscU/FlhB from several NF-T3SS homologues [10][11][12][13] and the ATPase from both NF-T3SS 14 and F-T3SS 15 homologues.…”

“…1,[5][6][7][8] It is proposed that the C-terminal domain of FlhA provides one of the main sites of interaction at the base of the F-T3SS for the soluble assembly complex before subsequent substrate insertion into the inner membrane portal of the F-T3SS. 7 Structural data for the conserved core inner membrane components of the T3SS export apparatus is limited to the C-terminal cytoplasmic domain of SpaS/ YscU/FlhB from several NF-T3SS homologues [10][11][12][13] and the ATPase from both NF-T3SS 14 and F-T3SS 15 homologues. To gain insight into the function of InvA/YscV/ FlhA we have solved the first representative structure of this family, the C-terminal domain of NF-T3SS Salmonella enterica serovar Typhimurium InvA.…”