TY  - JOUR
  - Lane, MC,O'Toole, PW,Moore, SA
  - 2006
  - January
  - The Journal of Biological Chemistry
  - Molecular basis of the interaction between the flagellar export proteins FliI and FliH from Helicobacter pylori
  - Validated
  - ()
  - SECRETION SYSTEM GASTRIC-CANCER ATPASE COMPONENTS APPARATUS SEQUENCE INFECTION MOTILITY GENE OLIGOMERIZATION
  - 281
  - 508
  - 517
  - Bacterial flagellar protein export requires an ATPase, FliI, and presumptive inhibitor, FliH. We have explored the molecular basis for FliI/ FliH interaction in the human gastric pathogen Helicobacter pylori. By using bioinformatic and biochemical analyses, we showed that residues 1-18 of FliI very likely form an amphipathic alpha-helix upon interaction with FliH, and that residues 21-91 of FliI resemble the N-terminal oligomerization domain of the F-1-ATPase catalytic subunits. A truncated FliI-(2- 91) protein was shown to be folded, although the N-terminal 18 residues were likely unstructured. Deletion and scanning mutagenesis showed that residues 1-18 of FliI were essential for the FliI/ FliH interaction. Scanning mutation of amino acids in the N-terminal 10 residues of FliI indicated that a cluster of hydrophobic residues in this segment was critical for the interaction with FliH. The interaction between FliI and FliH has similarities to the interaction between the N-terminal alpha-helix of the F-1-ATPase alpha-subunit and the globular domain of the F-1-ATPase delta-subunit, respectively. This similarity suggests that FliH may function as a molecular stator.
  - DOI 10.1074/jbc.M507238200
DA  - 2006/01
ER  - 

@article{V43336696,
   = {Lane,  MC and O'Toole,  PW and Moore,  SA },
   = {2006},
   = {January},
   = {The Journal of Biological Chemistry},
   = {Molecular basis of the interaction between the flagellar export proteins FliI and FliH from Helicobacter pylori},
   = {Validated},
   = {()},
   = {SECRETION SYSTEM GASTRIC-CANCER ATPASE COMPONENTS APPARATUS SEQUENCE INFECTION MOTILITY GENE OLIGOMERIZATION},
   = {281},
  pages = {508--517},
   = {{Bacterial flagellar protein export requires an ATPase, FliI, and presumptive inhibitor, FliH. We have explored the molecular basis for FliI/ FliH interaction in the human gastric pathogen Helicobacter pylori. By using bioinformatic and biochemical analyses, we showed that residues 1-18 of FliI very likely form an amphipathic alpha-helix upon interaction with FliH, and that residues 21-91 of FliI resemble the N-terminal oligomerization domain of the F-1-ATPase catalytic subunits. A truncated FliI-(2- 91) protein was shown to be folded, although the N-terminal 18 residues were likely unstructured. Deletion and scanning mutagenesis showed that residues 1-18 of FliI were essential for the FliI/ FliH interaction. Scanning mutation of amino acids in the N-terminal 10 residues of FliI indicated that a cluster of hydrophobic residues in this segment was critical for the interaction with FliH. The interaction between FliI and FliH has similarities to the interaction between the N-terminal alpha-helix of the F-1-ATPase alpha-subunit and the globular domain of the F-1-ATPase delta-subunit, respectively. This similarity suggests that FliH may function as a molecular stator.}},
   = {DOI 10.1074/jbc.M507238200},
  source = {IRIS}
}