Evolutionary links between FliH/YscL‐like proteins from bacterial type III secretion systems and second‐stalk components of the FoF1 and vacuolar ATPases
- 1 April 2006
- journal article
- Published by Wiley in Protein Science
- Vol. 15 (4) , 935-941
- https://doi.org/10.1110/ps.051958806
Abstract
Bacterial type III secretion drives flagellar biosynthesis and mediates bacterial-eukaryotic interactions. Type III secretion is driven by an ATPase that is homologous to the catalytic subunits of proton-translocating ATPases, such as the F(o)F(1) ATPase. Here we use PSI-BLAST searches to show that some noncalatytic components are also conserved between type III secretion systems and proton-translocating ATPases. In particular, we show that the FliH/YscL-like proteins and the E subunits of vacuolar ATPases represent fusions of domains homologous to second-stalk components of the F(o)F(1) ATPase (the b and delta subunits).Keywords
This publication has 30 references indexed in Scilit:
- Molecular Basis of the Interaction between the Flagellar Export Proteins FliI and FliH from Helicobacter pyloriJournal of Biological Chemistry, 2006
- The ATPase FliI Can Interact with the Type III Flagellar Protein Export Apparatus in the Absence of Its Regulator, FliHJournal of Bacteriology, 2003
- Structural Properties of FliH, an ATPase Regulatory Component of the Salmonella Type III Flagellar Export ApparatusJournal of Molecular Biology, 2002
- Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathwayMolecular Microbiology, 2002
- The “Second Stalk” of Escherichia coli ATP Synthase: Structure of the Isolated Dimerization Domain,Biochemistry, 2002
- Regulation of late flagellar gene transcription and cell division by flagellum assembly in Caulobacter crescentusMolecular Microbiology, 2001
- HrpB2 and HrpF from Xanthomonas are type III‐secreted proteins and essential for pathogenicity and recognition by the host plantMolecular Microbiology, 2000
- FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activityMolecular Microbiology, 2000
- ThebSubunit ofEscherichia coliATP SynthaseJournal of Bioenergetics and Biomembranes, 2000
- Lengthening the Second Stalk of F1F0 ATP Synthase in Escherichia coliJournal of Biological Chemistry, 1999