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• W19774080 abstract "ChpA is a Pseudomonas aeruginosa signal transduction protein that wasnoriginally identified in a transposon library for non-twitching mutants and hasnsubsequently been identified in whole-genome virulence screens, but as yetnthe precise role of this protein in these processes remains to be determined.nAnalysis of the protein sequence revealed that ChpA possesses 9 potentialnsites of phosphorylation, including 6 histidine phosphotransfer domains (HPt),na novel serine and threonine phosphotransfer domain (SPt, TPt) and a C-terminal CheY-like domain. As such, ChpA is probably the most complexnsignal transduction protein yet described in nature.n n A genome database search revealed that several other bacteria,npredominantly p and g-Proteobacteria, also possess genes homologous tonchpA, and together these genes encode what appears to represent a distinctnsub-class of CheA-like histidine kinases, hereafter referred to as multi-HPtnCheA/CheY hybrid proteins. Phylogenetic analysis of the multi-HPtnCheA/CheY hybrid proteins showed that the HPt-like domains can be groupedninto distinct clusters that probably reflect the evolutionary development of thenprotein class. Interestingly, the most ancient (inferred from clustering nearestnto the cyanobacterial outgroup) and most conserved HPt-like domains ofnChpA both participate in the regulation of twitching motility. This suggests thatnthis sub-class of proteins is likely to have evolved with twitching motility as itsnprimary function, possibly acquiring additional HPt-like domains to eithernintegrate additional signalling inputs into the regulation of twitching motility ornto coordinate twitching motility with the expression or function of othernvirulence determinants. Analysis of HPt domain active site substitutions innmulti-HPt domain CheA/CheY hybrid proteins suggests that there may be anselective advantage, or a particular function, conferred by threoninensubstitutions of histidine residues, possibly reflecting the use of differentnphosphotransfer chemistries.n n The encoded chemotaxis-like protein domain structure, the surroundingnchromosomal gene organisation and the identification in a non-twitchingnscreen all suggest that chpA is involved in the regulation of twitching motility,nbut to date this has not been definitively proven by complementation of thenphenotype. Therefore, a range of chpA expression vectors and ChpAnphosphotransfer domain point mutants were generated, that togethernconstitute an invaluable resource for the elucidation of the role of ChpA innmotility and virulence in P. aeruginosa. The involvement of ChpA in regulatingntwitching motility was then confirmed by complementation. The results alsonshowed that ChpA function is dosage sensitive, and that ChpA is expressed tonrelatively low levels off its native promoter. The HPt2, HPt3 and CheYndomains of ChpA were identified as the specific domains that participate in thenregulation of twitching motility, with further characterisation of thenphosphotransfer domain point mutants showing that ChpA is not responsiblenfor regulating twitching motility at the level of pilA transcription. A model fornthe phosphotransfer circuitry that regulates twitching motility is thereforenproposed that integrates the findings of this thesis with what is known aboutnphosphotransfer relays in chemosensory pathways.n n The ChpA point mutants displayed several distinct phenotypes undernconditions conducive to swarming. However, because the observed motilityndisplayed a complete dependence on type IV pili it is not entirely clearnwhether the motility is swarming (flagella-mediated) or a more complexnmanifestation of a retractile motility (fimbriae-mediated). Regardless of this,nthe swarm assay appears to be a more sensitive tool to investigate andnanalyse the perturbations and complexities of the ChpA point mutants thannthe standard twitching stab assay, as is evidenced by the five different motilitynphenotypes displayed. Of particular importance is the identification of anmotility phenotype for the SPt point mutant that has tentatively been linked tonaberrant rhamnolipid levels. This is then the first report to show functionalitynfor a bacterial serine phosphotransfer domain in the context of a CheA-likenprotein kinase, and possibly constitutes evidence that a function of ChpA is toncoordinate regulation of auxiliary virulence determinants with motility.n" @default.
• W19774080 created "2016-06-24" @default.
• W19774080 creator A5075233983 @default.
• W19774080 date "2004-01-01" @default.
• W19774080 modified "2023-09-27" @default.
• W19774080 title "The role of ChpA in Pseudomonas aeruginosa motility" @default.
• W19774080 hasPublicationYear "2004" @default.
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