Related Experiment Video
Updated: Jun 5, 2026

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
Aspartate chemosensory receptor signalling in Campylobacter jejuni
1Institute for Glycomics, Griffith University Gold Coast Campus, Gold Coast, QLD, Australia. v.korolik@griffith.edu.au
Abstract:
The human bacterial pathogen Campylobacter jejuni is able to respond to environmental stimuli utilising chemotactic motility. The bacterial senses external molecules via transmembrane sensory proteins called Transducer Like Proteins, TLPs. The specificity of the Tlp1 chemoreceptor (Cj1506c) of C. jejuni as the aspartate receptor, CcaA, and its role in chemotaxis signalling pathway were characterised by genetic and biochemical approaches including amino acid and small molecule arrays, Saturation Transfer Difference NMR spectroscopy, and mutational analysis. Yeast two-hybrid and three-hybrid analysis of protein-protein interactions showed that CcaA chemotactic signal was preferentially passed through CheV, rather than the CheW homologue of the chemotaxis signalling pathway allowing a new model for the C. jejuni chemotactic signalling pathway to be postulated.
Related Concept Videos
Chemotaxis in E. coli
cAMP-dependent Protein Kinase Pathways
Bacterial Signaling
Regulation of Bacterial Virulence
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
GPCRs Regulate Adenylyl Cylase Activity
Two...

