Abstract
UreE, a urease accessory protein, is proposed to be a metallochaperone assisting the nickel incorporation into the urease active site. We investigated the effects of salt and nickel on the conformational stability of the UreE from Bacillus pasteurii ( BpUreE), by circular dichroism (CD) and nuclear magnetic resonance spectroscopy accompanying a thermodynamic inspection. Far-UV CD spectra of BpUreE showed that both salt and nickel stabilized the ordered structure of the protein. The thermal denaturing of BpUreE showed a bimodal feature with an aggregation process before thermal unfolding. This thermally induced aggregation could be suppressed by the addition of salt up to 50 mM, and the further addition of salt increased the thermal resistance of the protein. The nickel addition also elevated the thermal resistance of BpUreE, although it could not prevent the aggregating process. Additionally, the stoichiometry of a specific nickel binding to BpUreE was revealed as one nickel per dimer. Altogether, the present results establish a rather detailed characterization of the thermostability and nickel-binding property of BpUreE.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
