Controlling Protein Nanocage Assembly with Hydrostatic Pressure.

Autor: Le Vay K; School of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, U.K.; Bristol Centre for Functional Nanomaterials, HH Wills Physics Laboratory, University of Bristol, Tyndall Avenue, Bristol BS8 1TL, U.K., Carter BM; School of Cellular and Molecular Medicine, University of Bristol, University Walk, Bristol BS8 1TD, U.K., Watkins DW; School of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, U.K., Dora Tang TY; School of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, U.K., Ting VP; Bristol Composites Institute (ACCIS), Department of Mechanical Engineering, University of Bristol, Queen's Building, Bristol BS8 1TR, U.K., Cölfen H; Department of Chemistry, University of Konstanz, Universitätsstraße 10, 78457 Konstanz, Germany., Rambo RP; Diamond House, Diamond Light Source Ltd., Harwell Science and Innovation Campus, Fermi Ave., Didcot OX11 0DE, U.K., Smith AJ; Diamond House, Diamond Light Source Ltd., Harwell Science and Innovation Campus, Fermi Ave., Didcot OX11 0DE, U.K., Ross Anderson JL; School of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, U.K.; BrisSynBio Synthetic Biology Research Centre, Life Sciences Building, University of Bristol, Tyndall Avenue, Bristol BS8 1TQ, U.K., Perriman AW; School of Cellular and Molecular Medicine, University of Bristol, University Walk, Bristol BS8 1TD, U.K.
Jazyk: angličtina
Zdroj: Journal of the American Chemical Society [J Am Chem Soc] 2020 Dec 09; Vol. 142 (49), pp. 20640-20650. Date of Electronic Publication: 2020 Nov 30.
DOI: 10.1021/jacs.0c07285
Abstrakt: Controlling the assembly and disassembly of nanoscale protein cages for the capture and internalization of protein or non-proteinaceous components is fundamentally important to a diverse range of bionanotechnological applications. Here, we study the reversible, pressure-induced dissociation of a natural protein nanocage, E. coli bacterioferritin (Bfr), using synchrotron radiation small-angle X-ray scattering (SAXS) and circular dichroism (CD). We demonstrate that hydrostatic pressures of 450 MPa are sufficient to completely dissociate the Bfr 24-mer into protein dimers, and the reversibility and kinetics of the reassembly process can be controlled by selecting appropriate buffer conditions. We also demonstrate that the heme B prosthetic group present at the subunit dimer interface influences the stability and pressure lability of the cage, despite its location being discrete from the interdimer interface that is key to cage assembly. This indicates a major cage-stabilizing role for heme within this family of ferritins.
Databáze: MEDLINE
Externí odkaz: