Assembly of the cytochrome bo3 complex.
An understanding of the mechanisms that govern the assembly of macromolecular protein complexes is fundamental for studying their function and regulation. With this in mind, we have determined the assembly pathway for the membrane-embedded cytochrome bo(3) of Escherichia coli. We show that there is a preferred order of assembly, where subunits III and IV assemble first, followed by subunit I and finally subunit II. We also show that cofactor insertion catalyses assembly. These findings provide novel insights into the biogenesis of this model membrane protein complex.
Stenberg
Filippa
F
Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, Sweden.
von Heijne
Gunnar
G
Daley
Daniel O
DO
D003067:Coenzymes / Q000378:metabolism; D003573:Cytochrome b Group; D003580:Cytochromes / Q000737:chemistry* / Q000378:metabolism; D019281:Dimerization; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism; D008970:Molecular Weight; D010084:Oxidation-Reduction; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism
D003067:Coenzymes; D003573:Cytochrome b Group; D003580:Cytochromes; D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; D021122:Protein Subunits; C083850:cytochrome bo3, E coli