TY  - JOUR
A1  - Schimo, Sonja
A1  - Wittig, Ilka
A1  - Pos, Klaas Martinus
A1  - Ludwig, Bernd
T1  - Cytochrome c oxidase biogenesis and metallochaperone interactions : steps in the assembly pathway of a bacterial complex
T2  - PLoS one
N2  - Biogenesis of mitochondrial cytochrome c oxidase (COX) is a complex process involving the coordinate expression and assembly of numerous subunits (SU) of dual genetic origin. Moreover, several auxiliary factors are required to recruit and insert the redox-active metal compounds, which in most cases are buried in their protein scaffold deep inside the membrane. Here we used a combination of gel electrophoresis and pull-down assay techniques in conjunction with immunostaining as well as complexome profiling to identify and analyze the composition of assembly intermediates in solubilized membranes of the bacterium Paracoccus denitrificans. Our results show that the central SUI passes through at least three intermediate complexes with distinct subunit and cofactor composition before formation of the holoenzyme and its subsequent integration into supercomplexes. We propose a model for COX biogenesis in which maturation of newly translated COX SUI is initially assisted by CtaG, a chaperone implicated in CuB site metallation, followed by the interaction with the heme chaperone Surf1c to populate the redox-active metal-heme centers in SUI. Only then the remaining smaller subunits are recruited to form the mature enzyme which ultimately associates with respiratory complexes I and III into supercomplexes.
Y1  - 2017
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/42886
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-428863
UR  - https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5249081
SN  - 1932-6203
N1  - Copyright: © 2017 Schimo et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
VL  - 12
IS  - (1): e0170037
SP  - 1
EP  - 19
PB  - PLoS
CY  - Lawrence, Kan.
ER  -