Structural basis for the interaction of the chaperone Cbp3 with newly synthesized cytochrome b during mitochondrial respiratory chain assembly
Ndi, Mama ; Masuyer, Geoffrey ; Dawitz, Hannah ; Carlström, Andreas ; Michel, Mirco ; Elofsson, Arne ; Rapp, Mikaela ; Stenmark, Pål LU
and Ott, Martin
(2019)
In Journal of Biological Chemistry
294(45).
p.16663-16671
- Abstract
Assembly of the mitochondrial respiratory chain requires the coordinated synthesis of mitochondrial and nuclear encoded subunits, redox co-factor acquisition, and correct joining of the subunits to form functional complexes. The conserved Cbp3-Cbp6 chaperone complex binds newly synthesized cytochrome b and supports the ordered acquisition of the heme co-factors. Moreover, it functions as a translational activator by interacting with the mitoribosome. Cbp3 consists of two distinct domains, an N-terminal domain present in mitochondrial Cbp3 homologs, and a highly conserved C-terminal domain comprising a ubiquinol-cytochrome c chaperone region. Here, we solved the crystal structure of this C-terminal domain from a bacterial homolog at 1.4... (More)
Assembly of the mitochondrial respiratory chain requires the coordinated synthesis of mitochondrial and nuclear encoded subunits, redox co-factor acquisition, and correct joining of the subunits to form functional complexes. The conserved Cbp3-Cbp6 chaperone complex binds newly synthesized cytochrome b and supports the ordered acquisition of the heme co-factors. Moreover, it functions as a translational activator by interacting with the mitoribosome. Cbp3 consists of two distinct domains, an N-terminal domain present in mitochondrial Cbp3 homologs, and a highly conserved C-terminal domain comprising a ubiquinol-cytochrome c chaperone region. Here, we solved the crystal structure of this C-terminal domain from a bacterial homolog at 1.4 Å resolution, revealing a unique all-helical fold. This structure allowed mapping of the interaction sites of yeast Cbp3 with Cbp6 and cytochrome b via site-specific photo-crosslinking. We propose that mitochondrial Cbp3 homologs carry an N-terminal extension that positions the conserved C-terminal domain at the ribosomal tunnel exit for an efficient interaction with its substrate, the newly synthesized cytochrome b protein.
(Less)
- author
- Ndi, Mama
; Masuyer, Geoffrey
; Dawitz, Hannah
; Carlström, Andreas
; Michel, Mirco
; Elofsson, Arne
; Rapp, Mikaela
; Stenmark, Pål
LU
and Ott, Martin
- publishing date
- 2019-09-19
- type
- Contribution to journal
- publication status
- published
- in
- Journal of Biological Chemistry
- volume
- 294
- issue
- 45
- pages
- 16663 - 16671
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- scopus:85074705948
- pmid:31537648
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.RA119.010483
- language
- English
- LU publication?
- no
- additional info
- Published under license by The American Society for Biochemistry and Molecular Biology, Inc.
- id
- 983873f2-a61a-4057-9d92-23182a2bab22
- date added to LUP
- 2019-09-25 14:24:15
- date last changed
- 2024-08-21 08:35:18
@article{983873f2-a61a-4057-9d92-23182a2bab22,
abstract = {{<p>Assembly of the mitochondrial respiratory chain requires the coordinated synthesis of mitochondrial and nuclear encoded subunits, redox co-factor acquisition, and correct joining of the subunits to form functional complexes. The conserved Cbp3-Cbp6 chaperone complex binds newly synthesized cytochrome b and supports the ordered acquisition of the heme co-factors. Moreover, it functions as a translational activator by interacting with the mitoribosome. Cbp3 consists of two distinct domains, an N-terminal domain present in mitochondrial Cbp3 homologs, and a highly conserved C-terminal domain comprising a ubiquinol-cytochrome c chaperone region. Here, we solved the crystal structure of this C-terminal domain from a bacterial homolog at 1.4 Å resolution, revealing a unique all-helical fold. This structure allowed mapping of the interaction sites of yeast Cbp3 with Cbp6 and cytochrome b via site-specific photo-crosslinking. We propose that mitochondrial Cbp3 homologs carry an N-terminal extension that positions the conserved C-terminal domain at the ribosomal tunnel exit for an efficient interaction with its substrate, the newly synthesized cytochrome b protein.</p>}},
author = {{Ndi, Mama and Masuyer, Geoffrey and Dawitz, Hannah and Carlström, Andreas and Michel, Mirco and Elofsson, Arne and Rapp, Mikaela and Stenmark, Pål and Ott, Martin}},
issn = {{1083-351X}},
language = {{eng}},
month = {{09}},
number = {{45}},
pages = {{16663--16671}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Structural basis for the interaction of the chaperone Cbp3 with newly synthesized cytochrome b during mitochondrial respiratory chain assembly}},
url = {{http://dx.doi.org/10.1074/jbc.RA119.010483}},
doi = {{10.1074/jbc.RA119.010483}},
volume = {{294}},
year = {{2019}},
}