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Structural basis fo...
Structural basis for Cbp3 interaction with newly synthesized cytochrome b during mitochondrial respiratory chain assembly
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- Ndi, Mama (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Masuyer, Geoffrey (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,University of Bath, UK
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- Dawitz, Hannah (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Carlström, Andreas (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Michel, Mirco (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,Science for Life Laboratory (SciLifeLab)
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- Elofsson, Arne (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,Science for Life Laboratory (SciLifeLab)
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- Rapp, Mikaela (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Stenmark, Pål (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,Lund University, Sweden
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- Ott, Martin (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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(creator_code:org_t)
- 2019
- 2019
- English.
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In: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 294:45, s. 16663-16671
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https://doi.org/10.1...
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https://urn.kb.se/re...
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Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- respiratory chain
- complex III
- assembly factor
- mitochondrial translation
- protein assembly
- membrane biogenesis
- protein crosslinking
- ubiquinol-cytochrome c chaperone domain
- structural biology
- electron transfer chain
- biokemi
- Biochemistry
Publication and Content Type
- ref (subject category)
- art (subject category)
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