Defining the architecture of the human TIM22 complex by chemical crosslinking

2020 | journal article; research paper. A publication with affiliation to the University of Göttingen.

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​Defining the architecture of the human TIM22 complex by chemical crosslinking​
Valpadashi, A.; Callegari, S. ; Linden, A.; Neumann, P. ; Ficner, R. ; Urlaub, H.   & Deckers, M.  et al.​ (2020) 
FEBS Letters595(2) pp. 157​-168​.​ DOI: https://doi.org/10.1002/1873-3468.13978 

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Authors
Valpadashi, Anusha; Callegari, Sylvie ; Linden, Andreas; Neumann, Piotr ; Ficner, Ralf ; Urlaub, Henning ; Deckers, Markus ; Rehling, Peter 
Abstract
The majority of mitochondrial proteins are nuclear encoded and imported into mitochondria as precursor proteins via dedicated translocases. The translocase of the inner membrane 22 (TIM22) is a multisubunit molecular machine specialized for the translocation of hydrophobic, multi‐transmembrane‐spanning proteins with internal targeting signals into the inner mitochondrial membrane. Here, we undertook a crosslinking‐mass spectrometry (XL‐MS) approach to determine the molecular arrangement of subunits of the human TIM22 complex. Crosslinking of the isolated TIM22 complex using the BS3 crosslinker resulted in the broad generation of crosslinks across the majority of TIM22 components, including the small TIM chaperone complex. The crosslinking data uncovered several unexpected features, opening new avenues for a deeper investigation into the steps required for TIM22‐mediated translocation in humans.
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Issue Date
2020
Journal
FEBS Letters 
Project
EXC 2067: Multiscale Bioimaging 
SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente 
SFB 1190 | P13: Protein Transport über den mitochondrialen Carrier Transportweg 
SFB 1190 | Z02: Massenspektrometrie-basierte Proteomanalyse 
Working Group
RG Ficner (Molecular Structural Biology) 
RG Rehling (Mitochondrial Protein Biogenesis) 
RG Urlaub (Bioanalytische Massenspektrometrie) 
External URL
https://mbexc.uni-goettingen.de/literature/publications/86
https://sfb1190.med.uni-goettingen.de/production/literature/publications/129
ISSN
0014-5793
eISSN
1873-3468
Language
English
Sponsor
Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659
Max Planck Society http://dx.doi.org/10.13039/501100004189

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