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Tim29 is a novel subunit of the human TIM22 translocase and is involved in complex assembly and stability

Kang, Yilin, Baker, Michael James, Liem, Michael, Louber, Jade, McKenzie, Matthew, Atukorala, Ishara, Ang, Ching-Seng, Keerthikumar, Shivakumar, Mathivanan, Suresh and Stojanovski, Diana 2016, Tim29 is a novel subunit of the human TIM22 translocase and is involved in complex assembly and stability, eLife, vol. 5, pp. 1-23, doi: 10.7554/eLife.17463.

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Title Tim29 is a novel subunit of the human TIM22 translocase and is involved in complex assembly and stability
Author(s) Kang, Yilin
Baker, Michael James
Liem, Michael
Louber, Jade
McKenzie, MatthewORCID iD for McKenzie, Matthew orcid.org/0000-0001-7508-1800
Atukorala, Ishara
Ang, Ching-Seng
Keerthikumar, Shivakumar
Mathivanan, Suresh
Stojanovski, Diana
Journal name eLife
Volume number 5
Start page 1
End page 23
Total pages 23
Publisher eLife Sciences Publications
Place of publication Cambridge, Eng.
Publication date 2016-08-24
ISSN 2050-084X
2050-084X
Keyword(s) TIM22
biochemistry
cell biology
human
mitochondria
protein trafficking
Cell Line
Humans
Mitochondrial Membrane Transport Proteins
Mitochondrial Membranes
Protein Multimerization
Protein Subunits
Science & Technology
Life Sciences & Biomedicine
Biology
Life Sciences & Biomedicine - Other Topics
MITOCHONDRIAL INNER MEMBRANE
DEAFNESS DYSTONIA SYNDROME
INTERMEMBRANE SPACE
PROTEIN IMPORT
QUANTITATIVE PROTEOMICS
PREPROTEIN TRANSLOCASE
MEDIATES INSERTION
TOM
SUPERCOMPLEX
BIOGENESIS
Summary The TIM22 complex mediates the import of hydrophobic carrier proteins into the mitochondrial inner membrane. While the TIM22 machinery has been well characterised in yeast, the human complex remains poorly characterised. Here, we identify Tim29 (C19orf52) as a novel, metazoan-specific subunit of the human TIM22 complex. The protein is integrated into the mitochondrial inner membrane with it’s C-terminus exposed to the intermembrane space. Tim29 is required for the stability of the TIM22 complex and functions in the assembly of hTim22. Furthermore, Tim29 contacts the Translocase of the Outer Mitochondrial Membrane, TOM complex, enabling a mechanism for transport of hydrophobic carrier substrates across the aqueous intermembrane space. Identification of Tim29 highlights the significance of analysing mitochondrial import systems across phylogenetic boundaries, which can reveal novel components and mechanisms in higher organisms.
Language eng
DOI 10.7554/eLife.17463
HERDC Research category C1.1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2016, Kang et al.
Free to Read? Yes
Use Rights Creative Commons Attribution licence
Persistent URL http://hdl.handle.net/10536/DRO/DU:30111629

Document type: Journal Article
Collections: School of Life and Environmental Sciences
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Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.