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  An inventory of interactors of the human HSP60/HSP10 chaperonin in the mitochondrial matrix space

Bie, A. S., Coemert, C., Körner, R., Corydon, T. J., Palmfeldt, J., Hipp, M. S., et al. (2020). An inventory of interactors of the human HSP60/HSP10 chaperonin in the mitochondrial matrix space. CELL STRESS & CHAPERONES. doi:10.1007/s12192-020-01080-6.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-FA6E-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-FDD6-D
Genre: Journal Article

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 Creators:
Bie, Anne Sigaard1, Author
Coemert, Cagla1, Author
Körner, Roman2, Author              
Corydon, Thomas J.1, Author
Palmfeldt, Johan1, Author
Hipp, Mark S.2, Author              
Hartl, F. Ulrich2, Author              
Bross, Peter1, Author
Affiliations:
1external, ou_persistent22              
2Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              

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Free keywords: SPASTIC PARAPLEGIA SPG13; HEAT-SHOCK-PROTEIN; CRYSTAL-STRUCTURE; IN-VITRO; HSP60; GENE; MUTATIONS; IDENTIFICATION; COMPLEX; GROESHSP60; HSP10; Molecular chaperone; Chaperonin; Mitochondrial protein quality control; Protein folding;
 Abstract: The HSP60/HSP10 chaperonin assists folding of proteins in the mitochondrial matrix space by enclosing them in its central cavity. The chaperonin forms part of the mitochondrial protein quality control system. It is essential for cellular survival and mutations in its subunits are associated with rare neurological disorders. Here we present the first survey of interactors of the human mitochondrial HSP60/HSP10 chaperonin. Using a protocol involving metabolic labeling of HEK293 cells, cross-linking, and immunoprecipitation of HSP60, we identified 323 interacting proteins. As expected, the vast majority of these proteins are localized to the mitochondrial matrix space. We find that approximately half of the proteins annotated as mitochondrial matrix proteins interact with the HSP60/HSP10 chaperonin. They cover a broad spectrum of functions and metabolic pathways including the mitochondrial protein synthesis apparatus, the respiratory chain, and mitochondrial protein quality control. Many of the genes encoding HSP60 interactors are annotated as disease genes. There is a correlation between relative cellular abundance and relative abundance in the HSP60 immunoprecipitates. Nineteen abundant matrix proteins occupy more than 60% of the HSP60/HSP10 chaperonin capacity. The reported inventory of interactors can form the basis for interrogating which proteins are especially dependent on the chaperonin.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published online
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

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Title: CELL STRESS & CHAPERONES
Source Genre: Journal
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Publ. Info: VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS : SPRINGER
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: - Identifier: ISSN: 1355-8145