Tcm62p, distantly related to chaperonins, is required for the assembly of succinate dehydrogenase in mitochondria of Saccharomyces cerevisiae and was proposed to exert chaperone activity. We demonstrate here crucial functions of Tcm62p under heat stress. It ensures mitochondrial gene expression at elevated temperatures and prevents heat-aggregation of the ribosomal subunit Var1p. Similar to chaperonins, Tcm62p forms a high molecular mass protein complex of approximately 850 kDa in the mitochondrial matrix space. These results suggest a more general chaperone function of Tcm62p in mitochondria.
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| rdf:type | |
| rdfs:comment |
Tcm62p, distantly related to chaperonins, is required for the assembly of succinate dehydrogenase in mitochondria of Saccharomyces cerevisiae and was proposed to exert chaperone activity. We demonstrate here crucial functions of Tcm62p under heat stress. It ensures mitochondrial gene expression at elevated temperatures and prevents heat-aggregation of the ribosomal subunit Var1p. Similar to chaperonins, Tcm62p forms a high molecular mass protein complex of approximately 850 kDa in the mitochondrial matrix space. These results suggest a more general chaperone function of Tcm62p in mitochondria.
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| skos:exactMatch | |
| uniprot:name |
FEBS Lett.
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| uniprot:author |
Klanner C.,
Langer T.,
Neupert W.
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| uniprot:date |
2000
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| uniprot:pages |
365-369
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| uniprot:title |
The chaperonin-related protein Tcm62p ensures mitochondrial gene expression under heat stress.
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| uniprot:volume |
470
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| dc-term:identifier |
doi:10.1016/S0014-5793(00)01322-3
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