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Structural and functional differences between mouse mot-1 and mot-2 proteins that differ in two amino acids.

Custer C Deocaris·Kazuhiko Yamasaki·Sunil C Kaul·Renu Wadhwa
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Abstract

Chaperone functions mediated by the heat-shock protein (HSP) family constitute a fundamental mechanism that governs the life span of organisms. Here we investigated the chaperone activities of the mitochondrial HSP70 protein, mortalin, which is a heat-uninducible stress protein involved in immortalization and tumorigenesis. There are two mortalin alleles, mot-1 and mot-2, in mouse, encoding two distinct proteins. Whereas an overexpression of mot-1-induced senescence in NIH 3T3 cells, overexpression of mot-2 promoted their malignant properties. Here, we provide evidence that mot-1 possesses very low chaperone activity as compared to mot-2. A "lazy lid" hypothesis is proposed for their differential aging phenotypes.

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AllelesAmino Acid SequenceAmino AcidsAnimalsCell Line, TumorFibroblastsHSP70 Heat-Shock ProteinsHot TemperatureHumansLuciferasesMiceMolecular Sequence DataMolecular StructureProtein RenaturationTransfectionComparative StudyJournal Article

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Custer C Deocaris, Kazuhiko Yamasaki, Sunil C Kaul, Renu Wadhwa. 2006. Structural and functional differences between mouse mot-1 and mot-2 proteins that differ in two amino acids.. https://doi.org/10.1196/annals.1354.027

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