Structural and stability studies of the human mtHsp70-escort protein 1: An essential mortalin co-chaperone
| العنوان: | Structural and stability studies of the human mtHsp70-escort protein 1: An essential mortalin co-chaperone |
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| المؤلفون: | Karine Minari, Carlos H.I. Ramos, Leandro R.S. Barbosa, Júlio César Borges, Paulo R. Dores-Silva |
| المصدر: | Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual) Universidade de São Paulo (USP) instacron:USP |
| بيانات النشر: | Elsevier B.V. |
| مصطلحات موضوعية: | Protein Folding, Mortalin, Mitochondrion, Biology, Biochemistry, Fluorescence, Structure-Activity Relationship, Hep1, Structural Biology, Humans, Oligomerization, HSP70 Heat-Shock Proteins, Protein Structure, Quaternary, Molecular Biology, Zinc finger, Protein Stability, Tryptophan, Zinc Fingers, General Medicine, BIOLOGIA MOLECULAR, Recombinant Proteins, In vitro, Mitochondria, Protein Structure, Tertiary, Transport protein, Co-chaperone, Zinc, Mitochondrial biogenesis, mtHsp70, Hydrodynamics, Analytical ultracentrifugation, Protein folding, Protein Multimerization, Function (biology), Molecular Chaperones |
| الوصف: | Mitochondrial Hsp70 is involved in both protein import and folding process, among other essential functions. In mammalian cells, due to its role in the malignant process, it receives the name of mortalin. Despite its importance in protein and mitochondrial homeostasis, mortalin tends to self-aggregate in vitro and in vivo, the later leads to mitochondrial biogenesis failure. Recently, a zinc-finger protein, named Hsp70-escort protein 1 (Hep1, also called Zim17/TIM15/DNLZ), was described as an essential human mitochondrial mortalin co-chaperone which avoids its self-aggregation. Here, we report structural studies of the human Hep1 (hHep1). The results indicate that hHep1 shares some structural similarities with the yeast ortholog despite the low identity and functional differences. We also observed that hHep1 oligomerizes in a concentration-dependent fashion and that the zinc ion, which is essential for hHep1 in vivo function, has an important protein-structure stabilizing effect. |
| اللغة: | English |
| تدمد: | 0141-8130 |
| DOI: | 10.1016/j.ijbiomac.2013.02.009 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d6f17ecb3c350172ae69dfac00dc698 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....5d6f17ecb3c350172ae69dfac00dc698 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 01418130 |
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| DOI: | 10.1016/j.ijbiomac.2013.02.009 |