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|Type:||Artigo de periódico|
|Title:||Structural and stability studies of the human mtHsp70-escort protein 1: An essential mortalin co-chaperone|
|Abstract:||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 hHepl oligomerizes in a concentration-dependent fashion and that the zinc ion, which is essential for hHepl in vivo function, has an important protein-structure stabilizing effect. (C) 2013 Elsevier B.V. All rights reserved.|
|Editor:||Elsevier Science Bv|
|Citation:||International Journal Of Biological Macromolecules. Elsevier Science Bv, v. 56, n. 140, n. 148, 2013.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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