| Título: | Biochemical and Biophysical Characterization of Recombinant Yeast Proteasome Maturation Factor Ump1 |
| Autores: |
Sá-Moura, Bebiana; IBMC - Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto Simões, Ana Marisa; IBMC - Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto Fraga, Joana; IBMC - Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto Fernandes, Humberto; Centre for Molecular and Structural Biomedicine, CBME/IBB, LA Abreu, Isabel A.; IBMC - Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto Botelho, Hugo M.; Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa Gomes, Cláudio M.; Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa Marques, António J.; Institute for Genetics, University of Cologne, Zülpicher Str. 47, D-50674 Cologne Dohmen, R. Jürgen; Institute for Genetics, University of Cologne, Zülpicher Str. 47, D-50674 Cologne Ramos, Paula C.; Centre for Molecular and Structural Biomedicine, CBME/IBB, LA Macedo-Ribeiro, Sandra; IBMC - Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto |
| Fecha: | 2013-09-10 |
| Publicador: | Computacional and structural biotechnology journal |
| Fuente: |
 |
| Tipo: |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Peer-reviewed Article |
| Tema: | No aplica |
| Descripción: | Protein degradation is essential for maintaining cellular homeostasis. The proteasome is the central enzyme responsible for non-lysosomal protein degradation in eukaryotic cells. Although proteasome assembly is not yet completely understood, a number of cofactors required for proper assembly and maturation have been identified. Ump1 is a short-lived maturation factor required for the efficient biogenesis of the 20S proteasome. Upon the association of the two precursor complexes, Ump1 is encased and is rapidly degraded after the proteolytic sites in the interior of the nascent proteasome are activated. In order to further understand the mechanisms behind proteasomal maturation, we expressed and purified yeast Ump1 in E. coli for biophysical and structural analysis. We show that recombinant Ump1 is purified as a mixture of different oligomeric species and that oligomerization is mediated by intermolecular disulfide bond formation involving the only cysteine residue present in the protein. Furthermore, a combination of bioinformatic, biochemical and structural analysis revealed that Ump1 shows characteristics of an intrinsically disordered protein, which might become structured only upon interaction with the proteasome subunits. |
| Idioma: | Inglés |
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