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Título: | The β-tubulin monomer release factor (p14) has homology with a region of the DnaJ protein |
Autor: | Llosa, Matxalen CSIC ORCID; Aloria, Kerman; Campo, Rafael; Padilla, Rodolfo; Ávila, Jesús CSIC ORCID ; Sánchez-Pulido, Luis; Zabala, Juan Carlos | Palabras clave: | J-domain p14 β-Tubulin α-Tubulin Protein folding Molecular chaperone |
Fecha de publicación: | 1996 | Editor: | Elsevier | Citación: | FEBS Letters 397(2-3): 283-289 (1996) | Resumen: | p14 is a molecular chaperone involved in β-tubulin folding which catalyzes the release of β-tubulin monomers from intermediate complexes. Here we demonstrate that active p14 protein which we have purified from an overproducing Escherichia coli strain can also release β-tubulin monomers from tubulin dimers in the presence of an additional cofactor (Z). Analysis of p14 secondary structure suggests that this protein may belong to a family of conserved proteins which share structural similarities with the J-domain of DnaJ. We have constructed deletions and site-directed mutations in the p14 gene. A single D to E mutation in the region shown in DnaJ to be an essential loop for its function affected the monomer-release activity of p14. These results support the hypothesis that this p14 loop interacts with β-tubulin in a similar fashion as DnaJ interacts with DnaK and suggest a possible role of p14 in the folding process. | URI: | http://hdl.handle.net/10261/93208 | DOI: | 10.1016/S0014-5793(96)01198-2 | Identificadores: | doi: 10.1016/S0014-5793(96)01198-2 issn: 0014-5793 e-issn: 1873-3468 |
Aparece en las colecciones: | (IBBTEC) Artículos (CNB) Artículos (CBM) Artículos |
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