The β-tubulin monomer release factor (p14) has homology with a region of the DnaJ protein
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...
| Autores: | , , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 1996 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/93208 |
| Acceso en línea: | http://hdl.handle.net/10261/93208 |
| Access Level: | acceso abierto |
| Palabra clave: | J-domain p14 β-Tubulin α-Tubulin Protein folding Molecular chaperone |
| Sumario: | 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. |
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