- Dos grupos del CNB entre los nuevos proyectos de investigación financiados en la sexta edición de la convocatoria CaixaResearch de Investigación en Salud, promovida por la Fundación ”la Caixa”
- La convocatoria apoya proyectos de investigación básica, clínica o traslacional de excelencia científica y de impacto social en los ámbitos de estudio de las enfermedades cardiovasculares y las infecciosas, en oncología y en neurociencias, así como proyectos que desarrollan tecnologías facilitadoras en estos ámbitos.
La Fundación ”la Caixa” ha celebrado en Barcelona el acto de entrega de ayudas a los 33 proyectos de investigación en biomedicina y salud que se llevarán a cabo en centros de España y Portugal. Se trata de proyectos seleccionados en el marco de la convocatoria CaixaResearch de Investigación en Salud 2023, que tiene el objetivo de impulsar la investigación biomédica de excelencia con gran impacto social en investigación básica, clínica y traslacional. Los grupos de Daniel López Serrano y José María Valpuesta se encuentran entre los seleccionados para desarrollar estos proyectos.
En la ceremonia, que ha tenido lugar en el Museo de la Ciencia CosmoCaixa, el director general de la Fundación ”la Caixa”, Antonio Vila Bertrán, ha recordado: «La investigación científica es fundamental para el progreso social y el bienestar de los ciudadanos. La ciencia no solo nos ayuda a construir la sociedad del conocimiento, sino que es clave para mejorar la calidad de vida de aquellos que más lo necesitan».
La convocatoria, a la que este año se habían presentado 493 propuestas, está especialmente dirigida al abordaje de retos de salud, como las enfermedades infecciosas (ámbito sobre el que se han elegido 8 proyectos), las neurociencias (7), las enfermedades cardiovasculares y metabólicas relacionadas (7) y la oncología (6). Además, otras 5 iniciativas premiadas desarrollarán tecnologías facilitadoras en alguno de estos campos.
La flexibilidad de las chaperonas moleculares, un conjunto de proteínas presentes en todas las células, favorece que actúen en diferentes procesos. Por un lado, ayudan a que otras proteínas recién formadas adopten la estructura tridimensional adecuada para su funcionamiento (plegamiento), pero, por otro, contribuyen a su degradación, un proceso opuesto al anterior, pero también esencial a nivel celular.
Nat Struct Mol Biol. 2016 Aug 1. doi: 10.1038/nsmb.3272
Sousa R, Liao HS, Cuéllar J, Jin S, Valpuesta JM, Jin AJ, Lafer EM
A study conducted jointly by scientists from the United States and Spain shows how Hsp70 chaperones work. As if they were nanomachines, the Hsp70 generate force on other proteins through collisions and stretching, to break bonds between them or transport them through the membranes of different cell compartments.
Del 2 al 4 de abril de 2014 se va a celebrar en el Centro Nacional de Biotecnología del CSIC (CNB) VIII Reunión de la Red Nacional de Estructura y Función de Proteínas.
Organizada por los científicos del CNB José María Valpuesta y José L. Carrascosa, la reunión pretende reunir a gran parte de la comunidad científica española que estudia distintos aspectos de las proteínas, para intercambiar conocimientos y fomentar colaboraciones. En esta reunión seguirá el formato de las anteriores, con charlas cortas que permitan mostrar los resultados al mayor número posible de investigadores, dando preferencia para las charlas a investigadores junior.
Para la organización de la reunión se cuenta con la ayuda del Ministerio de Economía y Competitividad y con apoyo por parte del Centro Nacional de Biotecnología y de varias sociedades científicas (SEBBM y SME) y empresas colaboradoras de la Red (Bruker, Sigma-Aldrich y Diffractia). Todo ello ha permitido la invitación de varios científicos que abrirán los simposios de la Reunión (ver Programa provisional).
La asistencia a la reunión será por cuenta de los investigadores participantes, tal como ha ocurrido en anteriores eventos, aunque habrá un número de ayudas a la asistencia para investigadores, financiadas por distintas sociedades científicas, cuyo número y cuantía está aun por determinar.
J Biol Chem. 2013 Jun 7;288(23):16998-7007
Daudén MI, Martín-Benito J, Sánchez-Ferrero JC, Pulido-Cid M, Valpuesta JM, Carrascosa JL.
During bacteriophage morphogenesis DNA is translocated into a preformed prohead by the complex formed by the portal protein, or connector, plus the terminase, which are located at an especial prohead vertex. The terminase is a powerful motor that converts ATP hydrolysis into mechanical movement of the DNA. Here, we have determined the structure of the T7 large terminase by electron microscopy.
The five terminase subunits assemble in a toroid that encloses a channel wide enough to accommodate dsDNA. The structure of the complete connector-terminase complex is also reported, revealing the coupling between the terminase and the connector forming a continuous channel. The structure of the terminase assembled into the complex showed a different conformation when compared with the isolated terminase pentamer. To understand in molecular terms the terminase morphological change, we generated the terminase atomic model based on the crystallographic structure of its phage T4 counterpart. The docking of the threaded model in both terminase conformations showed that the transition between the two states can be achieved by rigid body subunit rotation in the pentameric assembly. The existence of two terminase conformations and its possible relation to the sequential DNA translocation may shed light into the molecular bases of the packaging mechanism of bacteriophage T7.
Cuellar J, Perales-Calvo J, Muga A, Valpuesta JM, Moro F.
Hsp40 chaperones bind and transfer substrate proteins to Hsp70s and regulate their ATPase activity. The interaction of Hsp40s with native proteins modifies their structure and function. A good model for this function is DnaJ, the bacterial Hsp40 that interacts with RepE, the repressor/activator of plasmid F replication, and together with DnaK regulates its function. We characterize here the structure of the DnaJ:RepE complex by electron microscopy, the first described structure of a complex between an Hsp40 and a client protein. The comparison of the complexes of DnaJ with two RepE mutants reveals an intrinsic plasticity of the DnaJ dimer that allows the chaperone to adapt to different substrates. We also show that DnaJ induces conformational changes in dimeric RepE, which increase the intermonomeric distance and remodel both RepE domains enhancing its affinity for DNA.
Según se van sintetizando las proteínas en los ribosomas, éstas tienen que ir tomando la forma adecuada para poder ejercer su función. Aunque las características físico-químicas de los aminoácidos que las forman determinan en gran parte la forma que adquieren, hay muchas proteínas que necesitan ayuda extra de parte de un grupo de proteínas conocidas como chaperonas.
Para comprender mejor cómo funcionan estas proteínas, en su laboratorio del Centro Nacional de Biotecnología del CSIC (CNB), el grupo dirigido por José María Valpuesta ha utilizado la microscopía electrónica. Gracias a esta técnica han podido determinar por primera vez la estructura de un complejo formado por la chaperona DnaJ y su sustrato, lo que les ha permitido observar cómo la chaperona cambia la estructura del sustrato y con ello su función.
En colaboración con la Universidad del País Vasco, el investigador postdoctoral del CNB Jorge Cuéllar ha identificado además en dicha chaperona una zona de gran flexibilidad que le permite adaptarse a la forma de distintas proteínas. Como se puede apreciar en la imagen de abajo, la forma que adopta la chaperona DnaJ (en azul) cambia radicalmente en función del sustrato al que se une (RepE1-144, RepE o Rep54; en amarillo). De este modo, una misma chaperona es capaz de unirse a una variedad de proteínas diferentes, consiguiendo en todas ellas que adquieran la forma necesaria para funcionar.
- Cuéllar J, Perales-Calvo J, Muga A, Valpuesta JM, Moro F. Structural insights into the chaperone activity of the 40 kDa heat shock protein DnaJ. Binding and remodeling of a native substrate. J Biol Chem 2013 Apr 11. [doi: 10.1074/jbc.M112.430595].
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