RESEARCH SUMMARY

Our group is interested in the structural and functional characterisation of macromolecular complexes using as main tools electron microscopy and image processing techniques. In particular, we are very much interested in the study of molecular chaperones, a group of proteins involved in assisting not only the folding of other proteins but also their degradation.

These two processes are carried in most cases by the coordinated concourse of different chaperones, which form transient complexes, thus forming an assembly line that make more efficient the protein folding and degradation processes. Currently, we are working with different chaperones such as CCT, Hsp70, PFD, PhLP,...

We are also studying the structure of the centrosome and of some centrosomal complexes and proteins. The centrosome is the major microtubule organising center (MTOC) in most animal cells. Typically, centrosomes are made of a pair of centrioles embedded in the amorphous, pericentriolar material (PCM). We are studying the overall structure of the centrosome using two approaches, the first one is electron tomography, a technique that has recently undergone major advances, and which may allow the structural characterization of entire centrosomes in condition close to the native state. The second approach is to use X-ray tomography, a technique that certainly allows the reconstruction of whole centrosomes, albeit at lower resolution than electron tomography. We plan to use the facilities that are being set up in the dedicated beam line at the Spanish ALBA Synchrotron. We are also working in the structural characterisation of centrosomal proteins using conventional electron microscopy.

Finally, we are also interested, in collaboration with the group of Dr Carrascosa in the characterisation of the forces involved in the function of certain proteins and in the manipulation of cellular organelles, using single molecule techniques such as optical and magnetic tweezers.