Tesis doctoral de Roman Bonet Figueredo
The present work has been done in the protein nmr group from the structural and computational biology at the irb barcelona, under the direction of dr. Maria j. Macias. the group main interest is the structural determination of protein domains, in the study of their interactions and in the understanding of the mechanisms for their regulation. In particular, this work is focused in the structural study of ff domains. in our group, the study of ff domains began from the observation that these domains are often found in proteins that also contain ww domains, a small protein-protein interaction domain that has been, and continues to be the central research line of the group and that has been object of numerous and detailed studies. conversely, ff domains have been recently identified and the structural and functional information available on them is, to date, limited. One of the reasons of the few studies reported for these domains could be consequence of their reduced presence in proteins. In fact, ff domains are only present in three protein families: the splicing factors fbp11, prp40 and urn1, the transcription factor ca150 and a family of rhogtpase regulators, the p190 rhogaps. in our group, the work with ff domains started with the solution of the three-dimensional structure of the first ff domain from yeast prp40, which just represented the second solved structure for an ff domain. In the present work the aim has been to gain insight into ff domain knowledge, basically from a structural point of view, using nuclear magnetic resonance (nmr) as the principal methodology for the structural studies. this thesis has been divided in three parts, and in each of them we have work with ff domains from the different families mentioned above. The subject of study has been also slightly different in each part. In the first chapter, focused in ff domains present in prp40 and urn1 splicing factors, the principal work consisted in the obtaining of novel three-dimensional structures for these domains by nmr. In contrast, in the second chapter the main interest was the study of the interaction of ca150 ff domains with their first described ligand, a doubly phosphorylated motif of the rna polymerase ii c-terminal domain (phospho-ctd). Finally, in the last part our efforts were focused in the study of the regulation of p190-a rhogap ff domains association with the general transcription factor tfii-i through phosphorylation on the first ff domain of p190-a rhogap.
Datos académicos de la tesis doctoral «Sturctural studies on ff domains by nmr spectroscopy«
- Título de la tesis: Sturctural studies on ff domains by nmr spectroscopy
- Autor: Roman Bonet Figueredo
- Universidad: Autónoma de barcelona
- Fecha de lectura de la tesis: 10/09/2009
Dirección y tribunal
- Director de la tesis
- María Jesús Macías Hernández
- Tribunal
- Presidente del tribunal: miquel Pons valles
- María concepción Civera tejuca (vocal)
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