Dr. Fernando Moro Pérez
Unidad de Biofísica (CSIC/UPV-EHU) y Departamento de Bioquímica y Biología Molecular, Facultad de Ciencia y Tecnología, Universidad del País Vasco (UPV/EHU)
Chaperoning protein aggregates: the disaggregase machinery
I obtained my degree in Chemistry in 1990 at the University of the Basque Country UPV/EHU. Between 1991-1996, I worked in the group of Professor Felix Goñi, characterizing a membrane protein from the conjugative plasmid R388 that encodes a type IV secretion system of bacterial DNA. After obtaining my PhD in Biochemistry in 1996, I joined the laboratory of Professor Walter Neupert in the Ludwig Maximilians Universität in Munich, as a Marie Curie postdoctoral. My work focused on characterization of the protein translocation machinery in the mitochondrial inner membrane. One of the essential components of this machinery is a chaperone; the mitochondrial Hsp70 that builds the molecular motor that pulls protein precursors across the membrane. Hsp70 proteins, as well as other chaperones, are required to maintain protein homeostasis in the cells. This turned my scientific interest into the study of the mechanism of molecular chaperones. In 2001, I returned to the UPV/EHU and joined the group of Professor Arturo Muga as a postdoctoral researcher until 2007, studying the chaperone system formed by DnaK, the main bacterial Hsp70, and its cochaperones DnaJ (Hsp40) and GrpE. In 2007, I obtained a Ramón y Cajal research position, and in 2011 a permanent researcher position in UPV/EHU. The line of research developed over these years has continued the characterization of the functional mechanism of bacterial and yeast Hsp70 and Hsp40 chaperones, and their association to Hsp100 disaggregases that allows solubilization and refolding of proteins aggregates formed after exposure to stress conditions. Currently, I have started a new line of research to study the reactivation of protein aggregates by the human chaperones Hsc70 (Hsp70), Hdj1 (Hsp40) and Apg2 (Hsp110).