Ikerbasque Research Professor
Paola Fucini obtained her PhD degree in 1998, from the Ludwig-Maximilians-Universität in München, for a thesis conducted at the Max-Planck-Institute for Biochemistry, in Martinsried (Germany), under the supervision of Prof. Angelika Noegel and Tad Holak. With this first study she started her career in structural biology becoming interested in tackling the fascinating process of protein folding. During her postdoctoral studies, as a Research Associate in the group of Prof. Chris Dobson and Carol Robinson, first at the Oxford Center for Molecular Science (University of Oxford) in the period 1998-2001 and later in 2002, at the Chemical Laboratory at Cambridge University, UK, she developed an in vitro transcription/translation system for the preparation of nascent chain ribosomal complexes, suitable for Mass Spectrometry, NMR and Cryo-EM analysis. The system allowed pioneering studies on co-translational protein folding which she later pursued as an independent Group Leader at the Max-Planck-Institute for Molecular Genetics, AG Ribosomen, in Dahlem, Berlin (2002-2007). There, after acquiring further expertise in ribosome X-ray crystallography, she started to developed three main research lines, namely (i) the mode of action of antibiotics and translational factors, (ii) the process of co-translational protein folding and sorting, (iii) ribosome biogenesis. These studies, consolidated as Professor in X-ray Crystallography for RNA and Protein complexes at the Cluster of Excellence for Macromolecular Complexes at the University of Frankfurt (2007-2012), are currently continued since 2013 as Research Professor in the ideal environment offered by the Centro de Investigación Cooperativa en Biociencias, CIC bioGUNE, en Derio, Bizkaia.
Lastest Publications
2016
2015
2013
Amino acids are assembled into proteins following the genetic instructions encoded in the mRNA in a process called translation. This is primarily governed by a large macromolecular machine called the ribosome. Research in the Fucini and Connell labs focuses on understanding, at a biochemical and structural level, the molecular details of processes that regulate the ribosome at several levels including:
1) Inhibition of core ribosomal activities by antibiotics. Medically relevant antibiotics target the ribosome and inhibit its core functions to exert their anti-microbial activities. We aim to understand how these antibiotics interact with and inhibit the ribosome to improve existing drugs or develop novel antibiotics.
2) Regulation of core activities like initiation, elongation and termination by native protein factors. During protein synthesis the ribosome has several functional activates which are coordinated by specific protein factors. We aim to understand how these factors work together with the ribosome.
3) Ribosome Biosynthesis: Assembling a ribosome requires orchestrating the structural integration of more than 55 ribosomal proteins and three nucleic acid strands in Escherichia coli. This assembly process is facilitated by ribosome assembly factors and we aim to understand how these factors guide the maturation of the ribosome.
4) Co-translational folding and protein sorting. The nascent protein is synthesized in the core of the ribosome and passes through a 100Å long conduit to emerge outside the ribosome. This passage is a highly dynamic and 'personalized' event, where the ribosome and the protein chain communicate to regulate the translation and compartmentalization of the nascent protein. We aim to understand the details of this communication.
Accordingly, the groups have expertise in the preparation and structural characterization of ribosomal complexes. To provide a complete structural understanding of ribosomal functions we employ complementary structural biology methods like X-ray crystallography, NMR (Fucini Lab) and cryo-EM (Connell Lab).
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Principal Investigator
Sean Connell
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Idoia Iturrioz
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Borja Ochoa de Eribe
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Elisa de Astigarraga
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Andreas Schedlbauer
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Retina Capuni