Protein NMR group: RNA binding proteins in RNA metabolism
Jose M. Pérez Cañadillas (Madrid 1970) is graduate in Organic Chemistry by Universidad Complutense de Madrid (1993) and PhD in Physical Chemistry by the Universidad Autonoma de Madrid (1999). His PhD thesis was supervised by Prof. Marta Bruix Bayés at the Institute of Structure of Matter (CSIC) and was focused in the structure, dynamics and electrostatics of a-sarcin, an important fugal ribotoxin with promising therapeutic applications in human health. The NMR structure of this 17 KDa protein represented at that time a formidable challenge and remained for some time as one of the largest structures being determined by NMR in Spain.
After his PhD work he moved to Cambridge (UK) for a 5-year Post Doc stage at the prestigious Medical Research Council. Laboratory of Molecular Biology and MRC:Centre for Protein Engineering. During this period, he studied several RNA/DNA binding proteins involved in mRNA processing (CstF64 and Hrp1) and cancer (p53) in the labs of Prof Gabriele Varani and Sir Prof. Alan Fersht, two world figures of structural and chemical biology. During this period he obtained two highly-competitive long-term fellowships (EMBO and Marie Curie) and a Cancer Research UK contract and published a number of articles including two EMBO J (one as single-authors) and two PNAS.
In 2005 he returned to Spain as “Ramón y Cajal” researcher to the protein NMR group in the Rocasolano Physical Chemistry Institute (IQFR-CSIC), was certified as I3 researcher two years later and obtained a permanent “Científico Titular” position in 2008.
Dr Pérez-Cañadillas is expert in protein NMR, protein chemistry, biophysics and protein-nucleic acids interactions. He has published 26 articles, 25 protein and complex structures in the PDB, supervised 2 PhD thesis (one expected in 2019) and participated several research projects (3 as PI).
Our group studies structures of RNA binding proteins (RBPs) and their interactions with nucleic acids and proteins as a mean to obtain mechanistic insight into the biological function of these type of proteins. A large number of RBPs has a typical domain architecture combining one or several small folded RNA binding domains (RBDs) with large intrinsically disordered domains (IDD). Both types of elements are highly suitable to study by NMR – our main structural biology tool – in particular the IDD. We study several proteins involved in different stages of transcription like Gbp2/Hrb1, involved in elongation and THO recruitment; transcription terminator factors like Nrd1, Nab3, Hrp1 or CstF64; and mRNA export factors like Nab2. The second area of research is translation regulation and post-transcriptional control. We study biomolecular assemble of eIF4G, Pab1, Pub1 and RNA, with particular attention to the role of IDDs of these proteins in the regulation of the stress response. In addition to NMR, we use a battery of biophysical (ITC, DLS, MALS, FA) and structural (X-ray) techniques ourselves or in close collaboration with expert groups to further characterize our systems. This multidisciplinary approach is completed with in vivo studies through collaboration with expert groups in yeast genetics and cell biology.