GROUPS
Structure of Macromolecular Assemblies
Carlos Fernández Tornero > ORCID 0000-0001-5097-731X
Web https://www.cib.csic.es/research/structural-and-chemical-biology/structure-macromolecular-assemblies
Phone +34 91 837 31 12 (ext. 4327)
Mail cftornero@cib.csic.es
Carlos Fernández Tornero is a structural biologist who combines electron cryomicroscopy (cryo-EM) and X-ray crystallography to study cellular machines. He currently leads the laboratory of ‘Structure of Macromolecular Assemblies’ at the Margarita Salas Center for Biological Research (CIB) of the Spanish National Research Council (CSIC).
He completed a PhD on X-ray crystallography of bacterial virulence factors at CIB-CSIC, complemented with a stay with Nobel laureate Prof. Robert Huber. His PhD thesis received the Josep Tormo and Juan Abelló Pascual I awards. In 2002 he moved to Christoph Müller’s laboratory at EMBL-Grenoble with an EMBO Long Term fellowship. He combined cryo-EM, trained by Bettina Böttcher and Guy Schoëhn, with X-ray crystallography to study macromolecular assemblies involved in gene expression. In 2007 he became Staff Scientist at EMBL-Heidelberg, where he pursued cryo-EM studies of transcription complexes.
At the end of 2009 he joined CIB-CSIC and started an independent research group in 2010. The group initially focused on the X-ray structure of RNA polymerase I in its inactive state (Nature, 2013), then applied cryo-EM to study the enzyme activation process (eLife , 2017). The research team also uncovered the mechanism of UV light-induced DNA lesions detection by this enzyme (PNAS, 2018) and obtained the structure of the DNA repair endonuclease XPG in complex with DNA (NAR, 2020).
Carlos Fernández-Tornero has obtained competitive funding from the Spanish Ministry of Science, CSIC, Agence National de la Recherche (France), Ramón Areces Foundation and through collaboration contracts with biotech companies such as PharmaMar. His research is supported by a network of national and international collaborators, including researchers from the USA, the UK, France and Portugal. He was awarded the ‘Madrid Research Scientist’ distinction from CSIC in 2015. Since 2018 he coordinates the ‘Protein Structure and Function’ Group of the SEBBM. In 2019 he was nominated by the CIB director as member of the CIB Scientific Advisory Committee.
MEMBERS
- Sonia Huecas Gayo
- Federico M. Ruiz
- Adrián Plaza Pegueroles
- Phong Quoc Nguyen
RESEARCH
Our group aims to unveil the structure of cellular machines to gain mechanistic insight into macromolecular function and assist the development of biomedical applications. For this, we use electron cryomicroscopy (cryo-EM) and X-ray crystallography, both providing information to atomic resolution, combined with other biophysical and biochemical techniques. This integrative methodology is applied to study essential cell processes such as genome transcription and DNA repair.
Genome transcription. The transfer of genetic information encoded in DNA is the main determinant of gene expression. Alterations in this process have significant impact on cell homeostasis and are directly related to disease. RNA polymerases transcribe the genetic information from DNA to RNA, by catalyzing the addition of nucleotides that are complementary to the DNA template strand. Eukaryotes require three different RNA polymerases, each transcribing a specific set of genes. We focus on the study of RNA polymerase I and various transcription factors that regulate gene expression.
DNA damage detection and repair. DNA damage threatens cell life and must be repaired to maintain genome integrity. Transcription is particularly sensitive to DNA damage and, hence, it is linked to DNA repair. Different lesions induce RNA polymerase stalling, which activates the recruitment of DNA repair factors, including endonucleases XPF and XPG to eliminate the lesion. Alterations in these repair factors associate with genetic disorders such as xeroderma pigmentosum and Cockayne syndrome. We focus on the study of lesion detection by RNA polymerases and damaged DNA elimination by XPG.