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**Huecas, S., Canosa-Valls, A.J., Araújo-Bazán, L., Ruiz, F.M., Laurents, D.V., Fernández-Tornero, C., Andreu, J.M. [2020].** Nucleotide-induced folding of cell division protein FtsZ from Staphylococcus aureus. FEBS Journal. 287:4048-4067.

González-Corrochano, R., Ruiz, F.M., Taylor, N.M.I., Huecas, S., Drakulic, S., Spínola-Amilibia, M., Fernández-Tornero, C. [2020]. The crystal structure of human XPG, the xeroderma pigmentosum group G endonuclease, provides insight into nucleotide excision DNA repair. Nucleic acids research. 48:9943-9958.

Darrière, T., Pilsl, M., Sarthou, M.-K., Chauvier, A., Genty, T., Audibert, S., Dez, C., Léger-Silvestre, I., Normand, C., Henras, A.K., Kwapisz, M., Calvo, O., Fernandez-Tornero, C., Tschochner, H., Gadal, O. [2019]. Genetic analyses led to the discovery of a super-active mutant of the RNA polymerase I. PLoS Genetics. 15:e1008157.

Fernández-Tornero, C. [2018]. RNA polymerase I activation and hibernation: unique mechanisms for unique genes. Transcription. 9:248-254.

Sanz-Murillo, M., Xu, J., Belogurov, G.A., Calvo, O., Gil-Carton, D., Moreno-Morcillo, M., Wang, D., Fernández-Tornero, C. [2018]. Structural basis of RNA polymerase I stalling at UV light-induced DNA damage. Proceedings of the National Academy of Sciences of the United States of America. 115:8972-8977.

Garavís, M., González-Polo, N., Allepuz-Fuster, P., Louro, J.A., Fernández-Tornero, C., Calvo, O. [2017]. Sub1 contacts the RNA polymerase II stalk to modulate mRNA synthesis. Nucleic Acids Research. 45:2458-2471.

Torreira, E., Louro, J.A., Pazos, I., González-Polo, N., Gil-Carton, D., Duran, A.G., Tosi, S., Gallego, O., Calvo, O., Fernández-Tornero, C. [2017]. The dynamic assembly of distinct RNA polymerase i complexes modulates rDNA transcription. eLife. 6:e20832.

Canales, Á., Rösinger, M., Sastre, J., Felli, I.C., Jiménez-Barbero, J., Giménez-Gallego, G., Fernández-Tornero, C. [2017]. Hidden α-helical propensity segments within disordered regions of the transcriptional activator CHOP. PLoS ONE. 12:e0189171.

Moreno-Morcillo M, Taylor NM, Gruene T, Legrand P, Rashid UJ, Ruiz FM, Steuerwald U, Müller CW, Fernández-Tornero C [2014]. Solving the RNA polymerase I structural puzzle. Acta Cryst. D70:2570-2582

Basu RS, Warner BA, Molodtsov V, Pupov D, Esyunina D, Fernández-Tornero C, Kulbachinskiy A, Murakami KS [2014]. Structural basis of transcription initiation by bacterial RNA polymerase holoenzyme. J. Biol. Chem. 289:24549-24559

**Torreira E, Seabra AR, Marriott H, Zhou M, Llorca O, Robinson CV, Carvalho HG, Fernández-Tornero C, Pereira PJ [2014].** The structures of cytosolic and plastid-located glutamine synthetases from Medicago truncatula reveal a common and dynamic architecture. Acta Cryst. D70:981-993

**Fernández-Tornero C, Moreno-Morcillo M, Rashid UJ, Taylor NM, Ruiz FM, Gruene T, Legrand P, Steuerwald U, Müller CW [2013].** Crystal structure of the 14-subunit RNA polymerase I. Nature 502:644-649

Taylor NM, Glatt S, Hennrich ML, von Scheven G, Grötsch H, Fernández-Tornero C, Rybin V, Gavin AC, Kolb P, Müller CW [2013]. Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC. J. Biol. Chem. 288:15110-15120

**Fernández-Tornero C, Böttcher B, Rashid UJ, Müller CW [2011].** Analyzing RNA polymerase III by electron cryomicroscopy. RNA Biol. 8:760-765

Lane LA, Fernández-Tornero C, Zhou M, Morgner N, Ptchelkine D, Steuerwald U, Politis A, Lindner D, Gvozdenovic J, Gavin AC, Müller CW, Robinson CV [2011]. Mass spectrometry reveals stable modules in holo and apo RNA polymerases I and III. Structure 19:90-100

Gallego O, Betts MJ, Gvozdenovic-Jeremic J, Maeda K, Matetzki C, Aguilar-Gurrieri C, Beltran-Alvarez P, Bonn S, Fernández-Tornero C, Jensen LJ, Kuhn M, Trott J, Rybin V, Müller CW, Bork P, Kaksonen M, Russell RB, Gavin AC [2010]. A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae. Mol. Syst. Biol. 6:430

Fernández-Tornero C, Böttcher B, Rashid UJ, Steuerwald U, Flörchinger B, Devos DP, Lindner D, Müller CW [2010]. Conformational flexibility of RNA polymerase III during transcriptional elongation. EMBO J. 29:3762-3772

Huecas, S., Canosa-Valls, A.J., Araújo-Bazán, L., Ruiz, F.M., Laurents, D.V., Fernández-Tornero, C.*, Andreu, J.M.* [2020]. Nucleotide-induced folding of cell division protein FtsZ from Staphylococcus aureus. FEBS Journal. 287:4048-4067.

Fernández-Tornero, C. [2018]. RNA polymerase I activation and hibernation: unique mechanisms for unique genes. Transcription. 9:248-254.

Garavís, M., González-Polo, N., Allepuz-Fuster, P., Louro, J.A., Fernández-Tornero, C., Calvo, O. [2017]. Sub1 contacts the RNA polymerase II stalk to modulate mRNA synthesis. Nucleic Acids Research. 45:2458-2471.

Torreira, E., Louro, J.A., Pazos, I., González-Polo, N., Gil-Carton, D., Duran, A.G., Tosi, S., Gallego, O., Calvo, O., Fernández-Tornero, C. [2017]. The dynamic assembly of distinct RNA polymerase i complexes modulates rDNA transcription. eLife. 6:e20832.

Canales, Á., Rösinger, M., Sastre, J., Felli, I.C., Jiménez-Barbero, J., Giménez-Gallego, G., Fernández-Tornero, C. [2017]. Hidden α-helical propensity segments within disordered regions of the transcriptional activator CHOP. PLoS ONE. 12:e0189171.

Moreno-Morcillo M, Taylor NM, Gruene T, Legrand P, Rashid UJ, Ruiz FM, Steuerwald U, Müller CW, Fernández-Tornero C [2014]. Solving the RNA polymerase I structural puzzle. Acta Cryst. D70:2570-2582

Basu RS, Warner BA, Molodtsov V, Pupov D, Esyunina D, Fernández-Tornero C, Kulbachinskiy A, Murakami KS [2014]. Structural basis of transcription initiation by bacterial RNA polymerase holoenzyme. J. Biol. Chem. 289:24549-24559

Torreira E, Seabra AR, Marriott H, Zhou M, Llorca O, Robinson CV, Carvalho HG, Fernández-Tornero C*, Pereira PJ* [2014]. The structures of cytosolic and plastid-located glutamine synthetases from Medicago truncatula reveal a common and dynamic architecture. Acta Cryst. D70:981-993

Fernández-Tornero C*, Moreno-Morcillo M, Rashid UJ, Taylor NM, Ruiz FM, Gruene T, Legrand P, Steuerwald U, Müller CW* [2013]. Crystal structure of the 14-subunit RNA polymerase I. Nature 502:644-649

Taylor NM, Glatt S, Hennrich ML, von Scheven G, Grötsch H, Fernández-Tornero C, Rybin V, Gavin AC, Kolb P, Müller CW [2013]. Structural and functional characterization of a phosphatase domain within yeast general transcription factor IIIC. J. Biol. Chem. 288:15110-15120

Fernández-Tornero C*, Böttcher B, Rashid UJ, Müller CW* [2011]. Analyzing RNA polymerase III by electron cryomicroscopy. RNA Biol. 8:760-765

Lane LA, Fernández-Tornero C, Zhou M, Morgner N, Ptchelkine D, Steuerwald U, Politis A, Lindner D, Gvozdenovic J, Gavin AC, Müller CW, Robinson CV [2011]. Mass spectrometry reveals stable modules in holo and apo RNA polymerases I and III. Structure 19:90-100

Fernández-Tornero C, Böttcher B, Rashid UJ, Steuerwald U, Flörchinger B, Devos DP, Lindner D, Müller CW [2010]. Conformational flexibility of RNA polymerase III during transcriptional elongation. EMBO J. 29:3762-3772

**Huecas, S., Canosa-Valls, A.J., Araújo-Bazán, L., Ruiz, F.M., Laurents, D.V., Fernández-Tornero, C., Andreu, J.M. [2020].** Nucleotide-induced folding of cell division protein FtsZ from Staphylococcus aureus. FEBS Journal. 287:4048-4067.

**Torreira E, Seabra AR, Marriott H, Zhou M, Llorca O, Robinson CV, Carvalho HG, Fernández-Tornero C, Pereira PJ [2014].** The structures of cytosolic and plastid-located glutamine synthetases from Medicago truncatula reveal a common and dynamic architecture. Acta Cryst. D70:981-993

**Fernández-Tornero C, Moreno-Morcillo M, Rashid UJ, Taylor NM, Ruiz FM, Gruene T, Legrand P, Steuerwald U, Müller CW [2013].** Crystal structure of the 14-subunit RNA polymerase I. Nature 502:644-649

**Fernández-Tornero C, Böttcher B, Rashid UJ, Müller CW [2011].** Analyzing RNA polymerase III by electron cryomicroscopy. RNA Biol. 8:760-765