As a Principal Investigator (PI), I run a research group at the Instituto de Biomedicina y Biotecnología de Cantabria (IBBTEC), called "Molecular motors in Nanobiotecnología" (https://web.unican.es/ibbtec/Paginas/Groups/Cabezon.aspx). I am also Deputy Director of the IBBTEC since 2016 and Professor at the University of Cantabria since 2009.
B.Sc & M.Sc in Biochemistry (Academic Achievement Award), Universidad del País Vasco (UPV/EHU), and Ph.D. in Molecular Biology, Universidad de Cantabria (UC). In 1997, I joined John Walker´s group at the LMB (Medical Research Council, Cambridge, UK), just a few months before he got the Nobel Prize in Chemistry. I was supported by an EMBO Postdoctoral Fellowship and a Marie Curie Research Grant during the first years and then I continued my work as a Research Associate, until 2002. My work was focused on the inhibitor protein of mitochondrial F-ATPase. In 2002, I came back to Spain as a group leader with a Ramón & Cajal contract and I became Associate Professor in 2005. Since then, my work has been focused on molecular motors. I seek to understand their mechanism by using biochemical and structural approaches, with a special interest in recent advances in nanobiotechnology. In my scientific career, I have 32 publications, many of them in high impact scientific journals, such as Nature, EMBO Journal, PNAs, Nature Structural Biology, etc. as well as a patent. My research work has been funded by several Research Grants from public competitive calls and I have supervised six Ph.D students. As management tasks, I am a member of some international Committees, such as Faculty of 1000 and, in addition to the Deputy Direction of the IBBTEC, I have also been selected as a member of several committees at the UC, such as The University Research Committee, The Doctoral Program Committee or The PhD Awards Committee.
Molecular Motors in Nanobiotechnology
Research interests
Funding
Título del proyecto: “Aplicaciones biomédicas y biotecnológicas de motores moleculares implicados en la transferencia de ADN y proteínas a través de membranas biológicas”
Entidad financiadora: Ministerio de Economía, Industria y Competitividad
Referencia: BFU2016-78521-R
Duración:desde 30/12/2016 hasta 29/12/2019
Investigadores responsables: Dr. Elena Cabezón e Ignacio Arechaga
Título del proyecto: "Aplicación de un motor que transloca ssDNA en plataformas de secuenciación de tercera generación"
Entidad financiadora: Ministerio de Economía y Competitividad
Referencia: BFU2014-61823-EXP
Duración: desde 01/09/2015 hasta 31/08/2017
Investigador responsable: Dr. Elena Cabezón
Título del proyecto: "Morfogénesis de membranas bacterianas y mitocondriales: en busca del eslabón perdido"
Entidad financiadora: Ministerio de Economía y Competitividad
Referencia : BFU2013_49486-EXP
Duración: 2014-2016
Investigador responsable: Dr. Ignacio Arechaga
Título del proyecto: "Mecanismos moleculares y evolutivos en motores moleculares que translocan ADN y proteínas"
Entidad financiadora: Ministerio de Economía y Competitividad
Referencia: BFU2011-22874
Duración:desde 01/01/2012 hasta 31/12/2015
Investigador responsable: Dr. Elena Cabezón
Nanopore sensing reveals a preferential pathway for the co-translocational unfolding of a conjugative relaxase-DNA complex
Valenzuela-Gómez F, Arechaga I, Cabezón E.
Abstract
Bacterial conjugation is the main mechanism for the dissemination of antibiotic resistance genes. A single DNA strand of the conjugative plasmid is transferred across bacterial membranes covalently bound to a large multi-domain protein, named relaxase, which must be unfolded to traverse the secretion channel. Two tyrosine residues of the relaxase (Y18 and Y26 in relaxase TrwC) play an important role in the processing of conjugative DNA. We have used nanopore technology to uncover the unfolding states that take place during translocation of the relaxase-DNA complex. We observed that the relaxase unfolding pathway depends on the tyrosine residue involved in conjugative DNA binding. Transfer of the nucleoprotein complex is faster when DNA is bound to residue Y18. This is the first time in which a protein-DNA complex that is naturally translocated through bacterial membranes has been analyzed by nanopore sensing, opening new horizons to apply this technology to study protein secretion.
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Monitoring Bacterial Conjugation by Optical Microscopy
Carranza G, Menguiano T, Valenzuela-Gómez F, García-Cazorla Y, Cabezón E, Arechaga I.
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Conjugation inhibitors compete with palmitic acid for binding to the conjugative traffic ATPase TrwD, providing a mechanism to inhibit bacterial conjugation
García-Cazorla Y, Getino M, Sanabria-Ríos DJ, Carballeira NM, de la Cruz F, Arechaga I, Cabezón E
J Biol Chem. 2018 Oct 26;293(43):16923-16930.
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Conjugation Inhibitors and Their Potential Use to Prevent Dissemination of Antibiotic Resistance Genes in Bacteria
Cabezón E, de la Cruz F, Arechaga I.
Front Microbiol. 2017 Nov 30;8:2329. doi: 10.3389/fmicb.2017.02329. eCollection 2017.
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Fludarabine resistance mediated by aminoglycoside-3'-phosphotransferase-IIa and the structurally related eukaryotic cAMP-dependent protein kinase
Sánchez-Carrera D, Bravo-Navas S, Cabezón E, Arechaga I, Cabezas M, Yáñez L, Pipaón C
FASEB J. 2017 Jul;31(7):3007-3017. doi: 10.1096/fj.201601245R. Epub 2017 Apr 3.
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Substrate translocation involves specific lysine residues of the central channel of the conjugative coupling protein TrwB.
Larrea D, de Paz HD, Matilla I, Guzmán-Herrador DL, Lasso G, de la Cruz F, Cabezón E, Llosa M. ol Genet Genomics. 2017 Jun 8. doi: 10.1007/s00438-017-1331-3. (Epub ahead of print)
[pubmed]
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Type IV traffic ATPase TrwD as molecular target to inhibit bacterial conjugation.
Ripoll-Rozada J, García-Cazorla Y, Getino M, Machón C, Sanabria-Ríos D, de la Cruz F, Cabezón E, Arechaga I. Mol Microbiol. 2016 Jun;100(5):912-21. doi: 10.1111/mmi.13359.
[pubmed]
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Type IV traffic ATPase TrwD as molecular target to inhibit bacterial conjugation.
Ripoll-Rozada J, García-Cazorla Y, Getino M, Machón C, Sanabria-Ríos D, de la Cruz F, Cabezón E, Arechaga I. Mol Microbiol. 2016 Jun;100(5):912-21. doi: 10.1111/mmi.13359. Epub 2016 Mar 22.
[PubMed]
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Towards an integrated model of bacterial conjugation.
Cabezón E, Ripoll-Rozada J, Peña A, de la Cruz F, Arechaga I. FEMS Microbiol Rev. Vol.39:81-95. doi: 10.1111/1574-6976.12085.
[pubmed]
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Functional interactions of VirB11 traffic ATPases with VirB4 and VirD4 molecular motors in type IV secretion systems.
Ripoll-Rozada J, Zunzunegui S, de la Cruz F, Arechaga I, Cabezón E. J Bacteriol. 2013 Sep;195(18):4195-201. doi: 10.1128/JB.00437-13.
[pubmed]
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The hexameric structure of a conjugative VirB4 protein ATPase provides new insights for a functional and phylogenetic relationship with DNA translocases.
Peña A, Martín-Benito J, Valpuesta JM, Carrascosa JL, de la Cruz F, Cabezón E*, Arechaga I*. J. Biol. Chem. 2012, 287(47), 39925-32. doi: 10.1074/jbc.M112.413849.
[pubmed]
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Regulation of the type IV secretion ATPase TrwD by magnesium: implications for the catalytic mechanism of the secretion ATPase superfamily.
Ripoll-Rozada J, Peña A, Rivas S, Moro F, de la Cruz F, Cabezón E*,Arechaga I* J. Biol. Chem. 2012, 287(21), 17408-14. DOI:10.1074/jbc.M112.357905.
[pubmed]
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Membrane-associated nanomotors form macromolecular transport.
Cabezón E*, Lanza VF, Arechaga I* Curr. Opin. Biotechnol. 2012, 23(4), 537-44. DOI:10.1016/j.copbio.2011.11.031.
[pubmed]
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Autoinhibitory regulation of TrwK, an essential VirB4 ATPase in type IV secretion systems.
Peña A, Ripoll-Rozada J, Zunzunegui S, Cabezón E, de la Cruz F, Arechaga I* J. Biol. Chem. 2011, 286(19), 17376-82. DOI:10.1074/jbc.M110.208942.
[pubmed]
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The conjugative DNA translocase TrwB is a structure specific DNA-binding protein.
Matilla I, Alfonso C, Rivas G, Bolt EL, de la Cruz F, Cabezón E* J. Biol. Chem. 2010, 285(23, 17537-44. DOI:10.1074/jbc.M109.084137.
[pubmed]
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