• Jan 2023 - Present

• Jul 2022 - Dec 2022

• Jun 2022 - Dec 2022

Maria Falkenberg lab

• Oct 2017 - May 2022

Claes Gustafsson labThe laboratory investigates various aspects of mitochondrial molecular genetics. A major focus of our work is mitochondrial replication and transcription and how this process is regulated in response to the overall respiratory needs of the eukaryotic cell. Much of the work is performed using in vitro biochemistry and a reconstituted system for mammalian mtDNA replication and transcription. My PhD work has mainly focused on LON protease. We have discovered that LONP1 degrades mitochondrial polymerase gamma A, the replicative polymerase subunit in mitochondria, which explains the phenotype of several relevant disease-mutations found in patients. Using in vitro assays and cryoEM, we have also shedded light into how this protease recognise its substrates and how it is directly involved in mitochondrial gene expression. I have also had the chance to analyse several patients mutations in LONP1, adding valuable information from a mechanistic and in vitro perspective, complementing the clinical data.I have also had the opportunity to do my PhD as a Marie Curie ITN fellow, which has granted me the opportunity to meet and collaborate with 14 young researchers and 14 Principal Investigators around Europe under a framework of conferences, courses and other activities which have allowed me to get extensive training in many other areas apart from science. Check the details in the link below! Show less

Structural characterization of complexes involved in the regulation of the bacterial RNA polymerase

• Feb 2017 - Jun 2017

Master Thesis in Carlos-Fernández-Tornero lab Project: "Structural characterization of multiproteic complexes implied in the regulation of the bacterial RNA polymerase": The regulation of the bacterial RNA polymerase is important to its function and studying it can help to understand the whole process. The structural characterization of multiprotein complexes formed in the transcription can help us to deep into its function. The parD toxin-antitoxin system formed by proteins Kid and Kis is involved in the survival and maintenance of plasmid R1. In addition to other maintenance systems, the plasmid R1 survives at the expense of the bacterial cell. Kis and Kid can bind themselves and oligomerize, binding to their own promoter, thus regulating its own synthesis (they are attached to the promotor, the RNA polymerase is not able to start the transcription). Using electron microscopy, the objective of the project is to try to isolate and characterize the potential ternary complex formed by RNA polymerase, KisKid and the DNA fragment of these proteins. The techniques carried out in the project are: purification of proteins and recombinant protein complexes, biochemical binding studies, size-exclusion chromatography, electron microscope grids preparation, electron microscopy data collection and 3D-image processing. Show less

Membrane protein interactions through the holo-translocon machinery

• May 2016 - Aug 2016

I worked in Ian Collinson's lab in order to prepare my TFG (End of degree project/Bachelor thesis). Here it is a summary of the project and the different techniques used: The ubiquitous Sec-machinery provides the major pathway for protein-secretion and membrane protein insertion. In bacteria, the Sec-translocon (SecYEG) associates with ancillary membrane proteins, SecDF-YajC and YidC, forming a complex known as the holo-translocon (HTL), capable of post-translational protein secretion and co-translational membrane protein insertion. This knowledge is applied to perform in vitro cell-free membrane protein synthesis/translocation in presence of vesicles containing HTL. The passage of an inserting membrane protein is monitored through the HTL by the incorporation of non-native amino acids, with photo-active cross-linker properties, in the nascent membrane protein by genetic code reprogramming, a novel synthetic biology technique. Crosslinked products generated by these experiments are identified by Western Blotting and/or by Mass Spectroscopy. This approach is also performed in vivo experiments in E. coli live cells. Recent results in the lab have revealed that, in contrast to the prevailing view, YidC alone is less competent at membrane protein insertion, folding, and assembly, by comparison with the holo-translocon. Using the cell-free in vitro translation/insertion approach, we compare biochemically the different assembly states in vesicles of the subunit F(c) of the protein ATP synthase by the HTL, SecYEG and YidC and try to isolate these oligomeric species by chromatographic techniques. Show less

Research Internship

• Jun 2015 - Jul 2015

"Biología de Membranas y reparación axonal"​ lab internship in the project "Membrane neuraminidase Neu3 and carbohydrate-binding protein Galectin-4 role in axon growth, myelination and regeneration". Biochemical analysis of proteins (Western Blot), membrane fractions separation in sacarose gradient by ultracentrifugation, primary culture of the nervous system cells (neurons, astrocytes, oligodendrocytes), inmunohistochemical staining, microscopy (fluorescence and confocal), handling and care of Wistar rats. Show less

Clinical Laboratory Assistant

• Aug 2014 - Aug 2014

Participation and collaboration in the areas of Clinical Analysis and Microbiology. Participation and collaboration in the areas of Clinical Analysis and Microbiology.