Our laboratory is interested in understanding how macromolecular machines control the flow of genetic information and modulate genome integrity. One of our research aims is to investigate the molecular mechanisms that regulate horizontal gene transfer. Transposable elements often depend on the assembly of large and dynamic multisubunit complexes to prevent spurious double-strand breaks and promote efficient DNA transposition. Our group combines cryo-electron microscopy, x-ray crystallography, together with biochemical and functional assays, to develop atomic-level models to explain how these elements disseminate antibiotic resistance genes, modify gene expression, and generate genomic instability.
Arias-Palomo E*, Puri N, O'Shea Murray VL, Yan Q, Berger JM*. . Physical Basis for the Loading of a Bacterial Replicative Helicase onto DNA. Mol Cell. 2019 Apr 4;74(1):173-184.
Arias-Palomo E, Berger JM. . An Atypical AAA+ ATPase Assembly Controls Efficient Transposition through DNA Remodeling and Transposase Recruitment. Cell. Aug 13;162(4):860-71.
Arias-Palomo E, O'Shea VL, Hood IV, Berger JM. . The bacterial DnaC helicase loader is a DnaB ring breaker. Cell. Apr 11;153(2):438-48
Strycharska MS, Arias-Palomo E, Lyubimov AY, Erzberger JP, O'Shea VL, Bustamante CJ, Berger JM. . Nucleotide and partner-protein control of bacterial replicative helicase structure and function. Mol Cell. Dec 26;52(6):844-54
- Unraveling the molecular and structural mechanisms of ATP-dependent transposition. BFU2017-89143-P. MINECO. 2018-2020.
- “SUBVENCIONES A LA CONTRATACION DE DOCTORES POR CENTROS DE I+D. RAMON Y CAJAL 2015”. Spanish Ministry of Economy and Competitiveness (MINECO)