Fernando Moreno-Herrero | Biophysical Lab

We are interested in studying dsDNA break repair and Chromosome organisation at the single molecule level using Atomic Force Microscopy, Magnetic Tweezers, Fluorescence, and standard biochemical techniques.

Welcome to the Moreno-Herrero Lab

The main interest of my group is to answer key questions in DNA-break repair, replication and Chromosome organisation using novel approaches based on single-molecule techniques. To do this, we develop our own instrumentation based on Atomic Force Microscopy imaging, single-molecule manipulation techniques such as Magnetic Tweezers combined with fluorescence, and establish strategic collaborations with research groups specialized on different biological systems. We are also interested in studying the mechanical properties of nucleic acids and their role in protein interaction. We investigate this from an experimental perspective using our single-molecule tools but also by all-atom molecular dynamics simulations.

We work at the National Center of Biotechnology (CNB), a research center part of the Spanish National Research Council (CSIC). The CNB is the largest CSIC institute with over 600 people working in a multidisciplinary environment that combines the latest technology in molecular biology, and structural and functional biology.

Check out our Openings section for opportunities to join the group to do the Master project, PhD or Postdoctoral research.

MORE ABOUT OUR LAB

MORE ABOUT ME

DNA-end processing DNA Repair

SMC proteins DNA Organization

Type III partition systems DNA Organization

ParABS partition systems DNA Organization

Rolling Circle Replication of plasmids DNA Replication

Replication initiation proteins DNA Replication

Magnetic Tweezers Techniques

Combined MT-TIRF Techniques

BioLab Techniques

Atomic Force Microscopy Techniques

MD simulations of Nucleic Acids Mechanical Properties

Mechanical Properties of nucleic acids Mechanical Properties

High-resolution AFM imaging of nucleic acids Mechanical Properties

NEWS & EVENTS

ParB dynamics and the critical role of the CTD in DNA condensation unveiled by combined force-fluorescence measurements

Bacillus subtilis ParB forms multimeric networks involving non-specific DNA binding leading to DNA condensation. Previously, we found that an excess of the free C-terminal domain (CTD) of ParB impeded DNA condensation or promoted decondensation of pre-assembled networks (Fisher et al., 2017). However, interpretation of the molecular basis for this phenomenon was complicated by our inability to uncouple protein binding from DNA condensation.

Bacillus subtilis MutS modulates RecA-mediated DNA strand exchange between divergent DNA sequences

Natural transformation contributes to acquisition and spread of antibiotic resistance and pathogenicity traits.We show that Bacillus subtilis chromosomal transformation decreased logarithmically with increased sequence divergence up to 15% in wild type (wt) cells or in cells lacking MutS2 or mismatch repair proteins (MutL, MutS or both).

DNA crookedness regulates DNA mechanical properties at short length scales

Sequence-dependent DNA conformation and flexibility play a fundamental role in the specificity of DNA-protein interactions. Here we quantify the DNA crookedness: a sequence-dependent deformation of DNA that consists of periodic bends of the base pair centers chain.

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