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Structure-fonction of nucleoproteic complexes of DNA topoisomerases

Structure-fonction of nucleoproteic complexes of DNA topoisomerases

SUBGROUP LEADER

Valerie LAMOUR

We investigate the regulation of DNA topology by DNA topoisomerases that form large nucleoprotein complexes and catalyze relaxation of DNA entanglements in bacteria and human cells.

Our project is aiming at the functional and structural studies of DNA topoisomerase cellular complexes targeted by therapeutic compounds used in cancer and anti-bacterial therapies. The main goal of this study is to identify and study the structure/function of Topoisomerase-associated complexes targeted by drugs through a combination of functional and structural approaches.

Current projects

- Structural analysis of chromatin complexes of human DNA topoisomerases (TopoII).

- Impact of post-translational modifications on the catalytic activities of the human Topo II isoforms.

- Structure/function analysis of nucleoproteic complexes of the bacterial DNA gyrase. Check our latest article in Science 2024 : here

- Interplay of DNA topology and transcription (in collaboration with the team of Albert Weixlbaumer at IGBMC).

Check our latest article in Nature Structural and Molecular Biology 2025: here

Awards and recognitions

Check our latest article published in Science, April 12th 2024 !

https://www.science.org/stoken/author-tokens/ST-1818/full

 

DNA gyrase captures a positive crossover prior to taking action.

DNA gyrase captures a positive crossover prior to taking action.

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