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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Nature communications

Topoisomerase I (TOP1) dynamics: conformational transition from open to closed states.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nature communications - 10 Jan 2022

Takahashi DT, Gadelle D, Agama K, Kiselev E, Zhang H, Yab E, Petrella S, Forterre P, Pommier Y, Mayer C,

Link to Pubmed [PMID] – 35013228

Link to DOI – 10.1038/s41467-021-27686-7

Nat Commun 2022 01; 13(1): 59

Eukaryotic topoisomerases I (TOP1) are ubiquitous enzymes removing DNA torsional stress. However, there is little data concerning the three-dimensional structure of TOP1 in the absence of DNA, nor how the DNA molecule can enter/exit its closed conformation. Here, we solved the structure of thermostable archaeal Caldiarchaeum subterraneum CsTOP1 in an apo-form. The enzyme displays an open conformation resulting from one substantial rotation between the capping (CAP) and the catalytic (CAT) modules. The junction between these two modules is a five-residue loop, the hinge, whose flexibility permits the opening/closing of the enzyme and the entry of DNA. We identified a highly conserved tyrosine near the hinge as mediating the transition from the open to closed conformation upon DNA binding. Directed mutagenesis confirmed the importance of the hinge flexibility, and linked the enzyme dynamics with sensitivity to camptothecin, a TOP1 inhibitor targeting the TOP1 enzyme catalytic site in the closed conformation.

https://pubmed.ncbi.nlm.nih.gov/35013228