Mn²⁺-induced structural flexibility enhances the entire catalytic cycle and the cleavage of mismatches in prokaryotic argonaute proteins.

ABSTRACT: Prokaryotic Argonaute (pAgo) proteins, a class of DNA/RNA-guided programmable endonucleases, have been extensively utilized in nucleic acid-based biosensors. The specific binding and cleavage of nucleic acids by pAgo proteins, which are crucial processes for their applications, are dependent on the presence of Mn²⁺ bound in the pockets, as verified through X-ray crystallography. However, a comprehensive understanding of how dissociated Mn²⁺ in the solvent affects the catalytic cycle, and its underlying regulatory role in this structure-function relationship, remains underdetermined. By combining experimental and computational methods, this study reveals that unbound Mn²⁺ in solution enhances the flexibility of diverse pAgo proteins. This increase in flexibi

SUBMITTER: Zheng L 

PROVIDER: S-EPMC11023060 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature