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Showing 1–4 of 4 results
Advanced filters: Author: Mark D Szczelkun Clear advanced filters

  • Li et al. show that a Lamassu defense system protects bacteria from phage infection by activating a lethal tetrameric DNA-cutting enzyme. In the absence of phages, a protein clamp holds the enzyme as an inactive monomer, preventing self-damage.

    • Yan Li
    • David W. Adams
    • Stephan Gruber
    Research
    Nature Structural & Molecular Biology
    Volume: 32, P: 2503-2516

  • Using single-molecule magnetic tweezers and biochemical methods, Naqvi et al. revealed how CRISPR–Cas12a regulates the DNA cleavage rate through a conserved stacking interaction between the R-loop and the W355 residue and the sequence of the CRISPR RNA 3′ end.

    • Mohsin M. Naqvi
    • Laura Lee
    • Mark D. Szczelkun
    ResearchOpen Access
    Nature Chemical Biology
    Volume: 18, P: 1014-1022

  • Using single-molecule and biochemical methods, Göse et al. demonstrated that the helicase-like ATPase of a Type III restriction enzyme establishes DNA sliding through a sequential series of nucleoprotein remodeling steps driven by DNA translocation.

    • Martin Göse
    • Emma E. Magill
    • Mark D. Szczelkun
    ResearchOpen Access
    Nature Chemical Biology
    Volume: 20, P: 689-698

  • Crystal structure of the Type ISP restriction enzyme−DNA complex and single-molecule studies reveal that DNA cleavage occurs through remodeling of ATPase-DNA interactions resulting in translocation of the enzyme without loop formation.

    • Mahesh K Chand
    • Neha Nirwan
    • Kayarat Saikrishnan
    Research
    Nature Chemical Biology
    Volume: 11, P: 870-877