Timothy M. Lohman

This study compares ssDNA translocation and helicase activities of covalent dimers and monomers of E. coli UvrD, showing higher processivity and DNA unwinding in dimers.

This study identifies a conserved dimerization mechanism in SF1A UvrD-family helicases, showing that the 2B domain mediates dimerization and activation across multiple species.

This study shows that the RecB nuclease domain in E. coli RecBCD regulates DNA binding and base pair melting through allosteric effects and linker interactions.

This study reports the first structures of a dimeric UvrD-family helicase, revealing the 2B subdomain's regulatory role in dimerization and activation.

This study shows that specific dimer interactions and ATPase activity in both subunits are required for helicase activity in E. coli Rep and UvrD, with subunit communication demonstrated through Trp fluorescence.

This study shows that the nuclease domain of E. coli RecBCD affects dsDNA unwinding rates but not ssDNA translocation, suggesting the nuclease domain influences base pair melting rather than translocation.

This study shows that Mtb Ku stimulates UvrD1 monomers to unwind DNA in multiple rounds, revealing a mechanism for DNA repair activation in mycobacteria.