The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase

Thomas Wiegand, Riccardo Cadalbert, Denis Lacabanne, Joanna Timmins, Laurent Terradot, Anja Böckmann () and Beat H. Meier ()
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Thomas Wiegand: Physical Chemistry, ETH Zurich
Riccardo Cadalbert: Physical Chemistry, ETH Zurich
Denis Lacabanne: Physical Chemistry, ETH Zurich
Joanna Timmins: Univ. Grenoble Alpes, CNRS, CEA, CNRS, IBS
Laurent Terradot: Molecular Microbiology and Structural Biochemistry, Labex Ecofect, UMR 5086 CNRS/Université de Lyon
Anja Böckmann: Molecular Microbiology and Structural Biochemistry, Labex Ecofect, UMR 5086 CNRS/Université de Lyon
Beat H. Meier: Physical Chemistry, ETH Zurich

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: Abstract DnaB helicases are motor proteins that couple ATP-hydrolysis to the loading of the protein onto DNA at the replication fork and to translocation along DNA to separate double-stranded DNA into single strands during replication. Using a network of conformational states, arrested by nucleotide mimics, we herein characterize the reaction coordinates for ATP hydrolysis, DNA loading and DNA translocation using solid-state NMR spectroscopy. AMP-PCP is used as pre-hydrolytic, ADP:AlF4− as transition state, and ADP as post-hydrolytic ATP mimic. 31P and 13C NMR spectra reveal conformational and dynamic responses to ATP hydrolysis and the resulting DNA loading and translocation with single amino-acid resolution. This allows us to identify residues guiding the DNA translocation process and to explain the high binding affinities for DNA observed for ADP:AlF4−, which turns out to be optimally preconfigured to bind DNA.

Date: 2019
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DOI: 10.1038/s41467-018-07968-3

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