Contrasting views of the internal dynamics of the HhaI methyltransferase target DNA reported by solution and solid-state NMR spectroscopy.
Solution and solid-state NMR have been used conjointly to probe the internal motions of a DNA dodecamer containing the recognition site for the HhaI methyltransferase. The results strongly suggest that ns-mus motions contribute to the functionally relevant dynamic properties of nucleic acids during DNA methylation.
Miller
Paul A
PA
Department of Chemistry, University of Washington, Seattle, Washington 98195, USA.
Shajani
Zahra
Z
Meints
Gary A
GA
Caplow
Dorothy
D
Goobes
Gil
G
Varani
Gabriele
G
Drobny
Gary P
GP
D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D015257:DNA-Cytosine Methylases / Q000737:chemistry* / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy
D004247:DNA; C037664:DNA modification methylase HhaI; D015257:DNA-Cytosine Methylases