Backbone assignment of the little finger domain of a Y-family DNA polymerase.

Biomol NMR Assign. 2011 Oct;5(2):195-8. doi:10.1007/s12104-011-9298-1. Epub 2011 Feb 20

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Sulfolobus solfataricus DNA polymerase IV (Dpo4), a prototype Y-family DNA polymerase, contains a unique little finger domain besides a catalytic core. Here, we report the chemical shift assignments for the backbone nitrogens, Î± and Î² carbons, and amide protons of the little finger domain of Dpo4. This work and our published backbone assignment for the catalytic core provide the basis for investigating the conformational dynamics of Dpo4 during catalysis using solution NMR spectroscopy.

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Backbone assignment of the little finger domain of a Y-family DNA polymerase.

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