Abstract
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, α and β 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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Acknowledgments
This work was supported by the National Science Foundation grant MCB-0960961 (to Z. S.) and the National Institute of Health Grant ES009127 (to Z. S.). J.D.F. was supported by a Post-doctoral Fellowship from a Pulmonary National Institutes of Health Training Grant 5T32HL007946 (PI: Mark D. Wewers). The authors want to thank Dr. Chunhua Yuan for his helpful suggestions.
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Dejian Ma and Jason D. Fowler contributed equally.
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Ma, D., Fowler, J.D. & Suo, Z. Backbone assignment of the little finger domain of a Y-family DNA polymerase. Biomol NMR Assign 5, 195–198 (2011). https://doi.org/10.1007/s12104-011-9298-1
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DOI: https://doi.org/10.1007/s12104-011-9298-1