Abstract
DnaE intein from Nostoc punctiforme (Npu) is one of naturally occurring split inteins, which has robust protein splicing activity. Highly efficient trans-splicing activity of NpuDnaE intein could widen various biotechnological applications. However, structural basis of the efficient protein splicing activity is poorly understood. As a first step toward better understanding of protein trans-splicing mechanism, we present the backbone and side-chain resonance assignments of a single chain variant NpuDnaE intein as determined by triple resonance experiments with [13C,15N]-labeled protein.
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Acknowledgments
The authors thank Olga Valvuk and Kimmo Pääkkönen for their contributions at the early stage of the project. This work is supported by the grants from the Academy of Finland (118385), Sigrid Jusélius Foundation, and the Biocentrum Helsinki.
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J. S. Oeemig and K. Heinämäki contributed equally to this work.
An erratum to this article can be found online at http://dx.doi.org/10.1007/s12104-012-9435-5.
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Heinämäki, K., Oeemig, J.S., Djupsjöbacka, J. et al. NMR resonance assignment of DnaE intein from Nostoc punctiforme . Biomol NMR Assign 3, 41–43 (2009). https://doi.org/10.1007/s12104-008-9137-1
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DOI: https://doi.org/10.1007/s12104-008-9137-1