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Updated: Jun 21, 2026

An Assay for Quantifying Protein-RNA Binding in Bacteria
Published on: June 12, 2019
NMR resonance assignment of DnaE intein from Nostoc punctiforme
Kimmo Heinämäki1, Jesper S Oeemig, Kimmo Pääkkönen
1Research Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, P.O. Box 65, Helsinki, 00014, Finland.
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 [(13)C,(15)N]-labeled protein.
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