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1H, 13C and 15N NMR chemical shift assignments of A. thaliana RCD1 RST

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Abstract

The A. thaliana RCD1 (radical-induced cell death1) protein is a cellular signaling hub protein which interacts with numerous plant transcription factors from different families. It consists of three conserved domains and intervening unstructured regions, the C-terminal RST domain being responsible for the interactions with the transcription factors. It has been shown that many partner proteins interact with RCD1 RST via their intrinsically disordered regions, and that the domain is able to house partners with divergent folds. We aim to structurally characterize the RCD1 RST domain and its complexes [complex with DREB2A]. Here we report the 1H, 15N and 13C chemical shift assignments of the backbone and sidechain atoms for RCD1 (468–589) containing the RST (510–567) domain.

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Acknowledgements

This study was supported by the grants from Academy of Finland (Number 288235) and Sigrid Juselius foundation to PP.

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Authors and Affiliations

  1. Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Helsinki, Finland

    Helena Tossavainen & Perttu Permi

  2. Department of Chemistry, Nanoscience Center, University of Jyvaskyla, Jyvaskyla, Finland

    Maarit Hellman & Perttu Permi

  3. Division of Plant Biology, Department of Biosciences, Viikki Plant Science Centre, University of Helsinki, Helsinki, Finland

    Julia P. Vainonen & Jaakko Kangasjärvi

  4. Department of Biological and Environmental Science, Nanoscience Center, University of Jyvaskyla, Jyvaskyla, Finland

    Perttu Permi

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  1. Helena Tossavainen
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  2. Maarit Hellman
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  3. Julia P. Vainonen
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  4. Jaakko Kangasjärvi
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  5. Perttu Permi
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Correspondence to Perttu Permi.

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Tossavainen, H., Hellman, M., Vainonen, J.P. et al. 1H, 13C and 15N NMR chemical shift assignments of A. thaliana RCD1 RST. Biomol NMR Assign 11, 207–210 (2017). https://doi.org/10.1007/s12104-017-9749-4

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  • DOI: https://doi.org/10.1007/s12104-017-9749-4

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