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1H, 13C and 15N assignments of CdnL, an essential protein in Myxococcus xanthus

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Abstract

CdnL, an essential protein in Myxococcus xanthus and several other bacteria, is a member of the large CarD_TRCF family of bacterial proteins that interact with RNA polymerase. Structural analyses of the 164-residue M. xanthus CdnL by NMR is complicated because of broadening, and hence overlap, of the signals due to the self-association and the monomer–dimer equilibrium that occurs in solution. Here, we report 1H, 13C and 15N assignments for CdnL achieved by analyzing its NMR spectra on the basis of the complete assignment obtained in this study for the 68-residue N-terminal fragment of CdnL (CdnLNt) together with those we described previously for the stable, protease-resistant, 110-residue C-terminal domain (CdnLCt). This approach relied on our observation that many of the CdnLNt and CdnLCt chemical shifts matched closely with those of the equivalent residues in the full-length protein. Our assignments provide the crucial first step in the structural analysis of CdnL and this functionally important family of bacterial proteins.

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Acknowledgments

We thank C. López, Dr. Pantoja-Uceda and L. de la Vega (Instituto de Química Física Rocasolano, CSIC) for technical assistance, and Drs. César Flores-Flores and Alejandro Torrecillas (Universidad de Murcia) for DNA sequencing and mass spectrometry analysis. This work was funded by grants CTQ2008-0080/BQU (MAJ), BFU2009-12445-C02-02 (SP) and BFU2009-12445-C02-01 (MEA) from the Ministerio de Ciencia e Innovación (MCINN), Spain, and a Ph.D. fellowship (YM) from Consejo Superior de Investigaciones Científicas (CSIC), Spain.

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Correspondence to S. Padmanabhan or M. Angeles Jiménez.

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Mirassou, Y., Elías-Arnanz, M., Padmanabhan, S. et al. 1H, 13C and 15N assignments of CdnL, an essential protein in Myxococcus xanthus . Biomol NMR Assign 7, 51–55 (2013). https://doi.org/10.1007/s12104-012-9375-0

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  • DOI: https://doi.org/10.1007/s12104-012-9375-0

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