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A study on the secondary structure of the metalloregulatory protein CueR: effect of pH, metal ions and DNA

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Abstract

The response of CueR towards environmental changes in solution was investigated. CueR is a bacterial metal ion selective transcriptional metalloregulator protein, which controls the concentration of copper ions in the cell. Although several articles have been devoted to the discussion of the structural and functional features of this protein, CueR has not previously been extensively characterized in solution. Here, we studied the effect of change in pH, temperature, and the presence of specific or non-specific binding partners on the secondary structure of CueR with circular dichroism (CD) spectroscopy. A rather peculiar reversible pH-dependent secondary structure transformation was observed, elucidated and supplemented with pKa estimation by PROPKA and CpHMD simulations suggesting an important role of His(76) and His(94) in this process. CD experiments revealed that the presence of DNA prevents this structural switch, suggesting that DNA locks CueR in the α-helical-rich form. In contrast to the non-cognate metal ions HgII, CdII and ZnII, the presence of the cognate AgI ion affects the secondary structure of CueR, most probably by stabilizing the metal ion and DNA-binding domains of the protein.

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Acknowledgements

Financial support from the Hungarian National Research, Development and Innovation Office (GINOP-2.3.2-15-2016-00038 and K_16/120130), from the CALIPSOplus (EU Framework Programme for Research and Innovation HORIZON 2020, grant no. 730872) and from the COST Action CA15126 ARBRE MOBIEU is gratefully acknowledged. R.K.B. got a fellowship within the frame of NFTÖ-18 (NTP-NFTÖ-18-B-0137) New National Excellence Program of the Ministry of Human Capacities. The authors thank to Ferenc Bartha for useful discussions on CpHMD simulations, and Peter Waaben Thulstrup for his useful pieces of advice during SRCD measurements. National Information Infrastructure Development (NIIF) Programme is acknowledged for providing the supercomputing infrastructure at University of Debrecen (Debrecen2 server).

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  1. Eszter Németh

    Present address: Institute of Enzymology, Genome Stability Research Group, Research Centre for Natural Sciences, Magyar tudósok körútja 2, Budapest, 1117, Hungary

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  1. Department of Inorganic and Analytical Chemistry, University of Szeged, Dóm tér 7, Szeged, 6720, Hungary

    Ria K. Balogh, Eszter Németh, Attila Jancsó & Béla Gyurcsik

  2. ISA, Department of Physics and Astronomy, Aarhus University, Ny Munkegade 120, 8000, Aarhus C, Denmark

    Nykola C. Jones & Søren Vrønning Hoffmann

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Balogh, R.K., Németh, E., Jones, N.C. et al. A study on the secondary structure of the metalloregulatory protein CueR: effect of pH, metal ions and DNA. Eur Biophys J 50, 491–500 (2021). https://doi.org/10.1007/s00249-021-01539-z

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