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DNA binding ability of histone-like protein HPhA is negatively affected by interaction with Pb2+

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Abstract

The histone-like protein (HPhA) is highly homologous to the eukaryotic histones and has the ability to bind to the DNA molecules. In this study, we tested divalent metal ions Mg2+, Ca2+, Zn2+, Pb2+ for their effect on the recombinant HPhA (rHPhA)-DNA binding. We found that only Pb2+ was able to reduce the formation of rHPhA-DNA complex using gel mobility shift assays. Equilibrium dialysis showed that Pb2+ bound to rHPhA by a 2:1 ratio. The interaction of Pb2+ and rHPhA was further studied by spectroscopic method including fluorescence, ultraviolet visible (UV–Vis) absorption, and circular dichroism (CD) spectroscopies. Fluorescent spectroscopy results suggested that Pb2+ and rHPhA formed a complex that caused internal quenching of the fluorescence of the protein at the ground state, and the quenching is predominately static and mixed with dynamic quenching. UV–Vis absorption spectrum results showed Pb2+ caused a slightly blue shift of the maximum absorption wavelength of rHPhA which indicated the reduction of the protein’s hydrophobicity. The CD spectrum further indicated that a reduction of the α-helix content of rHPhA occurred upon binding to Pb2+. Synchronous fluorescence spectrometry analysis revealed that Pb2+ was able to affect the polarity of the amino acids that near the Trp and Tyr residues. These results together showed that Pb2+ interact with the recombinant rHPhA and this interaction negatively affect the ability of rHPhA to form complex with DNA molecules.

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Acknowledgments

The authors gratefully acknowledge financial support from the National Natural Science Foundation of China (No. 31170742, No. 31100574 and No. 31370742).

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Authors and Affiliations

  1. Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, College of Life Science, Jilin University, 2699 Qianjin Street, Changchun, 130012, People’s Republic of China

    Yanyan Wang, Yang Zhan, Jinrui Zhang, Weiguo Liang, Xuexun Fang, Dahai Yu & Yan Feng

  2. College of Life Science, Jilin University, 2699 Qianjin Street, Changchun, 130012, People’s Republic of China

    Ye Wang

  3. State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, 200240, People’s Republic of China

    Yan Feng

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  1. Yanyan Wang
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  2. Ye Wang
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  3. Yang Zhan
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  4. Jinrui Zhang
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  5. Weiguo Liang
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  6. Xuexun Fang
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  7. Dahai Yu
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  8. Yan Feng
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Correspondence to Xuexun Fang, Dahai Yu or Yan Feng.

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Wang, Y., Wang, Y., Zhan, Y. et al. DNA binding ability of histone-like protein HPhA is negatively affected by interaction with Pb2+ . Biometals 28, 207–217 (2015). https://doi.org/10.1007/s10534-014-9816-6

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  • DOI: https://doi.org/10.1007/s10534-014-9816-6

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