Journal of the Korean Magnetic Resonance Society (한국자기공명학회논문지)

Korean Magnetic Resonance Society (한국자기공명학회)
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NMR Hydrogen Exchange Study of DNA Duplex Containing the Consensus Binding Site for Human MEIS1

  • Choi, Seo-Ree (Department of Chemistry and Research Institute of Natural Science, Gyeongsang National University) ;
  • Jin, Ho-seong (Department of Chemistry and Research Institute of Natural Science, Gyeongsang National University) ;
  • Seo, Yeo-Jin (Department of Chemistry and Research Institute of Natural Science, Gyeongsang National University) ;
  • Lee, Joon-Hwa (Department of Chemistry and Research Institute of Natural Science, Gyeongsang National University)
  • Received : 2020.12.03
  • Accepted : 2020.12.17
  • Published : 2020.12.20
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Abstract

Transcription factors are proteins that bind specific sites or elements in regulatory regions of DNA, known as promoters or enhancers, where they control the transcription or expression of target genes. MEIS1 protein is a DNA-binding domain present in human transcription factors and plays important roles in various biological functions. The hydrogen exchange rate constants of the imino protons were determined for the wild-type containing the consensus DNA-binding site for the MEIS1 and those of the mutant DNA duplexes using NMR spectroscopy. The G2A-, A3G- and C4T-mutant DNA duplexes lead to clear changes in thermal stabilities of these four consensus base pairs. These unique dynamic features of the four base pairs in the consensus 5'-TGAC-3' sequence might play crucial roles in the effective DNA binding of the MEIS1 protein.

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References

  1. J. J. Moskow, F. Bullrich, K. Huebner and I. O. Daar, Mol. Cell. Biol, 15, 5434 (1995) https://doi.org/10.1128/MCB.15.10.5434
  2. T. Nakamura, N. A. Jenkins and N.G. Copeland. Oncogene, 13, 2235 (1996).
  3. A. M. Buchberg, H. G. Bedigian, N. A. Jenkins and N. G. Copeland. Mol. Cell. Biol, 10, 4658 (1990). https://doi.org/10.1128/MCB.10.9.4658
  4. T. Nakamura, D. A. Largaespada, J.D. Shaughnessy and N. A. Jenkins, Nat. Genet, 12, 149. (1996) https://doi.org/10.1038/ng0296-149
  5. A. P. G Crijns, P. de Graeff, D. Geerts and K. A. Ten Hoor, Eur. J. Cancer. Oxf. Engl. 1990, 43, 2495 (2007)
  6. T. A. Jones, R. H. Flomen, G. Senger and D. Nizetic, Eur. J. Cancer. Oxf. Engl. 1990 36, 2368 (2000)
  7. J. A. Rosales-Avina, J. Torres-Flores, A. Aguilar-Lemarroy and C. Gurrola-Diaz, J. Exp. Clin. Cancer. Res. 30, 1 (2011) https://doi.org/10.1186/1756-9966-30-1
  8. T. R. Burglin and M. Affolter. Chromosoma, 125, 497 (2016) https://doi.org/10.1007/s00412-015-0543-8
  9. E. Bertolino, B. Reimund, D. Wildt-Perinic and R. G. Clerc. J. Biol. Chem, 270, 31178 (1995) https://doi.org/10.1074/jbc.270.52.31178
  10. A. Jolma, Y. Yin, K. R. Nitta, K. Dave, A. Popov, M. Taipale, M. Enge, T. Kivioja, E. Morgunova and J Taipale. Nature. 527, 384 (2015) https://doi.org/10.1038/nature15518
  11. F. Delaglio, S. Grzesiek, G. W. Vuister, G. Zhu, J. Pfeifer and A. Bax, J. Biomol. NMR 6, 277. (1995).
  12. W. Lee, M. Tonelli and J. L. Markley. Bioinformatics, 31, 1325 (2015) https://doi.org/10.1093/bioinformatics/btu830
  13. J.-H. Lee and A. Pardi. Nucleic Acids Res. 35, 2965. (2007). https://doi.org/10.1093/nar/gkm184
  14. Y.-G. Choi, H.-E. Kim and J.-H. Lee. J. Korean Magn. Reson. Soc. 17, 76. (2013). https://doi.org/10.6564/JKMRS.2013.17.2.076
  15. H.-E. Kim, Y.-G. Choi, A.-R. Lee, Y.-J. Seo, M.-Y. Kwon and J.-H. Lee. J. Korean Magn. Reson. Soc. 18, 52 (2014) https://doi.org/10.6564/JKMRS.2014.18.2.052