Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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NMR Studies on the N-terminal Acetylation Domain of Histone H4

  • Published : 20010500
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Abstract

Histones, nuclear proteins that interact with DNA to form nucleosomes, are essential for both the regulation of transcription and the packaging of DNA within chromosomes. The N-terminal domain of histone H4 which contains four acetylation sites at lysines, may play a separate role in chromatin structure from the remainder of the H4 chain. NMR data suggest that H4NTP peptide does have relating disordered structure at physiological pH, however, it has a defined structure at lower pH conditions. The solution structure calculated from NMR data shows a well structured region comprising residues of Val21-Asp24. In addition, our results suggest that the H4NTP prefers an extended backbone conformation at acetylation sites, however, it (especially Lys 12 ) became more defined structures after acetylation for its optimum function.

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References

  1. Chromatin Structure and Function Wolffe, A. P.
  2. EMBO. J. v.12 Schild, C.;Claret, F, -X.;Wahli, W.;Wolffe, A. P.
  3. Curr. Opin. Genet. Dev. v.6 Brownell, J. B.;Allis, C. D.
  4. Genes Dev. v.7 Braunstein, M.;Rose, A. B.;Holmes, S. G.;Allis, C. D.;Broach, J. R.
  5. Mol. Cell. Biol. v.16 Braunstein, M;Sobel, R. E.;Allis, C. D.;Turner, B. M;Broach, J.
  6. Science v.272 Wolffe, A. P.
  7. J. Biol. Chem. v.270 Kleff, S.;ANdrulis, E. D.;Anderson, C. W.;Sternglanz. R.
  8. Cell. v.84 Brownell, J. E.;Zhou, J.;Ranalli, T.;Kobayashi. R.;Edmondson, D. G.;Roth, S. Y.;Allis, C. D.
  9. Science v.272 Taunton, J.;Hassig, C. A.;Schreiber, S. L.
  10. Proc. Natl. Acad. Sci. v.51 Allfrey, V. G.;Faulkner, R. M.;Mirsky, A. E.
  11. Biochem J. v.294 Clarke, D. J.;ONeill, L. P.;Turner, B. M.
  12. EMBO J. v.14 O'Neill, L. P.;Turner, B. M.
  13. Proc. Natl. Acad. Sci. v.92 Sobel, R. E.;Coolk, R. G.;Perry, C. A.;Annunziato, A. T.;Allis, C. D.
  14. Biochem. Biophys. Res. Commun. v.113 Marion, D.;Wuthrich, K.
  15. J. Chem. Phys. v.71 Jeener, J.;Meier, B. H.;Bachman, P.;Ernst, R. R.
  16. Biochem. Biophys. Res. Commun. v.117 Rance, M.;Sorensen, O. W.;Bodenhausen, G.;Wagner, G.;Ernst, R. R.;Wuthrich, K.
  17. J. Am. Chem. Soc. v.107 Davis, D. G.;Bax, A.
  18. J. Biomol. v.2 Piotto, M.;Saudek, V.;Sklenar, V.
  19. Biochemistry v.28 Driscoll, P. C.;Gronenborn, A. M.;Beress, L.;Clore, G. M.
  20. FEBS Leff. v.229 Nilges, M.;Clore, G. M.;Gronenborn, A. M.
  21. FEBS Leff. v.239 Nilges, M.;Clore, G. M.;Gronenborn, A. M.
  22. Protein Eng. v.2 Nilges, M.;Clore, G. M.;Gronenborn, A. M.
  23. Eur. J. Biochem. v.218 Lee, W.;Moore, C. H.;Watt, D. D.;Krishna, N. R.
  24. FEBS lett. v.243 Driscoll, P. C.;Gronenborn, A. M.;Clore, G. M.
  25. J. Mol. Biol. v.169 Wuthrich, K.;Billeten, M.;Braun, W.
  26. J. Mol. Biol. v.14 Koradi, R.;Billeter, M.;Wuthrich, M.
  27. J. Peptide Res. v.51 Vu, H. M.;Minch, M. J.
  28. NMR of Proteins and Nucleic Acides Wuthrch, K.
  29. Nature v.389 Luger, K.;Mader, A. W.;Richmond, R. K.;Sargent, D. F.;Richmond, T. J.
  30. Cell. v.94 Dutnall, R. N.;Tafrov, S. T.;Sternglanz, R.;Ramakrishnan, V.
  31. Eur. J. Biochem. v.127 Cary, P. D.;Crane-Robinson, C.;Bradbury, E. M.;Dixon, G. H.
  32. Cell. v.69 Turner, B. M.;Birley, A. J.;Lavender, J.