Histone H3 lysine 9 methylation is an epigenetic imprint of facultative heterochromatin (original) (raw)

References

  1. Turner, B.M. Histone acetylation and an epigenetic code. Bioassays 22, 836–845 (2000).
    Article CAS Google Scholar
  2. Jenuwein, T. & Allis, C.D. Translating the histone code. Science 293, 1074–1080 (2001).
    CAS PubMed Central Google Scholar
  3. Rea, S. et al. Regulation of chromatin struture by site-specific histone H3 methyltransferases. Nature 406, 593–599 (2000).
    Article CAS Google Scholar
  4. Lachner, M., O'Carroll, D., Rea, S., Mechtler, K. & Jenuwein, T. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410, 116–120 (2001).
    Article CAS Google Scholar
  5. Bannister, A.J. et al. Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. Nature 410, 120–124 (2001).
    Article CAS Google Scholar
  6. Nakayama, J.-I., Rice, J.C., Strahl, B.D., Allis, C.D. & Grewal, S.I.S. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 292, 110–113 (2001).
    Article CAS Google Scholar
  7. Jeppesen, P., Mitchell, A., Turner, B.M. & Perry, P. Antibodies to defined histone epitopes reveal variations in chromatin conformation and underacetylation of centromeric heterochromatin in human metaphase chromosomes. Chromosoma 101, 322–332 (1992).
    Article CAS Google Scholar
  8. Ekwall, K., Olsson, T., Turner, B.M., Cranston, G. & Allshire, R.C. Transient inhibition of histone deacetylation alters the structural and functional imprint at fission yeast centromeres. Cell 91, 1021–1032 (1997).
    Article CAS Google Scholar
  9. Taddei, A., Maison, C., Roche, D. & Almouzni, G. Reversible disruption of pericentric heterochromatin and centromere function by inhibiting deacetylases. Nature Cell Biol. 3, 114–120 (2001).
    Article CAS Google Scholar
  10. Peters, A.H.F.M. et al. Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability. Cell 107, 323–337 (2001).
    Article CAS Google Scholar
  11. Avner, P. & Heard, E. X chromosome inactivation: counting, choice and initiation. Nature Rev. Genet. 2, 59–67 (2001).
    Article CAS Google Scholar
  12. Barr, M.L. & Bertram, E.G. A morphological distinction between neurones of the male and female, and the behaviour of the nucleolar satellite during accelerated nucleoprotein synthesis. Nature 163, 676–677 (1949).
    Article CAS Google Scholar
  13. Brockdorff, N. et al. The product of the mouse Xist gene is a 15 kb inactive X specific transcript containing no conserved ORF and located in the nucleus. Cell 71, 515–526 (1992).
    Article CAS Google Scholar
  14. Brown, C.J. et al. The human XIST gene: analysis of a 17 kb inactive X specific RNAthat contains conserved repeats and is highly localised within the nucleus. Cell 71, 527–542 (1992).
    Article CAS Google Scholar
  15. Lee, J.T., Strauss, W.M., Dausman, J.A. & Jaenisch, R. A 450 kb transgene displays properties of the mammalian X-inactivation center. Cell 86, 83–94 (1996).
    Article CAS Google Scholar
  16. Lee, J.T. & Lu, N. Targeted mutagenesis of Tsix leads to nonrandom X-inactivation. Cell 99, 47–57 (1999).
    Article CAS Google Scholar
  17. Jeppesen, P. & Turner, B.M. The inactive X chromosome in female mammals is distinguished by a lack of H4 acetylation, a cytogenetic marker for gene expression. Cell 74, 281–289 (1993).
    Article CAS Google Scholar
  18. Boggs, B.A., Connors, B., Sobel, R.E., Chinault, A.C. & Allis, C.D. Reduced levels of histone H3 acetylation on the inactive X chromosome in human females. Chromosoma 105, 303–309 (1996).
    Article CAS Google Scholar
  19. Costanzi, C. & Pherson, J.R. Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals. Nature 393, 599–601 (1998).
    Article CAS Google Scholar
  20. Perche, P.-Y. et al. Higher concentrations of histone macroH2A in the Barr body are correlated with higher nucleosome density. Curr. Biol. 10, 1531–1534 (2000).
    Article CAS Google Scholar
  21. Duthie, S.M. et al. Xist RNA exhibits a banded localization on the inactive X chromosome and is excluded from autosomal material in cis. Hum. Mol. Gen. 8, 195–204 (1999).
    Article CAS Google Scholar
  22. Minc, E., Allory, Y., Worman, H.J., Courvalin, J.-C. & Buendia, B. Localization and phosphorylation of HP1 proteins during the cell cycle in mammalian cells. Chromosoma 108, 220–234 (1999).
    Article CAS Google Scholar
  23. Boggs, B.A. et al. Differentially methylated forms of histone H3 show unique association patterns with inactive human X chromosomes. Nature Genet. DOI: 10.1038/ng787 (2001).
  24. Keohane, A.M., O'Neill, L.P., Belyaev, N.D., Lavender, J.S. & Turner, B.M. X-inactivation and histone H4 acetylation in embryonic stem cells. Dev. Biol. 180, 618–630 (1996).
    Article CAS Google Scholar
  25. Mermoud, J.E., Costanzi, C., Pherson, J.R. & Brockdorff, N. Histone macroH2A1.2 relocates to the inactive X chromosome after initiation and propagation of X-inactivation. J. Cell Biol. 147, 1399–1408 (1999).
    Article CAS Google Scholar
  26. Csankovszki, G., Panning, B., Bates, B., Pherson, J.R. & Jaenisch, R. Conditional deletion of Xist disrupts histone macroH2A localization but not maintenance of X inactivation. Nature Genet. 22, 323–324 (1999).
    Article CAS Google Scholar
  27. Wutz, A. & Jaenisch, R. A shift from reversible to irreversible X inactivation is triggered during ES cell differentiation. Mol. Cell 5, 695–705 (2000).
    Article CAS Google Scholar
  28. Tachibana, M., Sugimoto, K., Fukushima, T. & Shinkai, Y. SET domain–containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3. J. Biol. Chem. 276, 25309–25317 (2001).
    Article CAS Google Scholar
  29. Aagaard, L. et al. Functional mammalian homologues of the Drosophila PEV modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31. EMBO J. 18, 1923–1938 (1999).
    Article CAS Google Scholar
  30. Akhtar, A., Zink, D. & Becker, P.B. Chromodomains are protein–RNA interaction modules. Nature 407, 405–409 (2000).
    Article CAS Google Scholar

Download references