Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins

@article{Lachner2001MethylationOH,
  title={Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins},
  author={M. Lachner and D. O’Carroll and Stephen C. Rea and K. Mechtler and T. Jenuwein},
  journal={Nature},
  year={2001},
  volume={410},
  pages={116-120}
}
  • M. Lachner, D. O’Carroll, +2 authors T. Jenuwein
  • Published 2001
  • Biology, Medicine
  • Nature
  • Distinct modifications of histone amino termini, such as acetylation, phosphorylation and methylation, have been proposed to underlie a chromatin-based regulatory mechanism that modulates the accessibility of genetic information. In addition to histone modifications that facilitate gene activity, it is of similar importance to restrict inappropriate gene expression if cellular and developmental programmes are to proceed unperturbed. Here we show that mammalian methyltransferases that… CONTINUE READING
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