14-3-3 interaction with histone H3 involves a dual modification pattern of phosphoacetylation.

@article{Walter20081433IW,
  title={14-3-3 interaction with histone H3 involves a dual modification pattern of phosphoacetylation.},
  author={Wendy Walter and David Clynes and Yong Tang and Ronen Marmorstein and Jane Mellor and Shelley L Berger},
  journal={Molecular and cellular biology},
  year={2008},
  volume={28 8},
  pages={2840-9}
}
Histone modifications occur in precise patterns and are proposed to signal the recruitment of effector molecules that profoundly impact chromatin structure, gene regulation, and cell cycle events. The linked modifications serine 10 phosphorylation and lysine 14 acetylation on histone H3 (H3S10phK14ac), modifications conserved from Saccharomyces cerevisiae to humans, are crucial for transcriptional activation of many genes. However, the mechanism of H3S10phK14ac involvement in these processes is… CONTINUE READING

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Yeast 14-3-3 proteins

  • G. P. van Heusden, H. Y. Steensma
  • Yeast
  • 2006
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