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Epigenetics

In Memoriam C. David Allis: Chromatin unlocked

Nature Reviews Molecular Cell Biology volume 24, page 311 (2023)Cite this article

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The deposition, recognition and removal of histone post-translational modifications (PTMs) create the ‘histone code’ and are fundamental to the organization and function of our genome. Many scientists have made the study of these PTMs — characterizing the enzymes, other proteins and mechanisms involved — the focus of their research.

Early biochemical techniques, such as radiolabelling and Edman degradation sequencing, enabled the identification of histone PTMs in the mid-twentieth century; however, the function(s) of these PTMs remained largely unknown. In the late 1980s, several groups embarked on developing new tools, including histone-specific and histone PTM-specific antibodies, to unlock the mysteries behind histone PTMs (Lin et al. 1989; Turner et al. 1989). The lab of C. David Allis was among these groups, and was known for widely sharing histone antibodies with the chromatin field.

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References

Original article

  • Lin, R. et al. Antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in Tetrahymena. J. Cell Biol. 108, 1577–1588 (1989)

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Related article

  • Turner, B. M. et al. Histone H4 acetylation in human cells. Frequency of acetylation at different sites defined by immunolabeling with site-specific antibodies. FEBS Let. 253, 141–145 (1989)

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Authors and Affiliations

  1. Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA

    Kanishk Jain & Brian D. Strahl

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  1. Kanishk Jain
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  2. Brian D. Strahl
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Correspondence to Kanishk Jain or Brian D. Strahl.

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Jain, K., Strahl, B.D. In Memoriam C. David Allis: Chromatin unlocked. Nat Rev Mol Cell Biol 24, 311 (2023). https://doi.org/10.1038/s41580-023-00601-2

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