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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Induction of rapid histone degradation by the cytotoxic T lymphocyte protease Granzyme A.

The cytotoxic T lymphocyte protease granzyme A induces caspase-independent cell death in which DNA single-strand nicking is observed instead of oligonucleosomal fragmentation. Granzyme A is a specific tryptase that concentrates in the nucleus of targeted cells and synergistically enhances DNA fragmentation induced by the caspase activator granzyme B. Here we show that granzyme A treatment of isolated nuclei enhances DNA accessibility to exogenous endonucleases. In vitro and after cell loading with perforin, GrnA completely degrades histone H1 and cleaves core histones into approximately 16-kDa fragments. Histone digestion provides a mechanism for unfolding compacted chromatin and facilitating endogenous DNase access to DNA during T cell and natural killer cell granule-mediated apoptosis.[1]

References

  1. Induction of rapid histone degradation by the cytotoxic T lymphocyte protease Granzyme A. Zhang, D., Pasternack, M.S., Beresford, P.J., Wagner, L., Greenberg, A.H., Lieberman, J. J. Biol. Chem. (2001) [Pubmed]
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