Cell Biology

A Code for Cell Death

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Science  30 May 2003:
Vol. 300, Issue 5624, pp. 1345
DOI: 10.1126/science.300.5624.1345c

There is increasing evidence that the regulation of gene transcription is controlled in part by a “histone code.” This code would consist of a series of distinct and specific covalent modifications to the N-terminal tails of the histones within the nucleosome: the core structural component of chromatin. The condensation of chromatin during cell division is similarly known to involve histone modification, specifically the phosphorylation of serine 10 in the N-terminal tail of histone H3.

Hacker et al. now show that programmed cell death, or apoptosis, which involves chromatin condensation and the subsequent destruction of genomic DNA, may also be regulated by a histone code. Phosphorylation of Ser14 in the tail of histone H2B is correlated with the onset of apoptosis, suggesting that it may be involved in triggering chromatin condensation, which is then followed by DNA fragmentation and cell death. The kinase responsible for phosphorylating Ser14 is Mst1 (Mammalian Sterile Twenty), and both the covalent mark and the activity of Mst1 are dependent on caspase-3, a key regulatory enzyme in apoptosis.—GR

Cell 113, 507 (2003).

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