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Science 18 May 2007:
Vol. 316. no. 5827, p. 949
DOI: 10.1126/science.316.5827.949n
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This Week in Science
DNA in eukaryotes is packaged onto nucleosomes, which consist of histone proteins. Covalent modification of histones plays a critical regulatory role in controlling transcription, replication, and repair. Different histone modifications are recognized by different protein modules, and these modules can be found in regulatory complexes with different, even antagonistic functions. Li et al. (p. 1050) tackle this apparent contradiction through analysis of the chromodomain protein Eaf3, which preferentially binds to histone H3 dimethylated at lysine 36. Eaf3 is a subunit of both the Rpd3S deacetylase complex and the NuA4 acetyltransferase complex. The affinity of the Rpd3S complex for nucleosomes and its control of global acetylation levels at transcribed chromatin are determined by the combined activities of Eaf3 and another protein, Rco1, which is not found in NuA4.
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Science. ISSN 0036-8075 (print), 1095-9203 (online)
