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Volume 14 Issue 8, August 2007

The Histone H3 N-terminal tail can be multiply methylated at different lysine residues. The structures of the histone demethylase JMJD2A in complex with peptides give insight into the specificity of histone demethylation. The clover and trefoil symbol represent JMJD2A's preference for acting on trimethylated lysines. Cover by Erin Boyle.pp 689-695 | News and Views p 682

Volume 14 Issue 8

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Editorial

  • Scientists coin new terms, or neologisms, at a tremendous pace, but name choice can have unforeseen results.

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News & Views

  • Targeting of enzymes regulating chromatin organization to specific histone residues is a key element in the hugely complex system of epigenetic signaling that controls gene regulation and repair. Understanding of how targeting is achieved is still limited, but structures of the histone lysine demethylase JMJD2A in complex with substrate peptides now offer insight into its dual specificity.

    • Jon R Wilson
    News & Views

  • Small RNAs can silence target genes by a variety of pathways and mechanisms. Specific microRNAs have now been shown to partition into distinct effector complexes, which may in turn affect their silencing output.

    • Priya Bellare
    • Erik J Sontheimer
    News & Views

  • How does RNA polymerase II cooperate with initiation factors to locate transcription start sites throughout the genome? A new cross-linking approach reveals previously unknown initiation factor–binding sites on the polymerase surface. The resulting model of the transcription initiation complex suggests that initiation factors cooperate above and inside the polymerase active center cleft to open DNA and find the transcription start site.

    • Patrick Cramer
    News & Views
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