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Volume 13 Issue 8, August 2006

Structural data from the Berger, Botchan and Nogales labs show that initiator proteins of DNA replication in E. coli and Drosophila form a spiraling superstructure represented here by a spring. pp 676-683 | 684-690 | p 665

Volume 13 Issue 8

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  • Replication initiators in both bacteria and eukaryotes are AAA+ proteins that bind and remodel origin DNA sequences, preparing them for chromosome duplication. Two new reports show that the bacterial DnaA and eukaryotic ORC initiators form protein helical filaments. Wrapping of origin DNA around these filaments may promote DNA unwinding and subsequent assembly of replication forks.

    • Mike O'Donnell
    • David Jeruzalmi
    News & Views

  • The activity of a handful of transcription factors, such as mammalian NF-κB, Drosophila melanogaster Cubitus interruptus and yeast Spt23 and Mga2, are regulated through partial protein degradation by the proteasome. New data now show that the proteasome activates membrane-bound Spt23 and Mga2 by initiating their proteolysis at an internal site and then degrading the proteins bidirectionally toward both ends of the polypeptide chain, modifying our ideas on how the proteasome degrades targeted substrates.

    • Lin Tian
    • Andreas Matouschek
    News & Views

  • A new crystal structure reveals the path taken by single-stranded (ss) DNA through the central channel of a hexameric helicase. The path resembles a spiral staircase and provides an answer to the question of how hexameric helicases translocate on ssDNA.

    • Kevin D Raney
    News & Views

  • The main function of mouse POT1 proteins is to regulate G-overhang length, suppress telomere recombination and prevent a telomeric DNA-damage response. They are not needed to prevent G-overhang loss and have only a minor role in preventing telomere fusions.

    • Carolyn M Price
    News & Views
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