Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

Volume 13 Issue 12, December 2006

The mechanism by which nucleosomes are evenly spaced at silent loci is explored by Narlikar and colleagues, who use a FRET assay to follow in vitro nucleosome movement mediated by the ACF chromatin remodeling complex. On the cover the beads on an abacus represent nucleosomes spaced on DNA. Photo licensed from iStockPhoto.com. pp 1078-1083 | News and Views p 1047

Editorial

Top of page ⤴

Essay

  • Elizabeth Blackburn, Carol Greider and Jack Szostak were recently recognized with the Lasker award for their work on telomerase and the role of this enzyme in cellular proliferation. Vicki Lundblad reflects on the excitement as these experiments were unfolding.

    • Vicki Lundblad
    Essay
  • Andrew Fire and Craig Mello have won the Nobel Prize in Medicine or Physiology for their discovery of RNA interference. Mary K. Montgomery, then a postdoc in the Fire laboratory, participated in some of the key experiments.

    • Mary K Montgomery
    Essay
Top of page ⤴

News & Views

  • Ubiquitin-like protein (Ubl)-specific proteases catalyze Ubl precursor processing and deconjugation. Two recent structural studies of SUMO-specific protease (SENP)–substrate complexes provide new insight into hydrolysis of the peptide bond at the C terminus of SUMO. A kinked, cis configuration for the scissile bond is crucial for proteolysis.

    • Danny T Huang
    • Brenda A Schulman
    News & Views
  • The mechanism by which ATP-dependent remodeling enzymes act to space nucleosomes is as yet unclear. A new study uses FRET to monitor nucleosome repositioning in real time to address how these enzymes sense when nucleosomes are evenly distributed.

    • Helder Ferreira
    • Tom Owen-Hughes
    News & Views
  • The first structures of an intramembrane serine protease reveal a catalytic His-Ser dyad in a water-filled cavity surrounded by six transmembrane helices, but just how substrate helices gain access to the dyad is controversial.

    • Stephen H White
    News & Views
Top of page ⤴

Perspective

Top of page ⤴

Article

Top of page ⤴

Search

Quick links