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 14 Issue 1, January 2007

DGCR8 is an RNA binding protein involved in the processing of primary microRNA transcripts. Guo and colleagues now show that DGCR8 binds heme. Upon heme binding, autoinhibition mediated by the heme-binding region of DGCR8 is alleviated, promoting primary microRNA processing. The heme molecule is represented within snowflakes on the cover image. Cover by Erin Boyle. pp 23-29

Editorial

Top of page ⤴

Obituary

Top of page ⤴

Meeting Report

  • Over the next few years, structural proteomics will grapple with the problem of visualizing increasingly elaborate structures, from the atomic details of protein structures up to subcellular structures and the whole cell. A recent EU workshop addressed the question of what experimental and theoretical approaches, technologies and infrastructures this will demand.

    • Lucia Banci
    • Wolfgang Baumeister
    • Joel L Sussman
    Meeting Report
Top of page ⤴

News & Views

  • The exosome, the major eukaryotic 3′ exoribonuclease acting in processing or degradation of a wide variety of RNA substrates, contains six subunits with predicted phosphorolytic activity and a single hydrolytic subunit. Recent data suggest that the phosphorolytic subunits of the yeast enzyme are catalytically inactive, and the hydrolytic subunit is solely responsible for the activity of the core exosome.

    • Elmar Wahle
    News & Views
  • The structures of APOBEC2 and TadA, members of a superfamily of Zn-dependent deaminases, reveal unexpected features and provide insight into the ability of some family members to act on DNA.

    • Silvestro G Conticello
    • Marc-Andre Langlois
    • Michael S Neuberger
    News & Views
  • Two independent crystal structure analyses have resolved the detailed interactions between botulinum neurotoxin serotype B and its neuronal receptor, synaptotagmin. The studies show how the toxin binds synaptotagmin and, along with previously determined interactions with the ganglioside GT1b, a coreceptor, explain the toxin's extreme toxicity and tropism for neurons.

    • Michael R Baldwin
    • Jung-Ja P Kim
    • Joseph T Barbieri
    News & Views
  • The central function of kinetochores is to grasp a dynamic microtubule. Structural, biochemical and cell biological approaches have converged to uncover a microtubule-binding activity within the Ndc80/HEC1 complex, providing a satisfying answer to a question that has puzzled biologists for the last century.

    • Michael Emanuele
    • Daniel J Burke
    • P Todd Stukenberg
    News & Views
Top of page ⤴

Article

Top of page ⤴

Brief Communication

Top of page ⤴

Search

Quick links