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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
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.
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.
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.
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.
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.