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An evening symposium was held at the Museu de Historia de Catalunya (Barcelona, Spain) as a precursor to the European Bioanalysis Forum meeting, as part of the Waters Corporation Bioanalysis World Tour. The symposium was chaired by Robert Plumb and Jing Lin (Waters Corporation, MA, USA) with a focus on the future of the DMPK laboratory and its role in addressing large-molecule therapeutics and biomarkers. Lieve Dillen (Johnson and Johnson, Belgium) spoke on ultra-sensitive peptide quantification, Richard Kay (Quotient Bioresearch, UK) discussed quantifying proteins and peptides in plasma, Ian Wilson (AstraZeneca, UK) covered metabolic biomarkers and Robert Plumb concluded the evening with a presentation on the future of MS in DMPK studies. Following the presentations, all the speakers took questions from the audience and continued lively discussion over a cocktails and canapés reception.

In plants, unorthodox multisubunit RNA polymerases (RNAPs) play key roles in small interfering RNA (siRNA) genesis and function. In a recent issue of Molecular Cell, Ream et al. (2009) established a 12-subunit composition for Arabidopsis RNAPIV and RNAPV. Subunit and sequence divergence between RNAPIV-V and RNAPI-III suggests significant functional deviation of these intriguing RNAPs.

The family Totiviridae comprises viruses with nonsegmented dsRNA genomes and isometric virions. A new genus, Victorivirus, has been approved for this family, named from the specific epithet of Helminthosporium victoriae, host of the type species, Helminthosporium victoriae virus 190S. Distinguishing characteristics of the 11 viruses so far assigned to this genus include infection of filamentous fungi, an apparently coupled termination-reinitiation mechanism for translating the RNA-dependent RNA polymerase as a separate product from the upstream capsid protein, and sequence-based phylogenetic grouping in a distinct clade from other family members.

In this issue of Structure, Amzel, Bessman, and colleagues (Gabelli et al., 2007) present the crystal structure of a 17 kDa Nudix hydrolase from Escherichia coli previously characterized as a dATPase and provide evidence that it functions in vivo to remove pyrophosphate from the folate precursor dihydroneopterin triphosphate.