In a paper published online in advance in Nature this week, researchers at the Northwestern University Feinberg School of Medicine and elsewhere report that mutations in UBQLN2 — which encodes the ubiquitin-like protein ubiquilin 2 — "cause dominantly inherited, chromosome-X-linked ALS [amyotrophic lateral sclerosis] and ALS/dementia." In its functional analyses, the team found evidence linking "abnormalities in ubiquilin 2 to defects in the protein degradation pathway, abnormal protein aggregation and neurodegeneration, indicating a common pathogenic mechanism that can be exploited for therapeutic intervention," it says.
In another Nature advance online publication, an international team led by investigators at the Wellcome Trust Sanger Institute reports its molecular investigation of the underlying phylogeny of the lineage responsible for the current cholera pandemic — including recent outbreaks in Zimbabwe and Haiti. "We identified high-resolution markers (SNPs) in 154 whole-genome sequences of globally and temporally representative V. cholerae isolates," the authors write, adding that "using this phylogeny, we show ... that the seventh pandemic has spread from the Bay of Bengal in at least three independent but overlapping waves with a common ancestor in the 1950s."
Over in this week's issue, the Brookings Institution's William Brown says that "to complement its efforts to conserve nature in the wild, the Convention on Biological Diversity should develop a comprehensive and adequately funded global effort to preserve intact genomes and viable cells for every known species and for new species as they are discovered." In his Nature correspondence, Brown breaks down the storage costs per species. "Preserving material from all the roughly 1.8 million known species would cost about $540 million," which, to Brown's mind is a bargain, he says. "Less than $1 billion to preserve the DNA of all known species on Earth, with whom we share billions of years of evolutionary history, seems like good value."
And in Nature Structural & Molecular Biology this week, researchers at Columbia University discuss the "transfer RNA-mediated regulation of ribosome dynamics during protein synthesis." Columbia's Jingyi Fei et al. report their use of single-molecule FRET to "characterize the dynamics of ribosomal pre-tanslocation complex analogs carrying either wild-type or systematically mutagenized tRNAs," finding that specific tRNA-ribosome interactions regulate the arrangement rate of the pre-translation complex to "a critical, on-pathway translocation intermediate and how these interactions control the stability of the resulting configuration."