Skoltech researchers Maria Sokolova, Arina Drobysheva, Julia Gordeeva and Konstantin Severinov have co-authored a paper “Structural basis of template strand deoxyuridine promoter recognition by a viral RNA polymerase” that has been recently published in Nature Communications. The scientists explain the mechanism by which the phage AR9 non-virion RNAP (nvRNAP), a bacterial RNAP homolog, recognizes the −10 element of its deoxyuridine-containing promoter in the template strand. The AR9 sigma-like subunit, the nvRNAP enzyme core, and the template strand together form two nucleotide base-accepting pockets whose shapes dictate the requirement for the conserved deoxyuridines. The researchers claim that the work demonstrates the extent to which viruses can evolve host-derived multisubunit enzymes to become transcriptionally independent from host. Full text of the paper is available here.