Wulf Blankenfeldt

TL;DR: Advances within the past two decades have provided significant new insights into the genetics, biochemistry, and regulation of phenazine synthesis, as well as the mode of action and functional roles of these compounds in the environment, which reveals conservation of biosynthetic enzymes across genera but raises questions about conserved biosynthesis mechanisms.

TL;DR: The ability of Legionella pneumophila to manipulate vesicular trafficking by the covalent modification of the small guanosine triphosphatase (GTPase) Rab1, which normally regulates the transport of endoplasmic reticulum–derived vesicles in eukaryotic cells is described.

TL;DR: Genome analyses and comparisons of phylogenies inferred from sequences of the key phenazine biosynthesis (phzF) and housekeeping (rrs, recA, rpoB, atpD, and gyrB) genes revealed that the evolution and dispersal of phenazine genes are driven by mechanisms ranging from conservation to horizontal gene transfer.

TL;DR: The structures of five distinct enzyme substrate–product complexes reveal the enzyme mechanism that involves precise positioning of the nucleophile and activation of the electrophile, suggesting that the basic mechanism is found in many nucleotidyltransferases.

TL;DR: It is shown that the GEF activity of DrrA is sufficient to displace prenylated Rab1 from the Rab1:GDI complex, suggesting a basic model for GDI displacement and specificity of Rab localization that does not require discrete GDI displaced activity.