AbstractProhibition that works: Prohibitin 1Prohibitin 1 (Phb1) was cloned in 1991 based on its ability to suppress the regrowth of liver tissue. That task was not trivial – Phb1 turned out to be a buddy of just about anyone of any importance. It is highly conserved, ubiquitous among eukaryotes, and exerts a controlling interest in apoptosis, cell cycle, differentiation, and senescence. It, in turn, is controlled by a variety of post‐translational modifications. Did I say it is a tumor suppressor, too? It is. Sánchez‐Quiles et al. set out to survey the effects of changing levels of Phb1 on a variety of cell functions in cultured human hematoma cells. Using si technology, they found more that than 500 genes were stimulated or repressed in one liver cell line. One partial explanation is the observation that Phb1 is also involved in tissue homeostasis through two interacting networks.Sánchez‐Quiles, V. et al., Proteomics 2010, 10, 1609–1620.Myxobacter mixes mean mixture for mealsMost of us learned what we know of microbiology in medical settings, concerned about infectivity, clinical symptoms and drug resistance. Some of us (“molecular biologists”) never got beyond Escherichia coli and Bacillus subtilis. The excuse for working with so few species of bacteria was that it took too long to move all the genetic and biochemical tools into a new species. We can no longer hide behind that excuse. Entire genomes can be sequenced in a matter of weeks (or days). In this study, Chao et al. analyze the proteomic response of Anaeromyxobacter dehalogenans to changes in nutrients including uranium(VI), halogenated phenols, Fe(III) to fumarate as electron acceptors. Applying commonly used proteomic tools (2‐DE/MALDI‐TOF), they found spots for 559 unique proteins. Pathway analysis revealed an unusually wide array of means of living off of amino acid metabolism (like lysine to butyrate fermentation).Chao, T.‐C. et al., Proteomics 2010, 10, 1685–1693.“Brain must be in gear before starting mouth”This group clearly had their brain in gear. Sievers et al. gave Staphylococcus aureus every chance to respond “normally” to the deletion of a critical gene but virtually nothing changed on first glance. It was expected that deletion of lysyl‐phosphatidylglycerol synthase (lys‐PGS) would cause a major change in the cell membrane proteome. Only 1.5–3.5% of cell envelope proteins shifted up or down out of more than 35% of theoretical. The levels of lipid biosynthetic enzymes were unchanged. What was affected were the stress sensing regulatory proteins and their targets. When it comes to specifying new drug targets, lys‐PGS must be approached with care – it's mouth may already be engaged.Sievers, S. et al. Proteomics 2010, 10, 1694–1698.