title: Molecular genetic and physical analysis of gas vesicles in buoyant enterobacteria.
abstract: Different modes of bacterial taxis play important roles in environmental adaptation, survival, colonization and dissemination of disease. One mode of taxis is flotation due to the production of gas vesicles. Gas vesicles are proteinaceous intracellular organelles, permeable only to gas, that enable flotation in aquatic niches. Gene clusters for gas vesicle biosynthesis are partially conserved in various archaea, cyanobacteria, and some proteobacteria, such as the enterobacterium, Serratia sp. ATCC 39006 (S39006). Here we present the first systematic analysis of the genes required to produce gas vesicles in S39006, identifying how this differs from the archaeon Halobacterium salinarum. We define 11 proteins essential for gas vesicle production. Mutation of gvpN or gvpV produced small bicone gas vesicles, suggesting that the cognate proteins are involved in the morphogenetic assembly pathway from bicones to mature cylindrical forms. Using volumetric compression, gas vesicles were shown to comprise 17% of S39006 cells, whereas in Escherichia coli heterologously expressing the gas vesicle cluster in a deregulated environment, gas vesicles can occupy around half of cellular volume. Gas vesicle production in S39006 and E. coli was exploited to calculate the instantaneous turgor pressure within cultured bacterial cells; the first time this has been performed in either strain.
authors.affiliation: Department of Biochemistry, University of Cambridge, Cambridge, CB2 1QW, UK.|Applied Chemistry and Biochemical Engineering Course, Department of Engineering, Graduate School of Integrated Science and Technology, Shizuoka University, Hamamatsu, 432-8561, Japan.
authors.forename: Yosuke
authors.initials: Y
authors.lastname: Tashiro
authors.affiliation: Department of Biochemistry, University of Cambridge, Cambridge, CB2 1QW, UK.
authors.forename: Rita E
authors.initials: RE
authors.lastname: Monson
authors.affiliation: Department of Biochemistry, University of Cambridge, Cambridge, CB2 1QW, UK.|Curtin Health Innovation Research Institute Biosciences Precinct, Faculty of Health Sciences, Curtin University, Bentley, WA, 6102, Australia.
authors.forename: Joshua P
authors.initials: JP
authors.lastname: Ramsay
authors.affiliation: Department of Biochemistry, University of Cambridge, Cambridge, CB2 1QW, UK.
authors.forename: George P C
authors.initials: GP
authors.lastname: Salmond
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics*; D000458:Cyanobacteria / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D019617:Halobacterium salinarum / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D015388:Organelles; D011506:Proteins / Q000235:genetics*; D012705:Serratia / Q000235:genetics / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D011506:Proteins; C038524:gas vesicle protein