title: Transcription- and translation-dependent changes in membrane dynamics in bacteria: testing the transertion model for domain formation.
abstract: Cell cycle events have been proposed to be triggered by the formation of membrane domains in the process of coupled transcription, translation and insertion ('transertion') of nascent membrane and exported proteins. Disruption of domain structure should lead to changes in membrane dynamics. Membrane viscosity of Escherichia coli and Bacillus subtilis decreased after inhibition of protein synthesis by chloramphenicol or puromycin, or of RNA initiation by rifampicin, but not after inhibition of RNA elongation by streptolydigin or amino acid starvation of a stringent strain. The decrease caused by inhibitors of protein synthesis was prevented by streptolydigin if added simultaneously, but was not reversed if added later. The drug-induced decrease in membrane viscosity is energy dependent: it did not happen in KCN-treated cells. All treatments decreasing membrane viscosity also induced nucleoid compaction and fusion. Inhibition of macromolecular synthesis without membrane perturbation caused nucleoids to expand. Changes in membrane dynamics were also displayed during a nutritional shift-down transition that causes imbalance in macromolecular syntheses. The results are consistent with the transertion model, predicting dissipation of membrane domains by termination of protein synthesis or detachment of polysomes from DNA; domain structure is conserved if the transertion process is 'frozen'.
authors.affiliation: Department of Life Sciences, Ben-Gurion University of the Negev, PO Box 653, Beer-Sheva 84105, USA.
authors.forename: Z
authors.initials: Z
authors.lastname: Binenbaum
authors.forename: A H
authors.initials: AH
authors.lastname: Parola
authors.forename: A
authors.initials: A
authors.lastname: Zaritsky
authors.forename: I
authors.initials: I
authors.lastname: Fishov
mesh_terms: D001412:Bacillus subtilis / Q000187:drug effects / Q000235:genetics / Q000502:physiology* / Q000648:ultrastructure; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors; D002462:Cell Membrane / Q000648:ultrastructure; D004269:DNA, Bacterial / Q000037:antagonists & inhibitors; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics / Q000502:physiology* / Q000648:ultrastructure; D008954:Models, Biological; D019384:Nucleic Acid Synthesis Inhibitors / Q000494:pharmacology; D014176:Protein Biosynthesis; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D012329:RNA, Bacterial / Q000037:antagonists & inhibitors; D014158:Transcription, Genetic
chemical_list: D001426:Bacterial Proteins; D004269:DNA, Bacterial; D019384:Nucleic Acid Synthesis Inhibitors; D011500:Protein Synthesis Inhibitors; D012329:RNA, Bacterial