title: Revisiting the cell biology of the acyl-ACP:phosphate transacylase PlsX suggests that the phospholipid synthesis and cell division machineries are not coupled in Bacillus subtilis.
abstract: PlsX is a central enzyme of phospholipid synthesis in bacteria, converting acyl-ACP to acyl-phosphate on the pathway to phosphatidic acid formation. PlsX has received attention because it plays a key role in the coordination of fatty acid and phospholipid synthesis. Recently, PlsX was also suggested to coordinate membrane synthesis with cell division in Bacillus subtilis. Here, we have re-investigated the cell biology of PlsX and determined that the enzyme is uniformly distributed on the membrane of most cells, but occasionally appears as membrane foci as well. Foci and homogenous patterns seem freely interconvertible but the prevalence of the uniform staining suggests that PlsX does not need to localize to specific sites to function correctly. We also investigated the relationship between PlsX and the divisome. In contrast to previous observations, PlsX's foci showed no obvious periodicity of localization and did not colocalize with the divisome. Furthermore, depletion of PlsX did not affect cell division if phospholipid synthesis is maintained by an alternative enzyme. These results suggest that coordination between division and membrane synthesis may not require physical or functional interactions between the divisome and phospholipid synthesis enzymes.
authors.affiliation: Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, SP, Brazil.
authors.forename: Diego Emiliano
authors.initials: DE
authors.lastname: Sastre
authors.affiliation: Department of Molecular and Cellular Biology and Faculty of Arts and Sciences (FAS) Center for Systems Biology, Harvard University, Cambridge, MA, 02138, USA.
authors.forename: Alexandre
authors.initials: A
authors.lastname: Bisson-Filho
authors.affiliation: Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET), and Departamento de Microbiología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Ocampo y Esmeralda, Predio CONICET Rosario, 2000, Rosario, Argentina.
authors.forename: Diego
authors.initials: D
authors.lastname: de Mendoza
authors.affiliation: Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, SP, Brazil.
authors.forename: Frederico J
authors.initials: FJ
authors.lastname: Gueiros-Filho
mesh_terms: D001412:Bacillus subtilis / Q000166:cytology* / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D002455:Cell Division; D005227:Fatty Acids / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism; D010743:Phospholipids / Q000096:biosynthesis* / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D005227:Fatty Acids; D010710:Phosphates; D010743:Phospholipids; C088150:plsX protein, bacteria