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

SASTRE, D.E; BISSON-FILHO, A; DE MENDOZA, D; GUEIROS-FILHO, J.F

MOLECULAR MICROBIOLOGY

WILEY-BLACKWELL PUBLISHING, INC

Lugar: Londres; Año: 2016

0950-382X

PlsX is a central enzyme of phospholipid synthesis in bacteria, converting acyl-ACP toacyl-phosphate on the pathway to phosphatidic acid formation. PlsX has receivedattention because it plays a key role in the coordination of fatty acid and phospholipidsynthesis. Recently, PlsX was also suggested to coordinate membrane synthesis withcell division in Bacillus subtilis. Here we have re-investigated the cell biology of PlsXand 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 seemfreely interconvertible but the prevalence of the uniform staining suggests that PlsXdoes not need to localize to specific sites to function correctly. We also investigated therelationship between PlsX and the divisome. In contrast to previous observations,PlsX´s foci showed no obvious periodicity of localization and did not colocalize withthe divisome. Furthermore, depletion of PlsX did not affect cell division if phospholipidsynthesis is maintained by an alternative enzyme. These results suggest thatcoordination between division and membrane synthesis may not require physical orfunctional interactions between the divisome and phospholipid synthesis enzymes.