| Full text | |
| Author(s): |
Sastre, Diego Emiliano
[1]
;
Bisson-Filho, Alexandre
[2, 3]
;
de Mendoza, Diego
[4, 5]
;
Gueiros-Filho, Frederico J.
[1]
Total Authors: 4
|
| Affiliation: | [1] Univ Sao Paulo, Inst Quim, Dept Bioquim, Sao Paulo, SP - Brazil
[2] Harvard Univ, Ctr Syst Biol, Dept Mol & Cellular Biol, Cambridge, MA 02138 - USA
[3] Harvard Univ, Ctr Syst Biol, FAS, Cambridge, MA 02138 - USA
[4] Univ Nacl Rosario, Inst Biol Mol & Celular Rosario IBR CONICET, Predio CONICET Rosario, RA-2000 Rosario - Argentina
[5] Univ Nacl Rosario, Dept Microbiol, Fac Ciencias Bioquim & Farmaceut, RA-2000 Rosario - Argentina
Total Affiliations: 5
|
| Document type: | Journal article |
| Source: | Molecular Microbiology; v. 100, n. 4, p. 621-634, MAY 2016. |
| Web of Science Citations: | 4 |
| 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. (AU) | |
| FAPESP's process: | 14/13411-1 - Study of acyltransferases required for the synthesis of membrane phospholipids in Gram-positive bacteria: an attractive target for antibacterial drug discovery |
| Grantee: | Diego Emiliano Sastre |
| Support type: | Scholarships in Brazil - Post-Doctorate |