An essential enzyme for phospholipid synthesis associates with the Bacillus subtilis divisome.
The mechanism by which the membrane synthetic machinery might be co-organized with the cell-division architecture during the bacterial cell cycle remains to be investigated. We characterized a key enzyme of phospholipid and fatty acid synthesis in Bacillus subtilis, the acyl-acyl carrier protein phosphate acyltransferase (PlsX), and identified it as a component of the cell-division machinery. Comprehensive interaction analysis revealed that PlsX interacts with FtsA, the FtsZ-anchoring protein. PlsX mainly localized at the potential division site independent of FtsA and FtsZ and then colocalized with FtsA. By multidirectional approaches, we revealed that the Z-ring stabilizes the association of PlsX at the septum and pole. The localization of PlsX is also affected by the progression of DNA replication. PlsX is needed for cell division and its inactivation leads to aberrant Z-ring formation. We propose that PlsX localization is prior to Z-ring formation in the hierarchy of septum formation events and that PlsX is important for co-ordinating membrane synthesis with cell division in order to properly complete septum formation.
Department of Bioscience, Tokyo University of Agriculture, 1-1-1 Sakuragaoka, Setagaya-ku, Tokyo, 156-8502, Japan.
Hiraku
H
Takada
Sanae
S
Fukushima-Tanaka
Masato
M
Morita
Yasuhiro
Y
Kasahara
Satoru
S
Watanabe
Taku
T
Chibazakura
Hiroshi
H
Hara
Kouji
K
Matsumoto
Hirofumi
H
Yoshikawa
D001412:Bacillus subtilis / Q000166:cytology / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002455:Cell Division; D016764:Cell Polarity; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D004261:DNA Replication; D004269:DNA, Bacterial / Q000502:physiology; D004795:Enzyme Stability
D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; D004269:DNA, Bacterial; C065103:FtsA protein, Bacteria; C071525:FtsZ protein, Bacteria; C088150:plsX protein, bacteria