Cell division in rod-shaped bacteria nearly always occurs exactly at mid-cell and is dependent on the formation of the cytokinetic FtsZ ring and its associated division proteins. Many thousands of copies of division, or septum-specific proteins assemble at this site and may lead to the exclusion of other integral membrane proteins that are normally able to diffuse freely throughout the cytoplasmic membrane. In this study we have investigated the localization of a series of integral membrane proteins in Bacillus subtilis and we show that the recruitment of division and septum-specific proteins does not necessarily preclude the diffusion of other integral membrane proteins. However, some proteins, namely ATP synthase and succinate dehydrogenase, are reduced/absent from the mid-cell region at the onset of cell division, which may reflect an association with lipid domains rich in phosphatidylglycerol that are thought to be present at diminished levels at sites of cell division.
BeallB.,
LutkenhausJ.1991; FtsZ in Bacillus subtilis is required for vegetative septation and for asymmetric septation during sporulation. Genes Dev 5:447–455
DaviesK. M.,
LewisP. J.2003; Localization of rRNA synthesis in Bacillus subtilis : characterization of loci involved in transcription focus formation. J Bacteriol 185:2346–2353
DaviesK. M.,
DedmanA.,
van HorckS.,
LewisP. J.2005; The NusA : RNA polymerase ratio is increased at sites of rRNA synthesis in Bacillus subtilis . Mol Microbiol 57:366–379
de MendozaD.,
SchujmanG. E.,
AguilarP. S.2002; Biosynthesis and function of membrane lipids. In Bacillus subtilis and its Closest Relatives: from Genes to Cells . pp 43–55 Edited by
SonenshineA. L.HochJ. A.,
LosickR.
Washington, DC: ASM Press;
ErringtonJ.,
DanielR. A.,
ScheffersD.-J.2003; Cytokinesis in bacteria. Microbiol Mol Biol Rev 67:52–65
HamoenL. W.,
MeileJ. C.,
de JongW.,
NoirotP.,
ErringtonJ.2006; SepF, a novel FtsZ-interacting protein required for a late step in cell division. Mol Microbiol 59:989–999
KatisV. L.,
HarryE. J.,
WakeR. G.1997; The Bacillus subtilis division protein DivIC is a highly abundant membrane-bound protein that localizes to the division site. Mol Microbiol 26:1047–1055
KsenzenkoS. M.,
BrusilowW. S. A.1993; Protein–-lipid interactions of the proteolipid c subunit of the Escherichia coli proton-translocating adenosinetriphosphatase. Arch Biochem Biophys 305:78–83
MeijerW. J.,
Serna-RicoA.,
SalasM.2001; Characterization of the bacteriophage phi29-encoded protein p16.7: a membrane protein involved in phage DNA replication. Mol Microbiol 39:731–746
MigockiM. D.,
LewisP. J.,
WakeR. G.,
HarryE. J.2004; The midcell replication factory in Bacillus subtilis is highly mobile: implications for coordinating chromosome replication with other cell cycle events. Mol Microbiol 54:452–463
MileykovskayaE.,
DowhanW.2000; Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10- N -nonyl acridine orange. J Bacteriol 182:1172–1175
SharpeM. E.,
HauserP. M.,
SharpeR. G.,
ErringtonJ.1998; Bacillus subtilis cell cycle as studied by fluorescence microscopy: constancy of cell length at initiation of DNA replication and evidence for active nucleoid partitioning. J Bacteriol 180:547–555
WuL. J.,
ErringtonJ.2004; Coordination of cell division and chromosome segregation by a nucleoid occlusion protein in Bacillus subtilis . Cell 117:915–925
WuL. J.,
LewisP. J.,
AllmansbergerR.,
HauserP. M.,
ErringtonJ.1995; A conjugation-like mechanism for prespore chromosome partitioning during sporulation in Bacillus subtilis . Genes Dev 9:1316–1326