PMID:18077456

Citation	Campo, N, Marquis, KA and Rudner, DZ (2008) SpoIIQ anchors membrane proteins on both sides of the sporulation septum in Bacillus subtilis. J. Biol. Chem. 283:4975-82
Abstract	During the process of spore formation in Bacillus subtilis, many membrane proteins localize to the polar septum where they participate in morphogenesis and signal transduction. The forespore membrane protein SpoIIQ plays a central role in anchoring several mother-cell membrane proteins in the septal membrane. Here, we report that SpoIIQ is also responsible for anchoring a membrane protein on the forespore side of the sporulation septum. Co-immunoprecipitation experiments reveal that SpoIIQ resides in a complex with the polytopic membrane protein SpoIIE. During the early stages of sporulation, SpoIIE participates in the switch from medial to polar division and co-localizes with FtsZ at the polar septum. We show that after cytokinesis, SpoIIE is released from the septum and transiently localizes to all membranes in the forespore compartment. Upon the initiation of engulfment, it specifically re-localizes to the septal membrane on the forespore side. Importantly, the re-localization of SpoIIE to the engulfing septum requires SpoIIQ. These results indicate that SpoIIQ is required to anchor membrane proteins on both sides of the division septum. Moreover, our data suggest that forespore membrane proteins can localize to the septal membrane by diffusion-and-capture as has been described for membrane proteins in the mother cell. Finally, our results raise the intriguing possibility that SpoIIE has an uncharacterized function at a late stage of sporulation.
Links	PubMed Online version:10.1074/jbc.M708024200
Keywords	Bacillus subtilis/cytology; Bacillus subtilis/physiology; Bacterial Proteins/metabolism; Cell Division/physiology; Cell Membrane/metabolism; Protein Transport/physiology; Spores, Bacterial
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
BACSU:SP2Q		GO:0042601: endospore-forming forespore	ECO:0000315:		C		Figure 3 shows location of SpollQ in relation to SpollE by showing SpollQ mutant failing to relocalizing SpollE to septal membrane	complete CACAO 2287
BACSU:SP2Q	part_of	GO:0042601: endospore-forming forespore	ECO:0000315: mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
BACSU:SP2E	part_of	GO:0042601: endospore-forming forespore	ECO:0000314: direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
BACSU:SP2E		GO:0042601: endospore-forming forespore	ECO:0000314:		C		Figure 2. Shows SpollE is located throughout forespore membrane after polar division but concentrated at septal membrane during polar division	complete CACAO 2278

References

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