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Cell Division Site (cell + division_site)
Selected AbstractsA complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal regionMOLECULAR MICROBIOLOGY, Issue 5 2004Nienke Buddelmeijer Summary Three membrane proteins required for cell division in Escherichia coli, FtsQ, FtsL and FtsB, localize to the cell septum. FtsL and FtsB, which each contain a leucine zipper-like sequence, are dependent on each other for this localization, and each of them is dependent on FtsQ. However, FtsQ is found at the cell division site in the absence of FtsL and FtsB. FtsQ, in turn, requires FtsK for its localization. Here, we show that FtsL, FtsB and FtsQ form a complex in vivo. Strikingly, this complex forms in the absence of FtsK, which is required for the localization of all three proteins to the mid-cell. These findings indicate that the FtsL, FtsB, FtsQ interactions can take place in cells before movement to the mid-cell and that migration to this position might occur only after the formation of the complex. Evidence indicating the regions of the three proteins involved in complex formation is presented. These findings provide the first example of preassembly of a subcomplex of cell division proteins before their localization to the septal region. [source] Identification of a protein, YneA, responsible for cell division suppression during the SOS response in Bacillus subtilisMOLECULAR MICROBIOLOGY, Issue 4 2003Yoshikazu Kawai Summary A knock-out mutant of the dinR gene that encodes the SOS regulon repressor in Bacillus subtilis was constructed. The yneA, yneB and ynzC genes transcribed divergently from the dinR gene were strongly induced in mutant cells. Northern hybridization analyses revealed that these genes collectively form an operon and belong to the SOS regulon. The simultaneous deletion of dinR and yneA suppressed the filamentous phenotype of the dinR mutant. Furthermore, although yneA is suppressed in the wild-type cell in the absence of SOS induction, artificial expression of the YneA protein using an IPTG-inducible promoter resulted in cell elongation. Disruption of yneA significantly reduced cell elongation after the induction of the SOS response by mitomycin C in dinR+ cells. These results indicate that the YneA protein is responsible for cell division suppression during the SOS response in B. subtilis. Localization of the FtsZ protein to the cell division site was reduced in dinR -disrupted or yneA -expressing cells, further suggesting that the YneA protein suppresses cell division through the suppression of FtsZ ring formation. Interestingly, the B. subtilis YneA protein is structurally and phylogenetically unrelated to its functional counterpart in Escherichia coli, SulA. [source] Golgi secretion is not required for marking the preprophase band site in cultured tobacco cellsTHE PLANT JOURNAL, Issue 1 2002Ram Dixit Summary The preprophase band predicts the future cell division site. However, the mechanism of how a transient preprophase band fulfils this function is unknown. We have investigated the possibility that Golgi secretion might be involved in marking the preprophase band site. Observations on living BY-2 cells labeled for microtubules and Golgi stacks indicated an increased Golgi stack frequency at the preprophase band site. However, inhibition of Golgi secretion by brefeldin A during preprophase band formation did not prevent accurate phragmoplast fusion, and subsequent cell plate formation, at the preprophase band site. The results show that Golgi secretion does not mark the preprophase band site and thus does not play an active role in determination of the cell division site. [source] | ||||||||||