A new FtsZ‐interacting protein, YlmF, complements the activity of FtsA during progression of cell division in <i>Bacillus subtilis</i>

Ishikawa, Shu; Kawai, Yoshikazu; Hiramatsu, Konosuke; Kuwano, Masayoshi; Ogasawara, Nagahisa

doi:10.1111/j.1365-2958.2006.05184.x

Cited by 139 publications

(190 citation statements)

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“…Construction of strains expressing C-terminally histidine-tagged DnaA Strains expressing C-terminally histidine-tagged DnaA from its original position without plasmid integration between dnaA and dnaN were constructed as previously described (Ishikawa et al, 2006). Briefly, CRK6000 and NIS6051 were transformed with the integration plasmid pMUTinAhisN (Ishikawa et al, 2007), and transformants were selected on PAB medium supplemented with 0.5 μg/ml erythromycin and 1 mM IPTG to induce essential dnaN expression from the spac promoter of the integration plasmid downstream of the integration position.…”

Section: Methodsmentioning

confidence: 99%

The functional analysis of YabA, which interacts with DnaA and regulates initiation of chromosome replication in Bacillus subtils

2008

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The initiation of bacterial chromosome DNA replication and its regulation are critical events. DnaA is essential for initiation of DNA replication and is conserved throughout bacteria. In Escherichia coli, hydrolysis of ATP-DnaA is promoted by Hda through formation of a ternary complex with DnaA and DnaN, ensuring the timely inactivation of DnaA during the replication cycle. In Bacillus subtilis, YabA also forms a ternary complex with DnaA and DnaN, and negatively regulates the initiation step of DNA replication. However, YabA shares no structural homology with Hda and the regulatory mechanism itself has not been clarified. Here, in contrast to Hda, we observed that dnaA transcription was stable during under-and overexpression of YabA. ChAP-chip assays showed that the depletion of YabA did not affect DNA binding by DnaA. On the other hand, yeast two-hybrid analysis indicated that the DnaA ATP-binding domain interacts with YabA. Moreover, mutations in YabA interaction-deficient mutants, isolated by yeast two-hybrid analysis, are located at the back of the ATP-binding domain, whereas Hda is thought to interact with the ATP-binding pocket itself. The introduction into B. subtilis of a dnaA Y144C mutation, which disabled the interaction with YabA but did not affect interactions either with DnaA itself or with DnaD, resulted in over-initiation and asynchronous initiation of replication and disabled the formation of YabA foci, further demonstrating that the amino acid on the opposite side to the ATP-binding pocket is important for YabA binding. These results indicate that YabA indeed regulates the initiation of DNA replication by a different mechanism from that used by Hda in the E. coli RIDA system. Interestingly, all DnaA mutants deficient in YabA binding also displayed reduced DnaD binding in yeast two-hybrid assays, suggesting that YabA can inhibit replication initiation through competitive inhibition of DnaD binding to DnaA.

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Section: Methodsmentioning

confidence: 99%

The functional analysis of YabA, which interacts with DnaA and regulates initiation of chromosome replication in Bacillus subtils

2008

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“…Moreover, there are no data suggesting that FtsA interacts directly with residues in the CTV of either E. coli FtsZ or B. subtilis FtsZ. Finally, although it is possible that the CTV is needed for an interaction with a modulatory protein other than FtsA, it is unclear what such a protein would be because the Bs ftsZ CTVE phenotype is unlike those of other cell division mutants, including zapA and sepF (6,49).…”

Section: ϩmentioning

confidence: 99%

Extreme C Terminus of Bacterial Cytoskeletal Protein FtsZ Plays Fundamental Role in Assembly Independent of Modulatory Proteins

Buske

Levin

2012

Journal of Biological Chemistry

142

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Background: Assembly of the cytoskeletal protein FtsZ into a loose bundle of filaments at the nascent septum initiates bacterial cell division. Results: The extreme C terminus of FtsZ mediates electrostatic interactions between FtsZ polymers. Conclusion: The FtsZ C terminus promotes lateral interactions in vitro and ensures efficient division in vivo. Significance: The extreme C terminus of FtsZ plays a role to promote its own stabilization.

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“…ZipA, another FtsZinteracting protein present in Gammaproteobacteria, is also a membrane-anchored protein that promotes FtsZ ring assembly (26,41). ZapA is a positive regulator of FtsZ ring assembly and stability, and SepF is required for proper septum formation (24,28,32). ZapB is a novel factor that concurrently stimulates FtsZ ring assembly and cell division (21).…”

mentioning

confidence: 99%

Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes

et al. 2011

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A new FtsZ‐interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis

Cited by 139 publications

References 58 publications

The functional analysis of YabA, which interacts with DnaA and regulates initiation of chromosome replication in Bacillus subtils

The functional analysis of YabA, which interacts with DnaA and regulates initiation of chromosome replication in Bacillus subtils

Extreme C Terminus of Bacterial Cytoskeletal Protein FtsZ Plays Fundamental Role in Assembly Independent of Modulatory Proteins

Characterization of CrgA, a New Partner of the Mycobacterium tuberculosis Peptidoglycan Polymerization Complexes

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