ZapC promotes assembly and stability of FtsZ filaments by binding at a different site on FtsZ than ZipA.
ZapC, a component of the divisome in Escherichia coli, is known to co-localize with FtsZ at the mid-cell position. A deletion or an overexpression of ZapC has been found to induce elongation of bacterial cells implying a role of ZapC in the cell division. ZapC has also been shown to enhance the assembly of purified FtsZ. In this study, ZapC was found to prevent the dilution-induced disassembly of preformed FtsZ polymers and to decorate FtsZ protofilaments along the length. ZapC interacted with FtsZ with a dissociation constant of 30±7nM. Salt had no discernable effect on the binding of ZapC to FtsZ; however, bis-ANS inhibited the binding of ZapC to FtsZ suggesting that the interaction was predominantly hydrophobic in nature. Several of the positive regulators of FtsZ assembly including ZipA are shown to bind FtsZ at the C-terminal tail of FtsZ. Using a 12-residue C-terminal tail peptide (LDIPAFLRKQAD) of FtsZ and a C-terminal tail truncated FtsZ construct, we provided data suggesting that ZapC does not bind at the C-terminal tail of FtsZ. The results indicated that ZapC and ZipA, two functionally similar proteins of the divisome complex, regulate FtsZ assembly through different sites of action on FtsZ.
Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai 400076, India.
Anusri
A
Bhattacharya
Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai 400076, India.
Shashikant
S
Ray
Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai 400076, India.
Dipty
D
Singh
Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai 400076, India.
Hemendra Pal Singh
HP
Dhaked
Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai 400076, India. Electronic address: panda@iitb.ac.in.
Dulal
D
Panda
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000378:metabolism*; D003598:Cytoskeletal Proteins / Q000737:chemistry* / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D055550:Protein Stability
D001426:Bacterial Proteins; D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; C071525:FtsZ protein, Bacteria; C557498:ZapC protein, E coli; C103795:ZipA protein, E coli
Accessory proteins; Bis-ANS; C-terminal tail of FtsZ; FtsZ assembly; ZapC; ZipA