Crossref journal-article
Wiley
Molecular Microbiology (311)
Abstract

The cell division protein FtsZ is a GTPase structurally related to tubulin and, like tubulin, it assembles in vitro into filaments, sheets and other structures. To study the roles that GTP binding and hydrolysis play in the dynamics of FtsZ polymerization, the nucleotide contents of FtsZ were measured under different polymerizing conditions using a nitrocellulose filter‐binding assay, whereas polymerization of the protein was followed in parallel by light scattering. Unpolymerized FtsZ bound 1 mol of GTP mol−1 protein monomer. At pH 7.5 and in the presence of Mg2+ and K+, there was a strong GTPase activity; most of the bound nucleotide was GTP during the first few minutes but, later, the amount of GTP decreased in parallel with depolymerization, whereas the total nucleotide contents remained invariant. These results show that the long FtsZ polymers formed in solution contain mostly GTP. Incorporation of nucleotides into the protein was very fast either when the label was introduced at the onset of the reaction or subsequently during polymerization. Molecular modelling of an FtsZ dimer showed the presence of a cleft between the two subunits maintaining the nucleotide binding site open to the medium. These results show that the FtsZ polymers are highly dynamic structures that quickly exchange the bound nucleotide, and this exchange can occur in all the subunits.

Bibliography

Mingorance, J., Rueda, S., Gómez‐Puertas, P., Valencia, A., & Vicente, M. (2001). Escherichia coli FtsZ polymers contain mostly GTP and have a high nucleotide turnover. Molecular Microbiology, 41(1), 83–91. Portico.

Authors 5
  1. Jesús Mingorance (first)
  2. Sonsoles Rueda (additional)
  3. Paulino Gómez‐Puertas (additional)
  4. Alfonso Valencia (additional)
  5. Miguel Vicente (additional)
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Dates
Type When
Created 22 years, 5 months ago (March 12, 2003, 6:38 a.m.)
Deposited 1 year, 10 months ago (Oct. 17, 2023, 3:29 p.m.)
Indexed 3 weeks, 2 days ago (July 30, 2025, 8:22 p.m.)
Issued 24 years, 1 month ago (July 1, 2001)
Published 24 years, 1 month ago (July 1, 2001)
Published Online 23 years, 8 months ago (Dec. 21, 2001)
Published Print 24 years, 1 month ago (July 1, 2001)
Funders 0

None

@article{Mingorance_2001, title={Escherichia coli FtsZ polymers contain mostly GTP and have a high nucleotide turnover}, volume={41}, ISSN={1365-2958}, url={http://dx.doi.org/10.1046/j.1365-2958.2001.02498.x}, DOI={10.1046/j.1365-2958.2001.02498.x}, number={1}, journal={Molecular Microbiology}, publisher={Wiley}, author={Mingorance, Jesús and Rueda, Sonsoles and Gómez‐Puertas, Paulino and Valencia, Alfonso and Vicente, Miguel}, year={2001}, month=jul, pages={83–91} }