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FtsZ ring in bacterial cytokinesis
1Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City 66103.
Molecular Microbiology
|August 1, 1993
Summary
The bacterial cell division protein FtsZ self-assembles into a ring, initiating septum formation. This process, involving membrane and cell wall invagination, may be conserved across bacteria and shares similarities with tubulin.
Area of Science:
- Microbiology
- Cell Biology
- Biochemistry
Background:
- FtsZ protein is crucial for bacterial cell division, localizing to a ring at the division site.
- Understanding the mechanism of FtsZ assembly is key to comprehending bacterial cytokinesis.
Purpose of the Study:
- To present a model for FtsZ self-assembly and ring formation during bacterial cell division.
- To explore the coordination of membrane and cell wall invagination by the FtsZ ring.
- To discuss the potential conservation of this process in peptidoglycan-containing eubacteria and compare FtsZ to tubulin.
Main Methods:
- This review discusses a proposed model for FtsZ function.
- Comparative analysis of FtsZ and tubulin.
Main Results:
- The model posits that FtsZ self-assembles into a ring at a membrane nucleation site under cell-cycle control.
- This FtsZ ring formation initiates and coordinates the invagination of the cytoplasmic membrane and cell wall to form the septum.
- Similarities between FtsZ and tubulin are highlighted.
Conclusions:
- The FtsZ ring model provides a framework for understanding bacterial cytokinesis.
- The FtsZ-mediated septation process is potentially conserved in eubacteria.
- FtsZ shares functional and possibly structural similarities with eukaryotic tubulin, suggesting evolutionary links.