FtsZ Protofilament Curvature Is the Opposite of Tubulin Rings.
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FtsZ protofilaments (pfs) form the bacterial cytokinetic Z ring. Previous work suggested that a conformational change from straight to curved pfs generated the constriction force. In the simplest model, the C-terminal membrane tether is on the outside of the curved pf, facing the membrane. Tubulin, a homologue of FtsZ, also forms pfs with a curved conformation. However, it is well-established that tubulin rings have the C terminus on the inside of the ring. Could FtsZ and tubulin rings have the opposite curvature? In this study, we explored the FtsZ curvature direction by fusing large protein tags to the FtsZ termini. Thin section electron microscopy showed that the C-terminal tag was on the outside, consistent with the bending pf model. This has interesting implications for the evolution of tubulin. Tubulin likely began with the curvature of FtsZ, but evolution managed to reverse direction to produce outward-curving rings, which are useful for pulling chromosomes.
Escherichia coli Proteins
Published Version (Please cite this version)10.1021/acs.biochem.6b00479
Publication InfoErickson, Harold Paul; Housman, Max; Milam, Sara L; Moore, Desmond A; & Osawa, Masaki (2016). FtsZ Protofilament Curvature Is the Opposite of Tubulin Rings. Biochemistry, 55(29). 10.1021/acs.biochem.6b00479. Retrieved from https://hdl.handle.net/10161/16450.
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James B. Duke Professor of Cell Biology
Cytoskeleton: It is now clear that the actin and microtubule cytoskeleton originated in bacteria. Our major research is on FtsZ, the bacterial tubulin homolog, which assembles into a contractile ring that divides the bacterium. We have studied FtsZ assembly in vitro, and found that it assembles into thin protofilaments (pfs). Dozens of these pfs are further clustered to form the contractile Z-ring in vivo. Some important discoveries in the last ten years include: &bul
Assistant Research Professor of Cell Biology
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