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- W2474169912 abstract "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." @default.
- W2474169912 created "2016-07-22" @default.
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- W2474169912 date "2016-07-14" @default.
- W2474169912 modified "2023-10-06" @default.
- W2474169912 title "FtsZ Protofilament Curvature Is the Opposite of Tubulin Rings" @default.
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- W2474169912 doi "https://doi.org/10.1021/acs.biochem.6b00479" @default.
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