ZipA and FtsA* stabilize FtsZ-GDP miniring structures.

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The cytokinetic division ring of Escherichia coli comprises filaments of FtsZ tethered to the membrane by FtsA and ZipA. Previous results suggested that ZipA is a Z-ring stabilizer, since in vitro experiments it is shown that ZipA enhanced FtsZ assembly and caused the filaments to bundles. However, this function of ZipA has been challenged by recent studies. First, ZipA-induced FtsZ bundling was not significant at pH greater than 7. Second, some FtsA mutants, such as FtsA* were able to bypass the need of ZipA. We reinvestigated the interaction of FtsZ with ZipA in vitro. We found that ZipA not only stabilized and bundled straight filaments of FtsZ-GTP, but also stabilized the highly curved filaments and miniring structures formed by FtsZ-GDP. FtsA* had a similar stabilization of FtsZ-GDP minirings. Our results suggest that ZipA and FtsA* may contribute to constriction by stabilizing this miniring conformation.






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Chen, Yaodong, Haiyan Huang, Masaki Osawa and Harold P Erickson (2017). ZipA and FtsA* stabilize FtsZ-GDP miniring structures. Sci Rep, 7(1). p. 3650. 10.1038/s41598-017-03983-4 Retrieved from

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Masaki Osawa

Assistant Research Professor of Cell Biology

Harold Paul Erickson

James B. Duke Distinguished Professor Emeritus

Recent research has been on cytoskeleton (eukaryotes and bacteria); a skirmish to debunk the irisin story; a reinterpretation of proposed multivalent binders of the coronavirus spike protein. I have also published an ebook on "Principles of Protein-Protein Association" suitable for a course module or individual learning.

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