ZipA and FtsA* stabilize FtsZ-GDP miniring structures.

Loading...
Thumbnail Image

Date

2017-06-16

Journal Title

Journal ISSN

Volume Title

Repository Usage Stats

209
views
174
downloads

Citation Stats

Abstract

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.

Department

Description

Provenance

Subjects

Citation

Published Version (Please cite this version)

10.1038/s41598-017-03983-4

Publication Info

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 https://hdl.handle.net/10161/14967.

This is constructed from limited available data and may be imprecise. To cite this article, please review & use the official citation provided by the journal.

Scholars@Duke

Erickson

Harold Paul Erickson

James B. Duke Distinguished Professor Emeritus of Cell Biology

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.


Unless otherwise indicated, scholarly articles published by Duke faculty members are made available here with a CC-BY-NC (Creative Commons Attribution Non-Commercial) license, as enabled by the Duke Open Access Policy. If you wish to use the materials in ways not already permitted under CC-BY-NC, please consult the copyright owner. Other materials are made available here through the author’s grant of a non-exclusive license to make their work openly accessible.