ZipA and FtsA* stabilize FtsZ-GDP miniring structures

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....

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Autores principales: Yaodong Chen, Haiyan Huang, Masaki Osawa, Harold P. Erickson
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Publicado: Nature Portfolio 2017
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spelling oai:doaj.org-article:16b42d13f92846d8898a352de1dd6d642021-12-02T16:06:03ZZipA and FtsA* stabilize FtsZ-GDP miniring structures10.1038/s41598-017-03983-42045-2322https://doaj.org/article/16b42d13f92846d8898a352de1dd6d642017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-03983-4https://doaj.org/toc/2045-2322Abstract 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.Yaodong ChenHaiyan HuangMasaki OsawaHarold P. EricksonNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Yaodong Chen
Haiyan Huang
Masaki Osawa
Harold P. Erickson
ZipA and FtsA* stabilize FtsZ-GDP miniring structures
description 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.
format article
author Yaodong Chen
Haiyan Huang
Masaki Osawa
Harold P. Erickson
author_facet Yaodong Chen
Haiyan Huang
Masaki Osawa
Harold P. Erickson
author_sort Yaodong Chen
title ZipA and FtsA* stabilize FtsZ-GDP miniring structures
title_short ZipA and FtsA* stabilize FtsZ-GDP miniring structures
title_full ZipA and FtsA* stabilize FtsZ-GDP miniring structures
title_fullStr ZipA and FtsA* stabilize FtsZ-GDP miniring structures
title_full_unstemmed ZipA and FtsA* stabilize FtsZ-GDP miniring structures
title_sort zipa and ftsa* stabilize ftsz-gdp miniring structures
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/16b42d13f92846d8898a352de1dd6d64
work_keys_str_mv AT yaodongchen zipaandftsastabilizeftszgdpminiringstructures
AT haiyanhuang zipaandftsastabilizeftszgdpminiringstructures
AT masakiosawa zipaandftsastabilizeftszgdpminiringstructures
AT haroldperickson zipaandftsastabilizeftszgdpminiringstructures
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