ARC6-mediated Z ring-like structure formation of prokaryote-descended chloroplast FtsZ in Escherichia coli

Abstract Plant chloroplasts proliferate through binary fission, and the stromal-side molecules that are involved in chloroplast division are bacterial derivatives. As in bacteria, the prokaryotic tubulin homolog FtsZ assembles into a ring-like structure (Z ring) at mid-chloroplast, and this process...

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Autores principales:	Hiroki Irieda, Daisuke Shiomi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/b1e97a8072c3459f88d9bedabb7b00b2
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spelling	oai:doaj.org-article:b1e97a8072c3459f88d9bedabb7b00b22021-12-02T12:30:42ZARC6-mediated Z ring-like structure formation of prokaryote-descended chloroplast FtsZ in Escherichia coli10.1038/s41598-017-03698-62045-2322https://doaj.org/article/b1e97a8072c3459f88d9bedabb7b00b22017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-03698-6https://doaj.org/toc/2045-2322Abstract Plant chloroplasts proliferate through binary fission, and the stromal-side molecules that are involved in chloroplast division are bacterial derivatives. As in bacteria, the prokaryotic tubulin homolog FtsZ assembles into a ring-like structure (Z ring) at mid-chloroplast, and this process is followed by constriction. However, the properties of chloroplast FtsZs remain unclarified. Here, we employed Escherichia coli as a novel heterologous system for expressing chloroplast FtsZs and their regulatory components. Fluorescently labelled Arabidopsis FtsZ2 efficiently assembled into long filaments in E. coli cells, and artificial membrane tethering conferred FtsZ2 filaments with the ability to form Z ring-like structures resembling the bacterial Z ring. A negative regulator of chloroplast FtsZ assembly, ARC3, retained its inhibitory effects on FtsZ2 filamentation and Z ring-like structure formation in E. coli cells. Thus, we provide a novel heterologous system by using bacterial cells to study the regulation of the chloroplast divisome. Furthermore, we demonstrated that the FtsZ2-interacting protein ARC6, which is a potential candidate for Z ring tethering to the chloroplast inner envelope membrane, genuinely targeted FtsZ2 to the membrane components and supported its morphological shift from linear filaments to Z ring-like structures in a manner dependent on the C-terminal ARC6-interacting domain of FtsZ2.Hiroki IriedaDaisuke ShiomiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Hiroki Irieda Daisuke Shiomi ARC6-mediated Z ring-like structure formation of prokaryote-descended chloroplast FtsZ in Escherichia coli
description	Abstract Plant chloroplasts proliferate through binary fission, and the stromal-side molecules that are involved in chloroplast division are bacterial derivatives. As in bacteria, the prokaryotic tubulin homolog FtsZ assembles into a ring-like structure (Z ring) at mid-chloroplast, and this process is followed by constriction. However, the properties of chloroplast FtsZs remain unclarified. Here, we employed Escherichia coli as a novel heterologous system for expressing chloroplast FtsZs and their regulatory components. Fluorescently labelled Arabidopsis FtsZ2 efficiently assembled into long filaments in E. coli cells, and artificial membrane tethering conferred FtsZ2 filaments with the ability to form Z ring-like structures resembling the bacterial Z ring. A negative regulator of chloroplast FtsZ assembly, ARC3, retained its inhibitory effects on FtsZ2 filamentation and Z ring-like structure formation in E. coli cells. Thus, we provide a novel heterologous system by using bacterial cells to study the regulation of the chloroplast divisome. Furthermore, we demonstrated that the FtsZ2-interacting protein ARC6, which is a potential candidate for Z ring tethering to the chloroplast inner envelope membrane, genuinely targeted FtsZ2 to the membrane components and supported its morphological shift from linear filaments to Z ring-like structures in a manner dependent on the C-terminal ARC6-interacting domain of FtsZ2.
format	article
author	Hiroki Irieda Daisuke Shiomi
author_facet	Hiroki Irieda Daisuke Shiomi
author_sort	Hiroki Irieda
title	ARC6-mediated Z ring-like structure formation of prokaryote-descended chloroplast FtsZ in Escherichia coli
title_short	ARC6-mediated Z ring-like structure formation of prokaryote-descended chloroplast FtsZ in Escherichia coli
title_full	ARC6-mediated Z ring-like structure formation of prokaryote-descended chloroplast FtsZ in Escherichia coli
title_fullStr	ARC6-mediated Z ring-like structure formation of prokaryote-descended chloroplast FtsZ in Escherichia coli
title_full_unstemmed	ARC6-mediated Z ring-like structure formation of prokaryote-descended chloroplast FtsZ in Escherichia coli
title_sort	arc6-mediated z ring-like structure formation of prokaryote-descended chloroplast ftsz in escherichia coli
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/b1e97a8072c3459f88d9bedabb7b00b2
work_keys_str_mv	AT hirokiirieda arc6mediatedzringlikestructureformationofprokaryotedescendedchloroplastftszinescherichiacoli AT daisukeshiomi arc6mediatedzringlikestructureformationofprokaryotedescendedchloroplastftszinescherichiacoli
_version_	1718394355358629888

ARC6-mediated Z ring-like structure formation of prokaryote-descended chloroplast FtsZ in Escherichia coli

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