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RodZ: a key-player in cell elongation and cell division in Escherichia coli

RodZ is required for determination of cell shape in rod-shaped bacterium, such as Escherichia coli. RodZ is a transmembrane protein and forms a supramolecular complex called the Rod complex with other proteins, such as MreB-actin and peptidoglycan synthesis enzymes (for e.g., PBP2). Deletion of the...

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Detalles Bibliográficos
Autores principales: Ago, Risa, Shiomi, Daisuke
Formato: Online Artículo Texto
Lenguaje:English
Publicado: AIMS Press 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6946637/
https://www.ncbi.nlm.nih.gov/pubmed/31915748
http://dx.doi.org/10.3934/microbiol.2019.4.358
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author Ago, Risa
Shiomi, Daisuke
author_facet Ago, Risa
Shiomi, Daisuke
author_sort Ago, Risa
collection PubMed
description RodZ is required for determination of cell shape in rod-shaped bacterium, such as Escherichia coli. RodZ is a transmembrane protein and forms a supramolecular complex called the Rod complex with other proteins, such as MreB-actin and peptidoglycan synthesis enzymes (for e.g., PBP2). Deletion of the rodZ gene changes the cell shape from rod to round or ovoid. Another supramolecular complex called divisome that controls cell division mainly consists of FtsZ-tubulin. MreB directly interacts with FtsZ and this interaction is critical to trigger a transition from cell elongation to cell division. Recently, we found that RodZ also directly interacts with FtsZ, and RodZ recruits MreB to the divisome. Formation of the division ring, called Z ring, is delayed if RodZ does not interact with FtsZ, indicating that RodZ might facilitate the formation of the Z ring during the cell division process. In this mini-review, we have summarized the roles of RodZ in cell elongation and cell division, especially based on our recent study.
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spelling pubmed-69466372020-01-08 RodZ: a key-player in cell elongation and cell division in Escherichia coli Ago, Risa Shiomi, Daisuke AIMS Microbiol Mini Review RodZ is required for determination of cell shape in rod-shaped bacterium, such as Escherichia coli. RodZ is a transmembrane protein and forms a supramolecular complex called the Rod complex with other proteins, such as MreB-actin and peptidoglycan synthesis enzymes (for e.g., PBP2). Deletion of the rodZ gene changes the cell shape from rod to round or ovoid. Another supramolecular complex called divisome that controls cell division mainly consists of FtsZ-tubulin. MreB directly interacts with FtsZ and this interaction is critical to trigger a transition from cell elongation to cell division. Recently, we found that RodZ also directly interacts with FtsZ, and RodZ recruits MreB to the divisome. Formation of the division ring, called Z ring, is delayed if RodZ does not interact with FtsZ, indicating that RodZ might facilitate the formation of the Z ring during the cell division process. In this mini-review, we have summarized the roles of RodZ in cell elongation and cell division, especially based on our recent study. AIMS Press 2019-11-07 /pmc/articles/PMC6946637/ /pubmed/31915748 http://dx.doi.org/10.3934/microbiol.2019.4.358 Text en © 2019 the Author(s), licensee AIMS Press This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0)
spellingShingle Mini Review
Ago, Risa
Shiomi, Daisuke
RodZ: a key-player in cell elongation and cell division in Escherichia coli
title RodZ: a key-player in cell elongation and cell division in Escherichia coli
title_full RodZ: a key-player in cell elongation and cell division in Escherichia coli
title_fullStr RodZ: a key-player in cell elongation and cell division in Escherichia coli
title_full_unstemmed RodZ: a key-player in cell elongation and cell division in Escherichia coli
title_short RodZ: a key-player in cell elongation and cell division in Escherichia coli
title_sort rodz: a key-player in cell elongation and cell division in escherichia coli
topic Mini Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6946637/
https://www.ncbi.nlm.nih.gov/pubmed/31915748
http://dx.doi.org/10.3934/microbiol.2019.4.358
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