FtsZ placement in nucleoid-free bacteria.

We describe the placement of the cytoplasmic FtsZ protein, an essential component of the division septum, in nucleoid-free Escherichia coli maxicells. The absence of the nucleoid is accompanied in maxicells by degradation of the SlmA protein. This protein, together with the nucleoid, prevents the pl...

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Autores principales:	Manuel Pazos, Mercedes Casanova, Pilar Palacios, William Margolin, Paolo Natale, Miguel Vicente
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2eb440b469ed45079f493550d61e9f8f
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spelling	oai:doaj.org-article:2eb440b469ed45079f493550d61e9f8f2021-11-18T08:27:40ZFtsZ placement in nucleoid-free bacteria.1932-620310.1371/journal.pone.0091984https://doaj.org/article/2eb440b469ed45079f493550d61e9f8f2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24638110/?tool=EBIhttps://doaj.org/toc/1932-6203We describe the placement of the cytoplasmic FtsZ protein, an essential component of the division septum, in nucleoid-free Escherichia coli maxicells. The absence of the nucleoid is accompanied in maxicells by degradation of the SlmA protein. This protein, together with the nucleoid, prevents the placement of the septum in the regions occupied by the chromosome by a mechanism called nucleoid occlusion (NO). A second septum placement mechanism, the MinCDE system (Min) involving a pole-to-pole oscillation of three proteins, nonetheless remains active in maxicells. Both Min and NO act on the polymerization of FtsZ, preventing its assembly into an FtsZ-ring except at midcell. Our results show that even in the total absence of NO, Min oscillations can direct placement of FtsZ in maxicells. Deletion of the FtsZ carboxyl terminal domain (FtsZ), a central hub that receives signals from a variety of proteins including MinC, FtsA and ZipA, produces a Min-insensitive form of FtsZ unable to interact with the membrane-anchoring FtsA and ZipA proteins. This protein produces a totally disorganized pattern of FtsZ localization inside the maxicell cytoplasm. In contrast, FtsZ-VM, an artificially cytoplasmic membrane-anchored variant of FtsZ*, forms helical or repetitive ring structures distributed along the entire length of maxicells even in the absence of NO. These results show that membrane anchoring is needed to organize FtsZ into rings and underscore the role of the C-terminal hub of FtsZ for their correct placement.Manuel PazosMercedes CasanovaPilar PalaciosWilliam MargolinPaolo NataleMiguel VicentePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 3, p e91984 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Manuel Pazos Mercedes Casanova Pilar Palacios William Margolin Paolo Natale Miguel Vicente FtsZ placement in nucleoid-free bacteria.
description	We describe the placement of the cytoplasmic FtsZ protein, an essential component of the division septum, in nucleoid-free Escherichia coli maxicells. The absence of the nucleoid is accompanied in maxicells by degradation of the SlmA protein. This protein, together with the nucleoid, prevents the placement of the septum in the regions occupied by the chromosome by a mechanism called nucleoid occlusion (NO). A second septum placement mechanism, the MinCDE system (Min) involving a pole-to-pole oscillation of three proteins, nonetheless remains active in maxicells. Both Min and NO act on the polymerization of FtsZ, preventing its assembly into an FtsZ-ring except at midcell. Our results show that even in the total absence of NO, Min oscillations can direct placement of FtsZ in maxicells. Deletion of the FtsZ carboxyl terminal domain (FtsZ), a central hub that receives signals from a variety of proteins including MinC, FtsA and ZipA, produces a Min-insensitive form of FtsZ unable to interact with the membrane-anchoring FtsA and ZipA proteins. This protein produces a totally disorganized pattern of FtsZ localization inside the maxicell cytoplasm. In contrast, FtsZ-VM, an artificially cytoplasmic membrane-anchored variant of FtsZ*, forms helical or repetitive ring structures distributed along the entire length of maxicells even in the absence of NO. These results show that membrane anchoring is needed to organize FtsZ into rings and underscore the role of the C-terminal hub of FtsZ for their correct placement.
format	article
author	Manuel Pazos Mercedes Casanova Pilar Palacios William Margolin Paolo Natale Miguel Vicente
author_facet	Manuel Pazos Mercedes Casanova Pilar Palacios William Margolin Paolo Natale Miguel Vicente
author_sort	Manuel Pazos
title	FtsZ placement in nucleoid-free bacteria.
title_short	FtsZ placement in nucleoid-free bacteria.
title_full	FtsZ placement in nucleoid-free bacteria.
title_fullStr	FtsZ placement in nucleoid-free bacteria.
title_full_unstemmed	FtsZ placement in nucleoid-free bacteria.
title_sort	ftsz placement in nucleoid-free bacteria.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/2eb440b469ed45079f493550d61e9f8f
work_keys_str_mv	AT manuelpazos ftszplacementinnucleoidfreebacteria AT mercedescasanova ftszplacementinnucleoidfreebacteria AT pilarpalacios ftszplacementinnucleoidfreebacteria AT williammargolin ftszplacementinnucleoidfreebacteria AT paolonatale ftszplacementinnucleoidfreebacteria AT miguelvicente ftszplacementinnucleoidfreebacteria
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FtsZ placement in nucleoid-free bacteria.

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