Free SepF interferes with recruitment of late cell division proteins

Abstract The conserved cell division protein SepF aligns polymers of FtsZ, the key cell division protein in bacteria, during synthesis of the (Fts)Z-ring at midcell, the first stage in cytokinesis. In addition, SepF acts as a membrane anchor for the Z-ring. Recently, it was shown that SepF overexpre...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Yongqiang Gao, Michaela Wenzel, Martijs J. Jonker, Leendert W. Hamoen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/569eec12e463423998eb20c4d829d865
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:569eec12e463423998eb20c4d829d865
record_format	dspace
spelling	oai:doaj.org-article:569eec12e463423998eb20c4d829d8652021-12-02T15:06:15ZFree SepF interferes with recruitment of late cell division proteins10.1038/s41598-017-17155-x2045-2322https://doaj.org/article/569eec12e463423998eb20c4d829d8652017-12-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-17155-xhttps://doaj.org/toc/2045-2322Abstract The conserved cell division protein SepF aligns polymers of FtsZ, the key cell division protein in bacteria, during synthesis of the (Fts)Z-ring at midcell, the first stage in cytokinesis. In addition, SepF acts as a membrane anchor for the Z-ring. Recently, it was shown that SepF overexpression in Mycobacterium smegmatis blocks cell division. Why this is the case is not known. Surprisingly, we found in Bacillus subtilis that SepF overproduction does not interfere with Z-ring assembly, but instead blocks assembly of late division proteins responsible for septum synthesis. Transposon mutagenesis suggested that SepF overproduction suppresses the essential WalRK two-component system, which stimulates expression of ftsZ. Indeed, it emerged that SepF overproduction impairs normal WalK localization. However, transcriptome analysis showed that the WalRK activity was in fact not reduced in SepF overexpressing cells. Further experiments indicated that SepF competes with EzrA and FtsA for binding to FtsZ, and that binding of extra SepF by FtsZ alleviates the cell division defect. This may explain why activation of WalRK in the transposon mutant, which increases ftsZ expression, counteracts the division defect. In conclusion, our data shows that an imbalance in early cell division proteins can interfere with recruitment of late cell division proteins.Yongqiang GaoMichaela WenzelMartijs J. JonkerLeendert W. HamoenNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-18 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yongqiang Gao Michaela Wenzel Martijs J. Jonker Leendert W. Hamoen Free SepF interferes with recruitment of late cell division proteins
description	Abstract The conserved cell division protein SepF aligns polymers of FtsZ, the key cell division protein in bacteria, during synthesis of the (Fts)Z-ring at midcell, the first stage in cytokinesis. In addition, SepF acts as a membrane anchor for the Z-ring. Recently, it was shown that SepF overexpression in Mycobacterium smegmatis blocks cell division. Why this is the case is not known. Surprisingly, we found in Bacillus subtilis that SepF overproduction does not interfere with Z-ring assembly, but instead blocks assembly of late division proteins responsible for septum synthesis. Transposon mutagenesis suggested that SepF overproduction suppresses the essential WalRK two-component system, which stimulates expression of ftsZ. Indeed, it emerged that SepF overproduction impairs normal WalK localization. However, transcriptome analysis showed that the WalRK activity was in fact not reduced in SepF overexpressing cells. Further experiments indicated that SepF competes with EzrA and FtsA for binding to FtsZ, and that binding of extra SepF by FtsZ alleviates the cell division defect. This may explain why activation of WalRK in the transposon mutant, which increases ftsZ expression, counteracts the division defect. In conclusion, our data shows that an imbalance in early cell division proteins can interfere with recruitment of late cell division proteins.
format	article
author	Yongqiang Gao Michaela Wenzel Martijs J. Jonker Leendert W. Hamoen
author_facet	Yongqiang Gao Michaela Wenzel Martijs J. Jonker Leendert W. Hamoen
author_sort	Yongqiang Gao
title	Free SepF interferes with recruitment of late cell division proteins
title_short	Free SepF interferes with recruitment of late cell division proteins
title_full	Free SepF interferes with recruitment of late cell division proteins
title_fullStr	Free SepF interferes with recruitment of late cell division proteins
title_full_unstemmed	Free SepF interferes with recruitment of late cell division proteins
title_sort	free sepf interferes with recruitment of late cell division proteins
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/569eec12e463423998eb20c4d829d865
work_keys_str_mv	AT yongqianggao freesepfinterfereswithrecruitmentoflatecelldivisionproteins AT michaelawenzel freesepfinterfereswithrecruitmentoflatecelldivisionproteins AT martijsjjonker freesepfinterfereswithrecruitmentoflatecelldivisionproteins AT leendertwhamoen freesepfinterfereswithrecruitmentoflatecelldivisionproteins
_version_	1718388512461422592

Free SepF interferes with recruitment of late cell division proteins

Ejemplares similares