Cell division protein CdpA organises and anchors the midcell ring in haloarchaea

Abstract Many archaea appear to divide through the coordinated activities of two FtsZ homologues (FtsZ1 and FtsZ2) and another bacterial cell division homologue (SepF), which are part of the midcell division ring. Here, we identify an additional protein (HVO_0739, renamed CdpA) that is involved in c...

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Main Authors: Yan Liao, Vinaya D. Shinde, Dalong Hu, Zhuang Xu, Bill Söderström, Katharine A. Michie, Iain G. Duggin
Format: Article
Language:English
Published: Nature Portfolio 2025-05-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-025-60079-8
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author Yan Liao
Vinaya D. Shinde
Dalong Hu
Zhuang Xu
Bill Söderström
Katharine A. Michie
Iain G. Duggin
author_facet Yan Liao
Vinaya D. Shinde
Dalong Hu
Zhuang Xu
Bill Söderström
Katharine A. Michie
Iain G. Duggin
author_sort Yan Liao
collection DOAJ
description Abstract Many archaea appear to divide through the coordinated activities of two FtsZ homologues (FtsZ1 and FtsZ2) and another bacterial cell division homologue (SepF), which are part of the midcell division ring. Here, we identify an additional protein (HVO_0739, renamed CdpA) that is involved in cell division in Haloferax volcanii, with homologues in other Haloarchaea. CdpA localises at the midcell division ring, and this requires the presence of the ring-assembly protein FtsZ1. The division constriction protein FtsZ2 also influences the proper midcell assembly and structure of CdpA. In the absence of CdpA, cells frequently fail to divide properly, and FtsZ1 formed poorly condensed pseudo-helical structures spanning across a broad region of the cell, whereas FtsZ2 showed mispositioned foci, nano-rings, and filaments. The rate of directional movement of FtsZ1 and FtsZ2 structures around the division ring appears minimally affected by loss of CdpA, which resulted in continual repositioning of the aberrant FtsZ structures in the cells. In contrast to the FtsZ proteins, CdpA formed relatively immobile foci around the ring. Protein domain function studies, pull-down assays, and multimer structure predictions suggest that CdpA is part of a membrane complex that tethers FtsZ2 and other division proteins to the midcell membrane. Our discovery of an archaeal FtsZ organisation and midcell anchor protein offers new insights into cell division mechanisms that are similar across the tree of life.
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spelling doaj-art-8761f7b5664b4b87bad19c3081a4e0da2025-08-20T03:16:55ZengNature PortfolioNature Communications2041-17232025-05-0116111710.1038/s41467-025-60079-8Cell division protein CdpA organises and anchors the midcell ring in haloarchaeaYan Liao0Vinaya D. Shinde1Dalong Hu2Zhuang Xu3Bill Söderström4Katharine A. Michie5Iain G. Duggin6Australian Institute for Microbiology and Infection, University of Technology SydneyAustralian Institute for Microbiology and Infection, University of Technology SydneyAustralian Institute for Microbiology and Infection, University of Technology SydneySchool of Mathematics and Statistics, The University of New South WalesAustralian Institute for Microbiology and Infection, University of Technology SydneyStructural Biology Facility, Mark Wainwright Analytical Centre, The University of New South WalesAustralian Institute for Microbiology and Infection, University of Technology SydneyAbstract Many archaea appear to divide through the coordinated activities of two FtsZ homologues (FtsZ1 and FtsZ2) and another bacterial cell division homologue (SepF), which are part of the midcell division ring. Here, we identify an additional protein (HVO_0739, renamed CdpA) that is involved in cell division in Haloferax volcanii, with homologues in other Haloarchaea. CdpA localises at the midcell division ring, and this requires the presence of the ring-assembly protein FtsZ1. The division constriction protein FtsZ2 also influences the proper midcell assembly and structure of CdpA. In the absence of CdpA, cells frequently fail to divide properly, and FtsZ1 formed poorly condensed pseudo-helical structures spanning across a broad region of the cell, whereas FtsZ2 showed mispositioned foci, nano-rings, and filaments. The rate of directional movement of FtsZ1 and FtsZ2 structures around the division ring appears minimally affected by loss of CdpA, which resulted in continual repositioning of the aberrant FtsZ structures in the cells. In contrast to the FtsZ proteins, CdpA formed relatively immobile foci around the ring. Protein domain function studies, pull-down assays, and multimer structure predictions suggest that CdpA is part of a membrane complex that tethers FtsZ2 and other division proteins to the midcell membrane. Our discovery of an archaeal FtsZ organisation and midcell anchor protein offers new insights into cell division mechanisms that are similar across the tree of life.https://doi.org/10.1038/s41467-025-60079-8
spellingShingle Yan Liao
Vinaya D. Shinde
Dalong Hu
Zhuang Xu
Bill Söderström
Katharine A. Michie
Iain G. Duggin
Cell division protein CdpA organises and anchors the midcell ring in haloarchaea
Nature Communications
title Cell division protein CdpA organises and anchors the midcell ring in haloarchaea
title_full Cell division protein CdpA organises and anchors the midcell ring in haloarchaea
title_fullStr Cell division protein CdpA organises and anchors the midcell ring in haloarchaea
title_full_unstemmed Cell division protein CdpA organises and anchors the midcell ring in haloarchaea
title_short Cell division protein CdpA organises and anchors the midcell ring in haloarchaea
title_sort cell division protein cdpa organises and anchors the midcell ring in haloarchaea
url https://doi.org/10.1038/s41467-025-60079-8
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