Nano-encapsulated Escherichia coli Divisome Anchor ZipA, and in Complex with FtsZ

Sarah C. Lee; Richard Collins; Yu-pin Lin; Mohammed Jamshad; Claire Broughton; Sarah A. Harris; Benjamin S Hanson; Cecilia Tognoloni; Rosemary A. Parslow; Ann E. Terry; Alison Rodger; Corinne J. Smith; Karen J. Edler; Robert Ford; David I. Roper; Timothy R. Dafforn

doi:10.1038/s41598-019-54999-x

Nano-encapsulated Escherichia coli Divisome Anchor ZipA, and in Complex with FtsZ

Sarah C. Lee, Richard Collins, Yu-pin Lin, Mohammed Jamshad, Claire Broughton, Sarah A. Harris, Benjamin S Hanson, Cecilia Tognoloni, Rosemary A. Parslow, Ann E. Terry, Alison Rodger, Corinne J. Smith, Karen J. Edler, Robert Ford, David I. Roper, Timothy R. Dafforn

Research output: Contribution to journal › Article › peer-review

16 Citations (SciVal)

Abstract

The E. coli membrane protein ZipA, binds to the tubulin homologue FtsZ, in the early stage of cell division. We isolated ZipA in a Styrene Maleic Acid lipid particle (SMALP) preserving its position and integrity with native E. coli membrane lipids. Direct binding of ZipA to FtsZ is demonstrated, including FtsZ fibre bundles decorated with ZipA. Using Cryo-Electron Microscopy, small-angle X-ray and neutron scattering, we determine the encapsulated-ZipA structure in isolation, and in complex with FtsZ to a resolution of 1.6 nm. Three regions can be identified from the structure which correspond to, SMALP encapsulated membrane and ZipA transmembrane helix, a separate short compact tether, and ZipA globular head which binds FtsZ. The complex extends 12 nm from the membrane in a compact structure, supported by mesoscale modelling techniques, measuring the movement and stiffness of the regions within ZipA provides molecular scale analysis and visualisation of the early divisome.

Original language	English
Article number	18712
Journal	Scientific Reports
Volume	9
Issue number	1
DOIs	https://doi.org/10.1038/s41598-019-54999-x
Publication status	Published - 10 Dec 2019

Funding

We would like to acknowledge the help of Ian Hands Portman in collection of negative stain transmission electron Microscopy images at the University of Warwick. This work is supported by BBSRC grant BB/J017310/1 (T.R.D, S.C.L, R.A.P). We would like to thank Diamond Light Source for the award of beamtime on instrument B21 (SM9727) and the assistance of Dr James Doutch in preparing the beamline and running this experiment. We would like to acknowledge ISIS Spallation Neutron and Muon Source for provision of neutron scattering facilities and the award of beamtime for experiment RB1410289 on SANS2D. We would also like to acknowledge Professor P. De Boer for providing the ZipA expression plasmid.

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Lee, S. C., Collins, R., Lin, Y., Jamshad, M., Broughton, C., Harris, S. A., Hanson, B. S., Tognoloni, C., Parslow, R. A., Terry, A. E., Rodger, A., Smith, C. J., Edler, K. J., Ford, R., Roper, D. I., & Dafforn, T. R. (2019). Nano-encapsulated Escherichia coli Divisome Anchor ZipA, and in Complex with FtsZ. Scientific Reports, 9(1), Article 18712. https://doi.org/10.1038/s41598-019-54999-x

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title = "Nano-encapsulated Escherichia coli Divisome Anchor ZipA, and in Complex with FtsZ",

abstract = "The E. coli membrane protein ZipA, binds to the tubulin homologue FtsZ, in the early stage of cell division. We isolated ZipA in a Styrene Maleic Acid lipid particle (SMALP) preserving its position and integrity with native E. coli membrane lipids. Direct binding of ZipA to FtsZ is demonstrated, including FtsZ fibre bundles decorated with ZipA. Using Cryo-Electron Microscopy, small-angle X-ray and neutron scattering, we determine the encapsulated-ZipA structure in isolation, and in complex with FtsZ to a resolution of 1.6 nm. Three regions can be identified from the structure which correspond to, SMALP encapsulated membrane and ZipA transmembrane helix, a separate short compact tether, and ZipA globular head which binds FtsZ. The complex extends 12 nm from the membrane in a compact structure, supported by mesoscale modelling techniques, measuring the movement and stiffness of the regions within ZipA provides molecular scale analysis and visualisation of the early divisome.",

author = "Lee, {Sarah C.} and Richard Collins and Yu-pin Lin and Mohammed Jamshad and Claire Broughton and Harris, {Sarah A.} and Hanson, {Benjamin S} and Cecilia Tognoloni and Parslow, {Rosemary A.} and Terry, {Ann E.} and Alison Rodger and Smith, {Corinne J.} and Edler, {Karen J.} and Robert Ford and Roper, {David I.} and Dafforn, {Timothy R.}",

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AU - Lee, Sarah C.

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AU - Jamshad, Mohammed

AU - Broughton, Claire

AU - Harris, Sarah A.

AU - Hanson, Benjamin S

AU - Tognoloni, Cecilia

AU - Parslow, Rosemary A.

AU - Terry, Ann E.

AU - Rodger, Alison

AU - Smith, Corinne J.

AU - Edler, Karen J.

AU - Ford, Robert

AU - Roper, David I.

AU - Dafforn, Timothy R.

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N2 - The E. coli membrane protein ZipA, binds to the tubulin homologue FtsZ, in the early stage of cell division. We isolated ZipA in a Styrene Maleic Acid lipid particle (SMALP) preserving its position and integrity with native E. coli membrane lipids. Direct binding of ZipA to FtsZ is demonstrated, including FtsZ fibre bundles decorated with ZipA. Using Cryo-Electron Microscopy, small-angle X-ray and neutron scattering, we determine the encapsulated-ZipA structure in isolation, and in complex with FtsZ to a resolution of 1.6 nm. Three regions can be identified from the structure which correspond to, SMALP encapsulated membrane and ZipA transmembrane helix, a separate short compact tether, and ZipA globular head which binds FtsZ. The complex extends 12 nm from the membrane in a compact structure, supported by mesoscale modelling techniques, measuring the movement and stiffness of the regions within ZipA provides molecular scale analysis and visualisation of the early divisome.

AB - The E. coli membrane protein ZipA, binds to the tubulin homologue FtsZ, in the early stage of cell division. We isolated ZipA in a Styrene Maleic Acid lipid particle (SMALP) preserving its position and integrity with native E. coli membrane lipids. Direct binding of ZipA to FtsZ is demonstrated, including FtsZ fibre bundles decorated with ZipA. Using Cryo-Electron Microscopy, small-angle X-ray and neutron scattering, we determine the encapsulated-ZipA structure in isolation, and in complex with FtsZ to a resolution of 1.6 nm. Three regions can be identified from the structure which correspond to, SMALP encapsulated membrane and ZipA transmembrane helix, a separate short compact tether, and ZipA globular head which binds FtsZ. The complex extends 12 nm from the membrane in a compact structure, supported by mesoscale modelling techniques, measuring the movement and stiffness of the regions within ZipA provides molecular scale analysis and visualisation of the early divisome.

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DO - 10.1038/s41598-019-54999-x

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JO - Scientific Reports

JF - Scientific Reports

IS - 1

M1 - 18712

ER -

Nano-encapsulated Escherichia coli Divisome Anchor ZipA, and in Complex with FtsZ

Abstract

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