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

^*Corresponding author for this work

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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
Pages (from-to)	1-16
Number of pages	16
Journal	Scientific Reports
Volume	9
DOIs	https://doi.org/10.1038/s41598-019-54999-x
Publication status	Published - 10 Dec 2019

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Copyright the Author(s) 2019. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

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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, 1-16. [18712]. https://doi.org/10.1038/s41598-019-54999-x

Lee, Sarah C. ; Collins, Richard ; Lin, Yu-pin ; Jamshad, Mohammed ; Broughton, Claire ; Harris, Sarah A. ; Hanson, Benjamin S. ; Tognoloni, Cecilia ; Parslow, Rosemary A. ; Terry, Ann E. ; Rodger, Alison ; Smith, Corinne J. ; Edler, Karen J. ; Ford, Robert ; Roper, David I. ; Dafforn, Timothy R. / Nano-encapsulated Escherichia coli divisome anchor ZipA, and in complex with FtsZ. In: Scientific Reports. 2019 ; Vol. 9. pp. 1-16.

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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.}",

note = "Copyright the Author(s) 2019. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher. ",

year = "2019",

month = dec,

day = "10",

doi = "10.1038/s41598-019-54999-x",

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Nano-encapsulated Escherichia coli divisome anchor ZipA, and in complex with FtsZ. / Lee, Sarah C.; Collins, Richard; Lin, Yu-pin; Jamshad, Mohammed; Broughton, Claire; Harris, Sarah A.; Hanson, Benjamin S.; Tognoloni, Cecilia; Parslow, Rosemary A.; Terry, Ann E.; Rodger, Alison; Smith, Corinne J.; Edler, Karen J.; Ford, Robert; Roper, David I.; Dafforn, Timothy R.

In: Scientific Reports, Vol. 9, 18712, 10.12.2019, p. 1-16.

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

TY - JOUR

T1 - Nano-encapsulated Escherichia coli divisome anchor ZipA, and in complex with FtsZ

AU - Lee, Sarah C.

AU - Collins, Richard

AU - Lin, Yu-pin

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.

N1 - Copyright the Author(s) 2019. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

PY - 2019/12/10

Y1 - 2019/12/10

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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JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

M1 - 18712

ER -

Nano-encapsulated Escherichia coli divisome anchor ZipA, and in complex with FtsZ

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