ZapE is a novel cell division protein interacting with FtsZ and modulating the Z-ring dynamics

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

ZapE is a novel cell division protein interacting with FtsZ and modulating the Z-ring dynamics. / Marteyn, B.S.; Karimova, G.; Fenton, A.K.; Gazi, A.D.; West, N.; Touqui, L.; Prevost, M.-C.; Betton, J.-M.; Poyraz, O.; Ladant, D.; Gerdes, Kenn; Sansonetti, P.J.; Tang, C.M.

In: mBio, Vol. 5, No. 2, e00022-14, 2014, p. 1-10.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Marteyn, BS, Karimova, G, Fenton, AK, Gazi, AD, West, N, Touqui, L, Prevost, M-C, Betton, J-M, Poyraz, O, Ladant, D, Gerdes, K, Sansonetti, PJ & Tang, CM 2014, 'ZapE is a novel cell division protein interacting with FtsZ and modulating the Z-ring dynamics', mBio, vol. 5, no. 2, e00022-14, pp. 1-10. https://doi.org/10.1128/mBio.00022-14

APA

Marteyn, B. S., Karimova, G., Fenton, A. K., Gazi, A. D., West, N., Touqui, L., Prevost, M-C., Betton, J-M., Poyraz, O., Ladant, D., Gerdes, K., Sansonetti, P. J., & Tang, C. M. (2014). ZapE is a novel cell division protein interacting with FtsZ and modulating the Z-ring dynamics. mBio, 5(2), 1-10. [e00022-14]. https://doi.org/10.1128/mBio.00022-14

Vancouver

Marteyn BS, Karimova G, Fenton AK, Gazi AD, West N, Touqui L et al. ZapE is a novel cell division protein interacting with FtsZ and modulating the Z-ring dynamics. mBio. 2014;5(2):1-10. e00022-14. https://doi.org/10.1128/mBio.00022-14

Author

Marteyn, B.S. ; Karimova, G. ; Fenton, A.K. ; Gazi, A.D. ; West, N. ; Touqui, L. ; Prevost, M.-C. ; Betton, J.-M. ; Poyraz, O. ; Ladant, D. ; Gerdes, Kenn ; Sansonetti, P.J. ; Tang, C.M. / ZapE is a novel cell division protein interacting with FtsZ and modulating the Z-ring dynamics. In: mBio. 2014 ; Vol. 5, No. 2. pp. 1-10.

Bibtex

@article{c0a5867f93654293a65ca2e2ec57ab39,
title = "ZapE is a novel cell division protein interacting with FtsZ and modulating the Z-ring dynamics",
abstract = "Bacterial cell division requires the formation of a mature divisome complex positioned at the midcell. The localization of the divisome complex is determined by the correct positioning, assembly, and constriction of the FtsZ ring (Z-ring). Z-ring constriction control remains poorly understood and (to some extent) controversial, probably due to the fact that this phenomenon is transient and controlled by numerous factors. Here, we characterize ZapE, a novel ATPase found in Gram-negative bacteria, which is required for growth under conditions of low oxygen, while loss of zapE results in temperature-dependent elongation of cell shape. We found that ZapE is recruited to the Z-ring during late stages of the cell division process and correlates with constriction of the Z-ring. Overexpression or inactivation of zapE leads to elongation of Escherichia coli and affects the dynamics of the Z-ring during division. In vitro, ZapE destabilizes FtsZ polymers in an ATP-dependent manner. {\textcopyright} 2014 Marteyn et al.",
author = "B.S. Marteyn and G. Karimova and A.K. Fenton and A.D. Gazi and N. West and L. Touqui and M.-C. Prevost and J.-M. Betton and O. Poyraz and D. Ladant and Kenn Gerdes and P.J. Sansonetti and C.M. Tang",
year = "2014",
doi = "10.1128/mBio.00022-14",
language = "English",
volume = "5",
pages = "1--10",
journal = "mBio",
issn = "2161-2129",
publisher = "American Society for Microbiology",
number = "2",

}

RIS

TY - JOUR

T1 - ZapE is a novel cell division protein interacting with FtsZ and modulating the Z-ring dynamics

AU - Marteyn, B.S.

AU - Karimova, G.

AU - Fenton, A.K.

AU - Gazi, A.D.

AU - West, N.

AU - Touqui, L.

AU - Prevost, M.-C.

AU - Betton, J.-M.

AU - Poyraz, O.

AU - Ladant, D.

AU - Gerdes, Kenn

AU - Sansonetti, P.J.

AU - Tang, C.M.

PY - 2014

Y1 - 2014

N2 - Bacterial cell division requires the formation of a mature divisome complex positioned at the midcell. The localization of the divisome complex is determined by the correct positioning, assembly, and constriction of the FtsZ ring (Z-ring). Z-ring constriction control remains poorly understood and (to some extent) controversial, probably due to the fact that this phenomenon is transient and controlled by numerous factors. Here, we characterize ZapE, a novel ATPase found in Gram-negative bacteria, which is required for growth under conditions of low oxygen, while loss of zapE results in temperature-dependent elongation of cell shape. We found that ZapE is recruited to the Z-ring during late stages of the cell division process and correlates with constriction of the Z-ring. Overexpression or inactivation of zapE leads to elongation of Escherichia coli and affects the dynamics of the Z-ring during division. In vitro, ZapE destabilizes FtsZ polymers in an ATP-dependent manner. © 2014 Marteyn et al.

AB - Bacterial cell division requires the formation of a mature divisome complex positioned at the midcell. The localization of the divisome complex is determined by the correct positioning, assembly, and constriction of the FtsZ ring (Z-ring). Z-ring constriction control remains poorly understood and (to some extent) controversial, probably due to the fact that this phenomenon is transient and controlled by numerous factors. Here, we characterize ZapE, a novel ATPase found in Gram-negative bacteria, which is required for growth under conditions of low oxygen, while loss of zapE results in temperature-dependent elongation of cell shape. We found that ZapE is recruited to the Z-ring during late stages of the cell division process and correlates with constriction of the Z-ring. Overexpression or inactivation of zapE leads to elongation of Escherichia coli and affects the dynamics of the Z-ring during division. In vitro, ZapE destabilizes FtsZ polymers in an ATP-dependent manner. © 2014 Marteyn et al.

U2 - 10.1128/mBio.00022-14

DO - 10.1128/mBio.00022-14

M3 - Journal article

C2 - 24595368

VL - 5

SP - 1

EP - 10

JO - mBio

JF - mBio

SN - 2161-2129

IS - 2

M1 - e00022-14

ER -

ID: 113411392