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

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 - 2014/3/4

Y1 - 2014/3/4

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.

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.

U2 - 10.1128/mBio.00022-14

DO - 10.1128/mBio.00022-14

M3 - Journal article

C2 - 24595368

SN - 2161-2129

VL - 5

SP - 1

EP - 10

JO - mBio

JF - mBio

IS - 2

M1 - e00022-14

ER -