| ZipA Uses a Two-Pronged FtsZ-Binding Mechanism Necessary for Cell Division. | ZipA Uses a Two-Pronged FtsZ-Binding Mechanism Necessary for Cell Division.
Cameron TA, Vega DE, Yu C, Xiao H, Margolin W., Free PMC Article | 02/26/2022 |
| ZipA attachment enables FtsZ-GMPCPP (where GMPCPP is a GTP analogue with a reduced level of hydrolysis) to assemble in several distinct ways: (i) two-dimensional polymerization at the membrane and (ii) three-dimensional polymerization from the membrane into the solution phase where this may be associated with the formation of higher-order complexes. | Reversible Membrane Tethering by ZipA Determines FtsZ Polymerization in Two and Three Dimensions.
Sobrinos-Sanguino M, Vélez M, Richter RP, Rivas G. | 06/20/2020 |
| Here, the authors use in vivo cross-linking to show that FtsA and ZipA indeed interact directly. They identify the exposed surface of FtsA helix 7, which also participates in binding to ATP through its internal surface, as a key interface needed for the interaction with ZipA. | Direct Interaction between the Two Z Ring Membrane Anchors FtsA and ZipA.
Vega DE, Margolin W., Free PMC Article | 10/26/2019 |
| When lower, more physiological levels of the soluble, cytoplasmic domain of Escherichia coli membrane proteins ZipA (sZipA) are attached to lipids, cytoskeletal proteins FtsZ assemble into highly dynamic vortices similar to those assembled with FtsA or other membrane anchors. ZipA does not dampen FtsZ dynamics but acts as a passive membrane attachment for FtsZ filaments as they treadmill. | Escherichia coli ZipA Organizes FtsZ Polymers into Dynamic Ring-Like Protofilament Structures.
Krupka M, Sobrinos-Sanguino M, Jiménez M, Rivas G, Margolin W., Free PMC Article | 09/14/2019 |
| study demonstrates a link between amino acid metabolism and ZipA, another essential cell division protein that binds directly to FtsZ and tethers it to the cytoplasmic membrane | Suppression of a Thermosensitive zipA Cell Division Mutant by Altering Amino Acid Metabolism.
Vega DE, Margolin W., Free PMC Article | 12/30/2017 |
| YciB protein directly interacted with ZipA. Furthermore, the septum localization of ZipA, an essential protein of cell division, is disturbed in a DeltayciB mutant | Escherichia coli inner membrane protein YciB interacts with ZipA that is important for cell division.
Badaluddin NA, Kitakawa M. | 08/13/2016 |
| these data inspire a model in which Kil interacts with FtsZ and ZipA in the cell to prevent FtsZ assembly into a coherent, division-competent ring structure | The Kil peptide of bacteriophage λ blocks Escherichia coli cytokinesis via ZipA-dependent inhibition of FtsZ assembly.
Haeusser DP, Hoashi M, Weaver A, Brown N, Pan J, Sawitzke JA, Thomason LC, Court DL, Margolin W., Free PMC Article | 11/29/2014 |
| A mutation in the promoter region of zipA, a component of the divisome, suppresses the shape defect of RodZ-deficient cells. | A mutation in the promoter region of zipA, a component of the divisome, suppresses the shape defect of RodZ-deficient cells.
Shiomi D, Niki H., Free PMC Article | 05/3/2014 |
| Data suggest a functional scenario in which ZipA acts as a flexible tether anchoring bacterial proto-ring elements to the membrane during the earlier stages of division. | Intrinsic disorder of the bacterial cell division protein ZipA: coil-to-brush conformational transition.
López-Montero I, López-Navajas P, Mingorance J, Rivas G, Vélez M, Vicente M, Monroy F. | 12/21/2013 |
| analysis of membrane reconstitution of FtsZ-ZipA complex inside giant spherical vesicles made of E. coli lipids | Membrane reconstitution of FtsZ-ZipA complex inside giant spherical vesicles made of E. coli lipids: large membrane dilation and analysis of membrane plasticity.
López-Montero I, López-Navajas P, Mingorance J, Vélez M, Vicente M, Monroy F. | 04/6/2013 |
| ZipA binds to FtsZ with high affinity and enhances the stability of FtsZ protofilaments | ZipA binds to FtsZ with high affinity and enhances the stability of FtsZ protofilaments.
Kuchibhatla A, Bhattacharya A, Panda D., Free PMC Article | 07/21/2012 |
| FtsA self-interaction at the Z ring is antagonized by ZipA, allowing unpolymerized FtsA to recruit downstream proteins such as FtsN. | FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins.
Pichoff S, Shen B, Sullivan B, Lutkenhaus J., Free PMC Article | 04/14/2012 |
| Escherichia coli cell division protein ZipA forms homodimers prior to association with FtsZ | The Escherichia coli cell division protein ZipA forms homodimers prior to association with FtsZ.
Skoog K, Daley DO. | 04/14/2012 |