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, Iván; López-Navajas, Pilar; Mingorance, Jesús; Vélez, Marisela; Vicente, Miguel; Monroy, Francisco

doi:10.1016/j.bbamem.2012.11.003

Cited by 15 publications

(11 citation statements)

References 68 publications

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“…Thus, this limiting case requires inexpensive membrane availability of the vesicle to increase its area [17]. This necessarily implies membrane uptake from either accumulated excess area or external lipid reservoirs [18], [19], [20], e.g. smaller vesicles or lipid aggregates in contact with the deformed vesicle.…”

Section: Resultsmentioning

confidence: 99%

Mechanics of Constriction during Cell Division: A Variational Approach

2013

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During symmetric division cells undergo large constriction deformations at a stable midcell site. Using a variational approach, we investigate the mechanical route for symmetric constriction by computing the bending energy of deformed vesicles with rotational symmetry. Forces required for constriction are explicitly computed at constant area and constant volume, and their values are found to be determined by cell size and bending modulus. For cell-sized vesicles, considering typical bending modulus of , we calculate constriction forces in the range . The instability of symmetrical constriction is shown and quantified with a characteristic coefficient of the order of , thus evidencing that cells need a robust mechanism to stabilize constriction at midcell.

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Section: Resultsmentioning

confidence: 99%

Mechanics of Constriction during Cell Division: A Variational Approach

2013

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“…Related to this, the interaction between FtsA and the late-assembling FtsN protein has been described Rico et al, 2010). Recently, it has been described a membrane dilation in lipid vesicles containing sZipA at both sides of the membrane when FtsZ polymerization was triggered by the release of caged GTP (Lopez-Montero et al, 2013).…”

Section: Synthetic Biology Bacterial Division Ftsz Escherichia Colmentioning

confidence: 99%

Giant vesicles: a powerful tool to reconstruct bacterial division assemblies in cell‐like compartments

Jiménez

Martos

Cabré

et al. 2013

Environmental Microbiology

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SummaryThe use of artificial lipid membranes, structured as giant unilamellar vesicles (GUVs), provides the opportunity to investigate membrane-associated biological processes under defined experimental conditions. Due to their large size, they are uniquely adapted to investigate the properties and organization (in time and space) of macromolecular complexes incorporated in the vesicle interior by imaging and micro-spectroscopic techniques. Experimental methods to produce giant vesicles and to encapsulate proteins inside them are here reviewed. Previous experimental work to reconstitute elements of the bacterial division machinery in these membrane-like systems is summarized. Future challenges towards reconstructing minimal divisome assemblies in giant vesicles as cytomimetic containers are discussed.

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“…1b) is not immediate and requires an incubation interval to occur (29). Polymerization under these conditions is accompanied by a change in the fluidity of the membrane (71,72). In addition, FtsZ and ZipA, but not FtsA, are required for preseptal peptidoglycan synthesis, which is independent of FtsI (also called PBP3), an enzyme involved in the synthesis of the septum (68).…”

Section: Proto-ring Maturationmentioning

confidence: 99%

In the Beginning, Escherichia coli Assembled the Proto-ring: An Initial Phase of Division

Rico

Krupka²,

Vicente

2013

Journal of Biological Chemistry

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Cell division in Escherichia coli begins by assembling three proteins, FtsZ, FtsA, and ZipA, to form a proto-ring at midcell. These proteins nucleate an assembly of at least 35 components, the divisome. The structuring of FtsZ to form a ring and the processes that effect constriction have been explained by alternative but not mutually exclusive mechanisms. We discuss how FtsA and ZipA provide anchoring of the cytoplasmic FtsZ to the membrane and how a temporal sequence of alternative protein interactions may operate in the maturation and stability of the proto-ring. How the force needed for constriction is generated and how the proto-ring proteins relate to peptidoglycan synthesis remain as the main challenges for future research. Overview of SeptationCell division is the last event in the bacterial cell cycle. It takes place by producing a rigid transversal septum after the growth processes fully duplicate the contents of the cell. Septation is always preceded by segregation of the duplicated nucleoids, ensuring that each of the daughter cells contains a fully replicated chromosome. Specialized molecules control the positioning of the division machinery at midcell, preventing any harmful fragmentation that septum progression could cause on unsegregated nucleoids.The division machinery, the divisome, establishes a complex interacting network together with DNA, lipids, and peptidoglycan components. It comprises a variable number of proteins, depending on the bacterial species. These proteins have redundant multiple functions and connections serving as safeguards to complete division and to guarantee the efficiency and versatility of the process. Altogether, an efficient division process allows the proliferation of bacteria under a variety of conditions, and it is one of the reasons for their success in the environment. Free-living bacteria, such as Escherichia coli, have more elaborated divisomes, whereas those that need to grow as intracellular parasites, as such Mycoplasma genitalium, have streamlined ones (1, 2).The structure of the E. coli divisome as revealed by immunofluorescence images of dividing cells is called the division ring (3). For its assembly, three essential proteins, FtsZ, FtsA, and ZipA, are first gathered at midcell, forming a proto-ring attached to the inner membrane ( Fig. 1) (4). In the proto-ring structure, the cytoplasmic GTPase FtsZ is anchored to the membrane by its interaction with ZipA and FtsA. ZipA is a bitopic protein containing a transmembrane domain (5). FtsA is a protein of the actin family that associates with the membrane by a short amphipathic helix (6, 7). The assembly of the FtsZ ring is dependent on a continuous energy supply. The FtsZ ring requires either ZipA or FtsA (8). Although it can be formed in the presence of either of them, division is affected unless both are present (9). A maturation period takes place after the protoring is assembled and before the rest of the divisome proteins become incorporated (10). During maturation, the proto-ring assembly is not stable...

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Membrane reconstitution of FtsZ–ZipA complex inside giant spherical vesicles made of E. coli lipids: Large membrane dilation and analysis of membrane plasticity

Cited by 15 publications

References 68 publications

Mechanics of Constriction during Cell Division: A Variational Approach

Mechanics of Constriction during Cell Division: A Variational Approach

Giant vesicles: a powerful tool to reconstruct bacterial division assemblies in cell‐like compartments

In the Beginning, Escherichia coli Assembled the Proto-ring: An Initial Phase of Division

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