Intrinsic disorder of the bacterial cell division protein ZipA: coil‐to‐brush conformational transition

López‐Montero, Iván; López-Navajas, Pilar; Mingorance, Jesús; Rivas, Germán; Vélez, Marisela; Vicente, Miguel; Monroy, Francisco

doi:10.1096/fj.12-224337

Cited by 18 publications

(19 citation statements)

References 88 publications

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“…The ZipA protein can bundle FtsZ protofilaments in vitro (RayChaudhuri, ) and induce the presence of higher‐order FtsZ helices in CSR603 maxicells (Pazos et al ., ). Furthermore, in vitro experiments demonstrate that depending on the lipid composition of the membrane, ZipA modulates the oligomeric state and the shape of the FtsZ protofilaments (Hernández‐Rocamora et al ., 2012a,b; Mateos‐Gil et al ., ; López‐Montero et al ., ). However, a detailed molecular mechanism for this observation is not described.…”

Section: The Proto‐ring Assemblymentioning

confidence: 97%

The Escherichia coli divisome: born to divide

Natale

Pazos

Vicente

2013

Environmental Microbiology

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SummarySeptation in Escherichia coli involves complex molecular mechanisms that contribute to the accuracy of bacterial division. The proto-ring, a complex made up by the FtsZ, FtsA and ZipA proteins, forms at the beginning of the process and directs the assembly of the full divisome. Central to this complex is the FtsZ protein, a GTPase able to assemble into a ringlike structure that responds to several modulatory inputs including mechanisms to position the septum at midcell. The connection with the cell wall synthesising machinery stabilizes the constriction of the cytoplasmic membrane. Although a substantial amount of evidence supports this description, many details on how individual divisome elements are structured or how they function are subjected to controversial interpretations. We discuss these discrepancies arising from incomplete data and from technical difficulties imposed by the small size of bacteria. Future work, including more powerful imaging and reconstruction technologies, will help to clarify the missing details on the architecture and function of the bacterial division machinery.

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Section: The Proto‐ring Assemblymentioning

confidence: 97%

The Escherichia coli divisome: born to divide

Natale

Pazos

Vicente

2013

Environmental Microbiology

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“…A typical example is given by the characterization of ZipA, a protein involved in the cell division machinery of Escherichia coli. It is a multidomain membrane-bound protein of 328 amino acids, which contains two terminal folded domains connected by an unfolded segment of $150 amino acids (58). Whereas the a-helical transmembrane domain at the N terminus anchors the protein to the cytoplasmic membrane, the globular C-terminal domain is responsible for the interaction of ZipA with a protein partner, FtsZ, involved in bacterial division.…”

Section: Comparison Of N Tail and Other Idps Undergoing Disorder-to-omentioning

confidence: 99%

“…Whereas the a-helical transmembrane domain at the N terminus anchors the protein to the cytoplasmic membrane, the globular C-terminal domain is responsible for the interaction of ZipA with a protein partner, FtsZ, involved in bacterial division. A study of ZipA at the A/W interface suggests that the protein undergoes a coil-to-brush conformational transition at high surface pressure, but preserves the disordered nature of its linker (58).…”

Section: Comparison Of N Tail and Other Idps Undergoing Disorder-to-omentioning

confidence: 99%

Interfacial Properties of NTAIL, an Intrinsically Disordered Protein

Bénarouche

Habchi

Cagna³

et al. 2017

Biophysical Journal

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Intrinsically disordered proteins (IDPs) lack stable secondary and tertiary structure under physiological conditions in the absence of their biological partners and thus exist as dynamic ensembles of interconverting conformers, often highly soluble in water. However, in some cases, IDPs such as the ones involved in neurodegenerative diseases can form protein aggregates and their aggregation process may be triggered by the interaction with membranes. Although the interfacial behavior of globular proteins has been extensively studied, experimental data on IDPs at the air/water (A/W) and water/lipid interfaces are scarce. We studied here the intrinsically disordered C-terminal domain of the Hendra virus nucleoprotein (N) and compared its interfacial properties to those of lysozyme that is taken as a model globular protein of similar molecular mass. Adsorption of N at the A/W interface was studied in the absence and presence of phospholipids using Langmuir films, polarization modulated-infrared reflection-absorption spectroscopy, and an automated drop tensiometer for interfacial tension and elastic modulus determination with oscillating bubbles. N showed a significant surface activity, with a higher adsorption capacity at the A/W interface and penetration into egg phosphatidylcholine monolayer compared to lysozyme. Whereas lysozyme remains folded upon compression of the protein layer at the A/W interface and shows a quasi-pure elastic behavior, N shows a much higher molecular area and forms a highly viscoelastic film with a high dilational modulus. To our knowledge, a new disorder-to-order transition is thus observed for the N protein that folds into an antiparallel β-sheet at the A/W interface and presents strong intermolecular interactions.

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“…Preliminary evidence suggests that, upon an increase in the density of its association with lipid bilayers, ZipA undergoes a transition from a compact to an extended conformation in which its globular domain can explore a wider volume in its environment (Fig. 1a) (73). ZipA may then compete for the C-terminal tail of FtsZ found inside the FtsA-FtsZ hetero-oligomers at midcell.…”

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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Intrinsic disorder of the bacterial cell division protein ZipA: coil‐to‐brush conformational transition

Cited by 18 publications

References 88 publications

The Escherichia coli divisome: born to divide

The Escherichia coli divisome: born to divide

Interfacial Properties of NTAIL, an Intrinsically Disordered Protein

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

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