The Monofunctional Glycosyltransferase of<i>Escherichia coli</i>Localizes to the Cell Division Site and Interacts with Penicillin-Binding Protein 3, FtsW, and FtsN

Derouaux, Adeline; Wolf, Benoît; Fraipont, Claudine; Breukink, Eefjan; Nguyen-Distèche, Martine; Terrak, Mohammed

doi:10.1128/jb.01377-07

Cited by 56 publications

(59 citation statements)

References 38 publications

(48 reference statements)

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“…It was possible, as was suggested by Nanninga (48), that preseptal peptidoglycan synthesis might require one or more penicillin-insensitive peptidoglycan synthases instead of PBP1a and -1b. The known candidates for such an activity in E. coli are PBP1c (56,69) and MtgA (4,24,25). Because these enzymes exhibit only glycosyltransferase activity, they can polymerize but not cross-link glycan strands.…”

Section: Resultsmentioning

confidence: 99%

ZipA Is Required for FtsZ-Dependent Preseptal Peptidoglycan Synthesis prior to Invagination during Cell Division

2012

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Rod-shaped bacteria grow by a repetitive cycle of elongation followed by division, and the mechanisms responsible for these two processes have been studied for decades. However, little is known about what happens during the transition between the two activities. At least one event occurs after elongation ends and before division commences, that being the insertion of new cell wall peptidoglycan into a narrowly circumscribed ribbon around midcell where septation is destined to take place. This insertion does not depend on the presence of the septation-specific protein PBP3 and is therefore known as PBP3-independent peptidoglycan synthesis (PIPS). Here we report that only FtsZ and ZipA are required to generate PIPS in wild-type Escherichia coli. PIPS does not require the participation of other members of the divisome, the MreB-directed cell wall elongation complex, alternate peptidoglycan synthases, the major peptidoglycan amidases, or any of the low-molecular-weight penicillin binding proteins. ZipA-directed PIPS may represent an intermediate stage that connects cell wall elongation to septal invagination and may be the reason ZipA is essential in the gammaproteobacteria.

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Section: Resultsmentioning

confidence: 99%

ZipA Is Required for FtsZ-Dependent Preseptal Peptidoglycan Synthesis prior to Invagination during Cell Division

2012

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“…FtsI and FtsN interact with nonessential divisome proteins that participate in other late septation processes, i.e. with PBP1B (85) or MtgA (86) for peptidoglycan synthesis, with the Tol-Pal complex for the invagination of the cell wall during constriction (87,88), and with the AmiB and AmiC amidases to effect the hydrolysis of peptidoglycan needed to split the wall of the two daughter cells (89).…”

Section: Proto-ring Stabilization and Divisome Completionmentioning

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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“…These modifications should destabilize the hydrophobic interface formed between the two LZ motifs without affecting the overall alpha-helical structure of the coiled coil, thus avoiding a dramatic alteration of the proteins that could lead to their instability and degradation (7,18). The impact of these modifications was assessed by using the BACTH assay that has been previously used to analyze interactions between Fts proteins (2,10,11,21,23). In this assay, the proteins of interest are fused to two complementary fragments, T25 and T18, from the adenylate cyclase of Bordetella pertussis and expressed in an E. coli cya strain.…”

mentioning

confidence: 99%

Role of Leucine Zipper Motifs in Association of the Escherichia coli Cell Division Proteins FtsL and FtsB

et al. 2011

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The Monofunctional Glycosyltransferase ofEscherichia coliLocalizes to the Cell Division Site and Interacts with Penicillin-Binding Protein 3, FtsW, and FtsN

Cited by 56 publications

References 38 publications

ZipA Is Required for FtsZ-Dependent Preseptal Peptidoglycan Synthesis prior to Invagination during Cell Division

ZipA Is Required for FtsZ-Dependent Preseptal Peptidoglycan Synthesis prior to Invagination during Cell Division

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

Role of Leucine Zipper Motifs in Association of the Escherichia coli Cell Division Proteins FtsL and FtsB

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