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Open AccessJournal ArticleDOI

Bacterial Cell Wall Synthesis: New Insights from Localization Studies

Dirk-Jan Scheffers, +1 more
- 01 Dec 2005 - 
- Vol. 69, Iss: 4, pp 585-607
TLDR
A model in which, at least for a subset of PBPs, the presence of substrate is a major factor in determining PBP localization is discussed, in both rod-shaped and coccoid cells.
Abstract
In order to maintain shape and withstand intracellular pressure, most bacteria are surrounded by a cell wall that consists mainly of the cross-linked polymer peptidoglycan (PG). The importance of PG for the maintenance of bacterial cell shape is underscored by the fact that, for various bacteria, several mutations affecting PG synthesis are associated with cell shape defects. In recent years, the application of fluorescence microscopy to the field of PG synthesis has led to an enormous increase in data on the relationship between cell wall synthesis and bacterial cell shape. First, a novel staining method enabled the visualization of PG precursor incorporation in live cells. Second, penicillin-binding proteins (PBPs), which mediate the final stages of PG synthesis, have been localized in various model organisms by means of immunofluorescence microscopy or green fluorescent protein fusions. In this review, we integrate the knowledge on the last stages of PG synthesis obtained in previous studies with the new data available on localization of PG synthesis and PBPs, in both rod-shaped and coccoid cells. We discuss a model in which, at least for a subset of PBPs, the presence of substrate is a major factor in determining PBP localization.

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Citations
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Genes and Molecules of Lactobacilli Supporting Probiotic Action

TL;DR: This review addresses the advances in the understanding of the probiotic-host interaction with a focus on the molecular microbiology of lactobacilli, facing the challenge of molecular characterization of probiotic traits.
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N-linked protein glycosylation in the ER.

TL;DR: This article summarizes the current knowledge of the N-glycosylation pathway in the ER that results in the covalent attachment of an oligosaccharide to asparagine residues of polypeptide chains and focuses on the model organism Saccharomyces cerevisiae.
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A Comprehensive, CRISPR-based Functional Analysis of Essential Genes in Bacteria

TL;DR: High-throughput microscopy indicated that cell morphology is relatively insensitive to mild knockdown but profoundly affected by depletion of gene function, revealing intimate connections between cell growth and shape.
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The archaeal cell envelope

TL;DR: The wide range of cell wall polymers, O- and N-glycosylated extracellular proteins and other cell surface structures that archaea use to interact with their environment are described.
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Penicillin Binding Proteins: key players in bacterial cell cycle and drug resistance processes

TL;DR: Structural, functional and biological features of penicillin-binding proteins, albeit having initially been identified several decades ago, are now being aggressively pursued as highly attractive targets for the development of novel antibiotherapies.
References
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Journal ArticleDOI

Growth of the Stress-Bearing and Shape-Maintaining Murein Sacculus of Escherichia coli

TL;DR: A model is presented that postulates that maintenance of bacterial shape is achieved by the enzyme complex copying the preexisting murein sacculus that plays the role of a template.
Journal ArticleDOI

A Continuum of Anionic Charge: Structures and Functions of d-Alanyl-Teichoic Acids in Gram-Positive Bacteria

TL;DR: The structures and functions of d- alanyl-TAs, the d-alanylation system encoded by the dlt operon, and the roles of TAs in cell growth are addressed.
Journal ArticleDOI

Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.

TL;DR: Evidence is presented that penicillin bulge formation is due to the inhibition of proteins 2 and 3 in the absence of inhibition of protein 1.
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