scholarly journals Membrane-partitioned cell wall synthesis in mycobacteria

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Alam García-Heredia ◽  
Takehiro Kado ◽  
Caralyn E Sein ◽  
Julia Puffal ◽  
Sarah H Osman ◽  
...  
Keyword(s):  
Cell Wall ◽  
Mycobacterium Smegmatis ◽  
General Feature ◽  
Membrane Domains ◽  
Peptidoglycan Biosynthesis ◽  
Cell Wall Assembly ◽  
Peptidoglycan Synthesis ◽  
Cell Wall Biogenesis ◽  
Wall Assembly ◽  
Made In

Many antibiotics target the assembly of cell wall peptidoglycan, an essential, heteropolymeric mesh that encases most bacteria. In rod-shaped bacteria, cell wall elongation is spatially precise yet relies on limited pools of lipid-linked precursors that generate and are attracted to membrane disorder. By tracking enzymes, substrates, and products of peptidoglycan biosynthesis in Mycobacterium smegmatis, we show that precursors are made in plasma membrane domains that are laterally and biochemically distinct from sites of cell wall assembly. Membrane partitioning likely contributes to robust, orderly peptidoglycan synthesis, suggesting that these domains help template peptidoglycan synthesis. The cell wall-organizing protein DivIVA and the cell wall itself promote domain homeostasis. These data support a model in which the peptidoglycan polymer feeds back on its membrane template to maintain an environment conducive to directional synthesis. Our findings are applicable to rod-shaped bacteria that are phylogenetically distant from M. smegmatis, indicating that horizontal compartmentalization of precursors may be a general feature of bacillary cell wall biogenesis.

scholarly journals The mycobacterial cell wall partitions the plasma membrane to organize its own synthesis

2019 ◽  
Author(s):  
Alam García-Heredia ◽  
Takehiro Kado ◽  
Caralyn E. Sein ◽  
Julia Puffal ◽  
Sarah H. Osman ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Membrane Domains ◽  
Peptidoglycan Biosynthesis ◽  
Cell Wall Assembly ◽  
Peptidoglycan Synthesis ◽  
Cell Wall Biogenesis ◽  
Mycobacterial Cell Wall ◽  
Wall Assembly ◽  
Made In

AbstractMany antibiotics target the assembly of cell wall peptidoglycan, an essential, heteropolymeric mesh that encases most bacteria. Different species have characteristic subcellular sites of peptidoglycan synthesis that they must carefully maintain for surface integrity and, ultimately, viability. In rod-shaped bacteria, cell wall elongation is spatially precise yet relies on a limited pool of lipid-linked precursors that generate and are attracted to membrane disorder. By tracking enzymes, substrates and products of peptidoglycan biosynthesis in Mycobacterium smegmatis, we show that precursors are made in plasma membrane domains that are laterally and biochemically distinct from sites of cell wall assembly. Membrane partitioning is required for robust, orderly peptidoglycan synthesis, indicating that these domains help template peptidoglycan synthesis. The cell wall-organizing protein DivIVA and the cell wall itself are essential for domain homeostasis. Thus, the peptidoglycan polymer feeds back on its membrane template to maintain an environment conducive to directional synthesis. We further show that our findings are applicable to rod-shaped bacteria that are phylogenetically distant from M. smegmatis, demonstrating that horizontal compartmentalization of precursors is a general feature of bacillary cell wall biogenesis.

scholarly journals Assemblies of DivIVA Mark Sites for Hyphal Branching and Can Establish New Zones of Cell Wall Growth in Streptomyces coelicolor

2008 ◽  
Vol 190 (22) ◽  
pp. 7579-7583 ◽  
Author(s):  
Antje Marie Hempel ◽  
Sheng-bing Wang ◽  
Michal Letek ◽  
José A. Gil ◽  
Klas Flärdh
Keyword(s):  
Cell Wall ◽  
Streptomyces Coelicolor ◽  
Time Lapse ◽  
Cell Wall Assembly ◽  
Peptidoglycan Synthesis ◽  
Wall Growth ◽  
Lateral Branches ◽  
Wall Assembly ◽  
Time Lapse Imaging

ABSTRACT Time-lapse imaging of Streptomyces hyphae revealed foci of the essential protein DivIVA at sites where lateral branches will emerge. Overexpression experiments showed that DivIVA foci can trigger establishment of new zones of cell wall assembly, suggesting a key role of DivIVA in directing peptidoglycan synthesis and cell shape in Streptomyces.

scholarly journals Modulation of peptidoglycan synthesis by recycled cell wall tetrapeptides

2019 ◽  
Author(s):  
Sara B. Hernández ◽  
Tobias Dörr ◽  
Matthew K. Waldor ◽  
Felipe Cava
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Bacterial Cell ◽  
Cell Shape ◽  
Cell Wall Assembly ◽  
Peptidoglycan Synthesis ◽  
Cross Linkage ◽  
Recycling Pathway ◽  
Wall Assembly ◽  
Substrate Competition

ABSTRACTThe bacterial cell wall is made of peptidoglycan (PG), a polymer that is essential for maintenance of cell shape and survival. During growth, bacteria remodel their PG, releasing fragments that are predominantly re-internalized by the cell, where they are recycled for synthesis of new PG. Although the PG recycling pathway is widely conserved, its components are not essential and its roles in cell wall homeostasis are not well-understood. Here, we identified LdcV, a Vibrio cholerae L,D-carboxypeptidase that cleaves the terminal D-Alanine from recycled murotetrapeptides. In the absence of ldcV, recycled tetrapeptides accumulated in the cytosol, leading to two toxic consequences for the cell wall. First, incorporation of tetrapeptide-containing PG precursors into the cell wall led to reduction in D,D-cross-linkage between stem peptides, diminishing PG integrity. Second, tetrapeptide accumulation led to a decrease in canonical UDP-pentapeptide precursors, reducing PG synthesis. Thus, LdcV and the recycling pathway promote optimal cell wall assembly and composition. Furthermore, Ldc substrate preference for murotetrapeptides containing canonical (D-Alanine) vs. non-canonical (D-Methionine) D-amino acids is conserved, suggesting that accumulation of tetrapeptide recycling intermediates may modulate PG homeostasis in environments enriched in non-canonical-muropeptides via substrate competition.

scholarly journals Peptidoglycan precursor synthesis along the sidewall of pole-growing mycobacteria

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Alam García-Heredia ◽  
Amol Arunrao Pohane ◽  
Emily S Melzer ◽  
Caleb R Carr ◽  
Taylor J Fiolek ◽  
...  
Keyword(s):  
Cell Wall ◽  
Amino Acid ◽  
Label Cell ◽  
Cell Wall Assembly ◽  
Support Cell ◽  
Peptidoglycan Synthesis ◽  
Precursor Synthesis ◽  
Alanine Synthesis ◽  
A Site ◽  
Wall Assembly

Rod-shaped mycobacteria expand from their poles, yet d-amino acid probes label cell wall peptidoglycan in this genus at both the poles and sidewall. We sought to clarify the metabolic fates of these probes. Monopeptide incorporation was decreased by antibiotics that block peptidoglycan synthesis or l,d-transpeptidation and in an l,d-transpeptidase mutant. Dipeptides complemented defects in d-alanine synthesis or ligation and were present in lipid-linked peptidoglycan precursors. Characterizing probe uptake pathways allowed us to localize peptidoglycan metabolism with precision: monopeptide-marked l,d-transpeptidase remodeling and dipeptide-marked synthesis were coincident with mycomembrane metabolism at the poles, septum and sidewall. Fluorescent pencillin-marked d,d-transpeptidation around the cell perimeter further suggested that the mycobacterial sidewall is a site of cell wall assembly. While polar peptidoglycan synthesis was associated with cell elongation, sidewall synthesis responded to cell wall damage. Peptidoglycan editing along the sidewall may support cell wall robustness in pole-growing mycobacteria.

scholarly journals Control of Cell Wall Assembly by a Histone-Like Protein in Mycobacteria

2007 ◽  
Vol 189 (22) ◽  
pp. 8241-8249 ◽  
Author(s):  
Tomoya Katsube ◽  
Sohkichi Matsumoto ◽  
Masaki Takatsuka ◽  
Megumi Okuyama ◽  
Yuriko Ozeki ◽  
...  
Keyword(s):  
Cell Wall ◽  
Wall Structure ◽  
Regulation Mechanism ◽  
Mycolic Acids ◽  
Growth State ◽  
Cell Wall Assembly ◽  
Cell Wall Biogenesis ◽  
Covalently Linked ◽  
Mycobacterial Cell Wall ◽  
Wall Assembly

ABSTRACT Bacteria coordinate assembly of the cell wall as well as synthesis of cellular components depending on the growth state. The mycobacterial cell wall is dominated by mycolic acids covalently linked to sugars, such as trehalose and arabinose, and is critical for pathogenesis of mycobacteria. Transfer of mycolic acids to sugars is necessary for cell wall biogenesis and is mediated by mycolyltransferases, which have been previously identified as three antigen 85 (Ag85) complex proteins. However, the regulation mechanism which links cell wall biogenesis and the growth state has not been elucidated. Here we found that a histone-like protein has a dual concentration-dependent regulatory effect on mycolyltransferase functions of the Ag85 complex through direct binding to both the Ag85 complex and the substrate, trehalose-6-monomycolate, in the cell wall. A histone-like protein-deficient Mycobacterium smegmatis strain has an unusual crenellated cell wall structure and exhibits impaired cessation of glycolipid biosynthesis in the growth-retarded phase. Furthermore, we found that artificial alteration of the amount of the extracellular histone-like protein and the Ag85 complex changes the growth rate of mycobacteria, perhaps due to impaired down-regulation of glycolipid biosynthesis. Our results demonstrate novel regulation of cell wall assembly which has an impact on bacterial growth.

The role of the exocytic pathway in cell wall assembly in yeast

Yeast ◽  
2021 ◽  
Author(s):  
Qingguo Guo ◽  
Na Meng ◽  
Guanzhi Fan ◽  
Dong Sun ◽  
Yuan Meng ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Wall Assembly ◽  
Wall Assembly ◽  
Exocytic Pathway

scholarly journals Properties of Arabinogalactan Proteins (AGPs) in Apple (Malus × Domestica) Fruit at Different Stages of Ripening

Biology ◽  
2020 ◽  
Vol 9 (8) ◽  
pp. 225
Author(s):  
Agata Leszczuk ◽  
Justyna Cybulska ◽  
Tomasz Skrzypek ◽  
Artur Zdunek
Keyword(s):  
Cell Wall ◽  
Malus Domestica ◽  
Arabinogalactan Proteins ◽  
Ex Situ ◽  
Morphological Properties ◽  
Mature Stage ◽  
Fruit Storage ◽  
Cell Wall Assembly ◽  
Wall Assembly

Arabinogalactan proteins (AGPs) are constituents of the cell wall–plasma membrane continuum in fruit tissue. The aim of the study was to characterise AGPs contained in fruit by determination of their chemical structure and morphological properties. The results were obtained from in and ex situ investigations and a comparative analysis of AGPs present in Malus × domestica fruit at different stages of ripening from green fruit through the mature stage to over-ripening during fruit storage. The HPLC and colorimetric methods were used for analyses of the composition of monosaccharides and proteins in AGPs extracted from fruit. We have found that AGPs from fruit mainly consists of carbohydrate chains composed predominantly of arabinose, galactose, glucose, galacturonic acid, and xylose. The protein moiety accounts for 3.15–4.58%, which depends on the various phases of ripening. Taken together, our results show that the structural and morphological properties of AGPs and calcium concentration in AGPs are related to the progress of ripening, which is correlated with proper fruit cell wall assembly. In line with the existing knowledge, our data confirmed the typical carbohydrate composition of AGPs and may be the basis for studies regarding their presumed properties of binding calcium ions.

scholarly journals Chlamydomonas reinhardtii Has Multiple Prolyl 4-Hydroxylases, One of Which Is Essential for Proper Cell Wall Assembly

2007 ◽  
Vol 19 (1) ◽  
pp. 256-269 ◽  
Author(s):  
Katriina Keskiaho ◽  
Reija Hieta ◽  
Raija Sormunen ◽  
Johanna Myllyharju
Keyword(s):  
Cell Wall ◽  
Chlamydomonas Reinhardtii ◽  
Cell Wall Assembly ◽  
Wall Assembly
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