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

2018 ◽  
Author(s):  
Alam García-Heredia ◽  
Amol Arunrao Pohane ◽  
Emily S. Melzer ◽  
Caleb R. Carr ◽  
Taylor J. Fiolek ◽  
...  
Keyword(s):  
Cell Wall ◽  
Amino Acid ◽  
Rapid Growth ◽  
Cell Elongation ◽  
Label Cell ◽  
Cell Periphery ◽  
Polar Growth ◽  
Peptidoglycan Synthesis ◽  
Precursor Synthesis ◽  
The Face

Abstractd-amino acid probes label cell wall peptidoglycan at both the poles and sidewall of pole-growing mycobacteria. Since peptidoglycan assembly along the cell periphery could provide a rapid, growth-independent means by which to edit the cell wall, we sought to clarify the precise metabolic fates of these probes.d-amino acid monopeptides were incorporated into peptidoglycan byl,d-transpeptidase remodeling enzymes to varying extents. Dipeptides were incorporated into cytoplasmic precursors. While dipeptide-marked peptidoglycan synthesis at the poles was associated with cell elongation, synthesis along the periphery was highly responsive to cell wall damage. Our observations suggest a post-expansion role for peptidoglycan assembly along the mycobacterial sidewall and provide a conceptual framework for understanding cell wall robustness in the face of polar growth.

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 SEDS-bPBP pairs direct Lateral and Septal Peptidoglycan Synthesis in Staphylococcus aureus

2019 ◽  
Author(s):  
Nathalie T. Reichmann ◽  
Andreia C. Tavares ◽  
Bruno M. Saraiva ◽  
Ambre Jousselin ◽  
Patricia Reed ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Wall ◽  
Cell Division ◽  
Late Stage ◽  
Cell Elongation ◽  
Cell Shape ◽  
Protein A ◽  
Interacting Proteins ◽  
Peptidoglycan Synthesis ◽  
Multiple Rings

Peptidoglycan (PGN) is the major component of the bacterial cell wall, a structure essential for the physical integrity and shape of the cell. Bacteria maintain cell shape by directing PGN incorporation to distinct regions of the cell, namely through the localisation of the late stage PGN synthesis proteins. These include two key protein families, SEDS transglycosylases and the bPBP transpeptidases, proposed to function in cognate pairs. Rod-shaped bacteria have two SEDS-bPBP pairs, involved in cell elongation and cell division. Here, we elucidate why coccoid bacteria, such as Staphylococcus aureus, also possess two SEDS-bPBP pairs. We determined that S. aureus RodA-PBP3 and FtsW-PBP1 likely constitute cognate pairs of interacting proteins. Lack of RodA-PBP3 decreased cell eccentricity due to deficient pre-septal PGN synthesis, whereas the depletion of FtsW-PBP1 arrested normal septal PGN incorporation. Although PBP1 is an essential protein, a mutant lacking PBP1 transpeptidase activity is viable, showing that this protein has a second function. We propose that the FtsW-PBP1 pair has a role in stabilising the divisome at midcell. In the absence of these proteins, the divisome appears as multiple rings/arcs that drive lateral PGN incorporation, leading to cell elongation. We conclude that RodA-PBP3 and FtsW-PBP1 mediate lateral and septal PGN incorporation, respectively, and that the activity of these pairs must be balanced in order to maintain coccoid morphology.

scholarly journals Tol-Pal System and Rgs Proteins Interact to Promote Unipolar Growth and Cell Division in Sinorhizobium meliloti

mBio ◽  
2020 ◽  
Vol 11 (3) ◽  
Author(s):  
Elizaveta Krol ◽  
Hamish C. L. Yau ◽  
Marcus Lechner ◽  
Simon Schäper ◽  
Gert Bange ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Division ◽  
Cell Growth ◽  
Cell Elongation ◽  
Sinorhizobium Meliloti ◽  
Rgs Proteins ◽  
Polar Growth ◽  
Content Type ◽  
Cell Pole ◽  
Growing Cell

ABSTRACT Sinorhizobium meliloti is an alphaproteobacterium belonging to the Rhizobiales. Bacteria from this order elongate their cell wall at the new cell pole, generated by cell division. Screening for protein interaction partners of the previously characterized polar growth factors RgsP and RgsM, we identified the inner membrane components of the Tol-Pal system (TolQ and TolR) and novel Rgs (rhizobial growth and septation) proteins with unknown functions. TolQ, Pal, and all Rgs proteins, except for RgsE, were indispensable for S. meliloti cell growth. Six of the Rgs proteins, TolQ, and Pal localized to the growing cell pole in the cell elongation phase and to the septum in predivisional cells, and three Rgs proteins localized to the growing cell pole only. The putative FtsN-like protein RgsS contains a conserved SPOR domain and is indispensable at the early stages of cell division. The components of the Tol-Pal system were required at the late stages of cell division. RgsE, a homolog of the Agrobacterium tumefaciens growth pole ring protein GPR, has an important role in maintaining the normal growth rate and rod cell shape. RgsD is a periplasmic protein with the ability to bind peptidoglycan. Analysis of the phylogenetic distribution of the Rgs proteins showed that they are conserved in Rhizobiales and mostly absent from other alphaproteobacterial orders, suggesting a conserved role of these proteins in polar growth. IMPORTANCE Bacterial cell proliferation involves cell growth and septum formation followed by cell division. For cell growth, bacteria have evolved different complex mechanisms. The most prevalent growth mode of rod-shaped bacteria is cell elongation by incorporating new peptidoglycans in a dispersed manner along the sidewall. A small share of rod-shaped bacteria, including the alphaproteobacterial Rhizobiales, grow unipolarly. Here, we identified and initially characterized a set of Rgs (rhizobial growth and septation) proteins, which are involved in cell division and unipolar growth of Sinorhizobium meliloti and highly conserved in Rhizobiales. Our data expand the knowledge of components of the polarly localized machinery driving cell wall growth and suggest a complex of Rgs proteins with components of the divisome, differing in composition between the polar cell elongation zone and the septum.

scholarly journals DivIVA Is Required for Polar Growth in the MreB-Lacking Rod-Shaped Actinomycete Corynebacterium glutamicum

2008 ◽  
Vol 190 (9) ◽  
pp. 3283-3292 ◽  
Author(s):  
Michal Letek ◽  
Efrén Ordóñez ◽  
José Vaquera ◽  
William Margolin ◽  
Klas Flärdh ◽  
...  
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Cell Division ◽  
Streptococcus Pneumoniae ◽  
Corynebacterium Glutamicum ◽  
Chromosome Segregation ◽  
Polar Growth ◽  
Cell Wall Synthesis ◽  
Peptidoglycan Synthesis ◽  
Polarized Cell Growth

ABSTRACT The actinomycete Corynebacterium glutamicum grows as rod-shaped cells by zonal peptidoglycan synthesis at the cell poles. In this bacterium, experimental depletion of the polar DivIVA protein (DivIVACg) resulted in the inhibition of polar growth; consequently, these cells exhibited a coccoid morphology. This result demonstrated that DivIVA is required for cell elongation and the acquisition of a rod shape. DivIVA from Streptomyces or Mycobacterium localized to the cell poles of DivIVACg-depleted C. glutamicum and restored polar peptidoglycan synthesis, in contrast to DivIVA proteins from Bacillus subtilis or Streptococcus pneumoniae, which localized at the septum of C. glutamicum. This confirmed that DivIVAs from actinomycetes are involved in polarized cell growth. DivIVACg localized at the septum after cell wall synthesis had started and the nucleoids had already segregated, suggesting that in C. glutamicum DivIVA is not involved in cell division or chromosome segregation.

scholarly journals Tol-Pal system and Rgs proteins interact to promote unipolar growth and cell division in Sinorhizobium meliloti

2020 ◽  
Author(s):  
Elizaveta Krol ◽  
Hamish C. L. Yau ◽  
Marcus Lechner ◽  
Simon Schäper ◽  
Gert Bange ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Division ◽  
Cell Growth ◽  
Cell Elongation ◽  
Sinorhizobium Meliloti ◽  
Normal Growth ◽  
Rgs Proteins ◽  
Polar Growth ◽  
Cell Pole ◽  
Growing Cell

ABSTRACTSinorhizobium meliloti is an α-proteobacterium belonging to the Rhizobiales. Bacteria from this order elongate their cell wall at the new cell pole, generated by cell division. Screening for protein interaction partners of the previously characterized polar growth factors RgsP and RgsM, we identified the inner membrane components of the Tol-Pal system (TolQ and TolR) and novel Rgs (rhizobial growth and septation) proteins with unknown functions. TolQ, Pal and all Rgs proteins, except for RgsE, were indispensable for S. meliloti cell growth. Six of the Rgs proteins, TolQ and Pal localized to the growing cell pole in the cell elongation phase and to the septum in pre-divisional cells, and three Rgs proteins localized to growing cell pole only. The FtsN-like protein RgsS contains a conserved SPOR domain and is indispensable at the early stages of cell division. The components of the Tol-Pal system were required at the late stages of cell division. RgsE, a homolog of the Agrobacterium tumefaciens growth pole ring protein GPR, has an important role in maintaining the normal growth rate and rod cell shape. RgsD is a novel periplasmic protein with the ability to bind peptidoglycan. Analysis of the phylogenetic distribution of novel Rgs proteins showed that they are conserved in Rhizobiales and mostly absent from other α-proteobacterial orders, suggesting a conserved role of these proteins in polar growth.IMPORTANCEBacterial cell proliferation involves cell growth and septum formation followed by cell division. For cell growth, bacteria have evolved different complex mechanisms. The most prevalent growth mode of rod shaped bacteria is cell elongation by incorporating new peptidoglycan in a dispersed manner along the sidewall. A small share of rod-shaped bacteria, including the α-proteobacterial Rhizobiales, grow unipolarly. Here, we identified and initially characterized a set of Rgs (rhizobial growth and septation) proteins, which are involved in cell division and unipolar growth of Sinorhizobium meliloti and highly conserved in Rhizobiales. Our data expand the knowledge of components of the polarly localized machinery driving cell wall growth and suggest a complex of Rgs proteins with components of the divisome, differing in composition between the polar cell elongation zone and the septum.

scholarly journals Demonstration of the role of cell wall homeostasis in Staphylococcus aureus growth and the action of bactericidal antibiotics

2021 ◽  
Vol 118 (44) ◽  
pp. e2106022118
Author(s):  
Bartłomiej Salamaga ◽  
Lingyuan Kong ◽  
Laia Pasquina-Lemonche ◽  
Lucia Lafage ◽  
Milena von und zur Muhlen ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Wall ◽  
Turgor Pressure ◽  
Regulatory System ◽  
Bactericidal Effect ◽  
Hydrolase Activity ◽  
Peptidoglycan Hydrolase ◽  
Peptidoglycan Synthesis ◽  
Peptidoglycan Hydrolases ◽  
The Face

Bacterial cell wall peptidoglycan is essential, maintaining both cellular integrity and morphology, in the face of internal turgor pressure. Peptidoglycan synthesis is important, as it is targeted by cell wall antibiotics, including methicillin and vancomycin. Here, we have used the major human pathogen Staphylococcus aureus to elucidate both the cell wall dynamic processes essential for growth (life) and the bactericidal effects of cell wall antibiotics (death) based on the principle of coordinated peptidoglycan synthesis and hydrolysis. The death of S. aureus due to depletion of the essential, two-component and positive regulatory system for peptidoglycan hydrolase activity (WalKR) is prevented by addition of otherwise bactericidal cell wall antibiotics, resulting in stasis. In contrast, cell wall antibiotics kill via the activity of peptidoglycan hydrolases in the absence of concomitant synthesis. Both methicillin and vancomycin treatment lead to the appearance of perforating holes throughout the cell wall due to peptidoglycan hydrolases. Methicillin alone also results in plasmolysis and misshapen septa with the involvement of the major peptidoglycan hydrolase Atl, a process that is inhibited by vancomycin. The bactericidal effect of vancomycin involves the peptidoglycan hydrolase SagB. In the presence of cell wall antibiotics, the inhibition of peptidoglycan hydrolase activity using the inhibitor complestatin results in reduced killing, while, conversely, the deregulation of hydrolase activity via loss of wall teichoic acids increases the death rate. For S. aureus, the independent regulation of cell wall synthesis and hydrolysis can lead to cell growth, death, or stasis, with implications for the development of new control regimes for this important pathogen.

Properties of cell wall peptidoglycan synthesized by amino acid deprived relA mutants of Escherichia coli

1984 ◽  
Vol 30 (10) ◽  
pp. 1239-1246 ◽  
Author(s):  
Désirée Vanderwel ◽  
Edward E. Ishiguro
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Amino Acid ◽  
Free Form ◽  
Amino Acid Deprivation ◽  
Peptidoglycan Synthesis ◽  
Cell Wall Peptidoglycan ◽  
Covalently Linked

Cell wall peptidoglycan synthesis in Escherichia coli is under stringent control. During amino acid deprivation, peptidoglycan synthesis is inhibited in re1A+ bacteria but not in re1A mutants. The relaxed synthesis of peptidoglycan by amino acid deprived re1A bacteria was inhibited by Several β-lactam antibiotics at concentrations which inhibited cell elongation in growing cultures suggesting that the transpeptidase activity of penicillin-binding protein (PBP-1B) was involved in this process. Structural studies on the peptidoglycan also indicated the involvement of transpeptidation in relaxed peptidoglycan synthesis. The peptidoglycan synthesized during amino acid deprivation was cross-linked to the existing cell wall peptidoglycan, and the degree of cross-linkage was the same as that of peptidoglycan synthesized by growing control cells. The relaxed synthesis of peptidoglycan was also inhibited by moenomycin, an inhibitor of the in vitro transglycosylase activities of PBPs, but the interpretation of this result depends on whether the transglycosylases are the sole targets of moenomycin in vivo. Most of the peptidoglycan lipoprotein synthesized by histidine-deprived re1A+ bacteria was in the free form as previously reported, possibly because of the restriction in peptidoglycan synthesis. In support of this proposal, most of the lipoprotein synthesized during histidine deprivation of re1A mutants was found to be covalently linked to peptidoglycan. Nevertheless, the peptidoglycan synthesized by amino acid deprived re1A bacteria was apparently deficient in bound lipoprotein as compared with peptidoglycan synthesized by normal growing control bacteria suggesting that the rate of lipoprotein synthesis during amino acid deprivation may be limiting.

The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus

2007 ◽  
Vol 64 (4) ◽  
pp. 938-952 ◽  
Author(s):  
Michelle Aaron ◽  
Godefroid Charbon ◽  
Hubert Lam ◽  
Heinz Schwarz ◽  
Waldemar Vollmer ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Elongation ◽  
Caulobacter Crescentus ◽  
Precursor Synthesis

scholarly journals Transcriptome and metabolome profiling provide insights into molecular mechanism of pseudostem elongation in banana

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Guiming Deng ◽  
Fangcheng Bi ◽  
Jing Liu ◽  
Weidi He ◽  
Chunyu Li ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Elongation ◽  
Molecular Mechanisms ◽  
Specific Gene ◽  
Wild Type ◽  
Banana Plant ◽  
Cell Wall Modification ◽  
Dwarf Cultivar ◽  
Important Trait ◽  
Metabolome Profiling

AbstractBackgroundBanana plant height is an important trait for horticultural practices and semi-dwarf cultivars show better resistance to damages by wind and rain. However, the molecular mechanisms controlling the pseudostem height remain poorly understood. Herein, we studied the molecular changes in the pseudostem of a semi-dwarf banana mutant Aifen No. 1 (Musaspp. Pisang Awak sub-group ABB) as compared to its wild-type dwarf cultivar using a combined transcriptome and metabolome approach.ResultsA total of 127 differentially expressed genes and 48 differentially accumulated metabolites were detected between the mutant and its wild type. Metabolites belonging to amino acid and its derivatives, flavonoids, lignans, coumarins, organic acids, and phenolic acids were up-regulated in the mutant. The transcriptome analysis showed the differential regulation of genes related to the gibberellin pathway, auxin transport, cell elongation, and cell wall modification. Based on the regulation of gibberellin and associated pathway-related genes, we discussed the involvement of gibberellins in pseudostem elongation in the mutant banana. Genes and metabolites associated with cell wall were explored and their involvement in cell extension is discussed.ConclusionsThe results suggest that gibberellins and associated pathways are possibly developing the observed semi-dwarf pseudostem phenotype together with cell elongation and cell wall modification. The findings increase the understanding of the mechanisms underlying banana stem height and provide new clues for further dissection of specific gene functions.

Sign in / Sign up

Export Citation Format

Share Document