A matter of life and death: cell wall homeostasis and the WalKR (YycGF) essential signal transduction pathway

Dubrac, Sarah; Bisicchia, Paola; Devine, Kevin M.; Msadek, Tarek

doi:10.1111/j.1365-2958.2008.06483.x

Cited by 268 publications

(375 citation statements)

References 77 publications

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“…The system was first discovered in Bacillus subtilis as essential for cell division and growth because it directly regulates the ftsAZ operon [98,99]. Orthologues of vicR and vicK form operons with one to four accessory cistrons [100]. In B. subtilis , two of these cistrons ( yycH and yycI ) encode transmembrane proteins that negatively regulate YycFG (VicK) kinase activity, but the function of a third gene ( yycJ ) is still unclear [101].…”

Section: Tcs Vicrk Of Streptococcimentioning

confidence: 99%

“…Staphylococcus, Enterococcus , Listeria , and Lactobacillus , except for Streptococcus spp. and Lactococcus lactis , in which the operons include only the yycJ orthologue, also known as vicX or walJ [100,102]. Proteins encoded by vicX are metal-dependent beta-lactamases of as-yet unknown function, although there is evidence suggesting that VicX modulates VicK activity in S. mutans , because vicX -defective strains showed altered phenotypes in VicRK-regulated functions [103].…”

Section: Tcs Vicrk Of Streptococcimentioning

confidence: 99%

“…VicR is in the OmpR/PhoB family of regulators in which the output domain forms a DNA-binding winged-helix domain. In B. subtilis and Staphylococcus aureus , both VicR and VicK are essential for bacterial viability [100]; on the other hand, only vicR is essential in S. pneumoniae [105], S. mutans [106,107], and S. sanguinis [90], and both vicR and vicK can be deleted in S. gordonii [91]. In S. pyogenes , insertional inactivation of vicR was possible, but the mutant was not viable in a mice model of infection [108].…”

Section: Tcs Vicrk Of Streptococcimentioning

confidence: 99%

“…The general role of VicRK in controlling the biosynthesis of peptidoglycan and cell division might imply that this TCS senses signals associated with peptidoglycan biosynthesis [100]. In B. subtilis , YycG (VicK) co-localized with FtsZ of the divisome, and it was proposed that VicK Bs senses cell division directly [133].…”

Section: What Are the Signals Sensed By Vicrk Tcs?mentioning

confidence: 99%

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Two-component signal transduction systems in oral bacteria

Mattos-Graner

Duncan²

2017

Journal of Oral Microbiology

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We present an overview of how members of the oral microbiota respond to their environment by regulating gene expression through two-component signal transduction systems (TCSs) to support conditions compatible with homeostasis in oral biofilms or drive the equilibrium toward dysbiosis in response to environmental changes. Using studies on the sub-gingival Gram-negative anaerobe Porphyromonas gingivalis and Gram-positive streptococci as examples, we focus on the molecular mechanisms involved in activation of TCS and species specificities of TCS regulons.

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Section: Tcs Vicrk Of Streptococcimentioning

confidence: 99%

Section: Tcs Vicrk Of Streptococcimentioning

confidence: 99%

Section: Tcs Vicrk Of Streptococcimentioning

confidence: 99%

Section: What Are the Signals Sensed By Vicrk Tcs?mentioning

confidence: 99%

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Two-component signal transduction systems in oral bacteria

Mattos-Graner

Duncan²

2017

Journal of Oral Microbiology

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“…Its synthesis and turnover involve a number of enzymes that must function in a coordinated manner. During the last decade it has become clear that a twocomponent regulatory system termed WalKR (also known as VicKR and YycGF) controls PG metabolism in low G þ C Grampositive bacteria 2 . Analysis of the WalKR regulons of Bacillus subtilis and Staphylococcus aureus have revealed their role in the control of the expression of a number of PG hydrolases, some of which are involved in the separation of daughter cells 3,4 .…”

mentioning

confidence: 99%

Structural basis of PcsB-mediated cell separation in Streptococcus pneumoniae

et al. 2014

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Separation of daughter cells during bacterial cell division requires splitting of the septal cross wall by peptidoglycan hydrolases. In Streptococcus pneumoniae, PcsB is predicted to perform this operation. Recent evidence shows that PcsB is recruited to the septum by the transmembrane FtsEX complex, and that this complex is required for cell division. However, PcsB lacks detectable catalytic activity in vitro, and while it has been proposed that FtsEX activates PcsB, evidence for this is lacking. Here we demonstrate that PcsB has muralytic activity, and report the crystal structure of full-length PcsB. The protein adopts a dimeric structure in which the V-shaped coiled-coil (CC) domain of each monomer acts as a pair of molecular tweezers locking the catalytic domain of each dimeric partner in an inactive configuration. This suggests that the release of the catalytic domains likely requires an ATP-driven conformational change in the FtsEX complex, conveyed towards the catalytic domains through coordinated movements of the CC domain.

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Bacterial Cell Wall Recycling

Mayer

2012

Encyclopedia of Life Sciences

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Cell wall recycling is a process whereby bacteria degrade their own wall during growth, recover released constituents by active transport and reutilise them either to rebuild the wall or to gain energy. Most knowledge about cell wall recycling comes from studies with the Gram‐negative bacterium Escherichia coli . Within one generation, this organism breaks down and efficiently recycles approximately 60% of the mature peptidoglycan of its side‐wall during cell elongation and approximately 30% of newly deposited septal peptidoglycan during cell division. The reason for the massive turnover of the peptidoglycan is still unclear, although many other bacteria, including Gram‐positives, have been reported to turnover their cell wall and release similar quantities of peptidoglycan fragments during growth and differentiation. Whether these fragments are also recycled is basically unknown. The presence of recycling genes on most bacterial genomes, however, suggests that cell wall recycling is a very common pathway of bacteria. Key Concepts: The peptidoglycan of the bacterial cell wall represents a single, giant, reticular macromolecule (i.e. the murein sacculus) that encases the entire bacterial cell. The peptidoglycan cell wall has to be cleaved continuously during growth to allow cell expansion by insertion of new wall material. Bacteria possess a huge and partially redundant set of cell wall lytic enzymes that potentially target every covalent bond connecting the amino acid and amino sugar building blocks within the peptidoglycan network (cell wall lytic complement). Many bacteria release a great amount of cell wall material during bacterial growth (cell elongation and division). The reason for the massive turnover of approximately 50% of the existing peptidoglycan in one generation is still unclear. Bacteria eventually recover cell wall turnover fragments. The pathways for the continuous recycling of peptidoglycan have been explored in great detail in Escherichia coli . Cell wall recycling in Gram‐positive bacteria has been appreciated just recently and apparently differs from the E. coli paradigm as well as between Gram‐positive species. Cell wall‐derived peptidoglycan fragments function as potent biological effectors. They are involved in sensing the cell wall and growth state, inducing expression of antibiotic resistance genes, and triggering cell differentiation and resuscitation of dormant cells.

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A matter of life and death: cell wall homeostasis and the WalKR (YycGF) essential signal transduction pathway

Cited by 268 publications

References 77 publications

Two-component signal transduction systems in oral bacteria

Two-component signal transduction systems in oral bacteria

Structural basis of PcsB-mediated cell separation in Streptococcus pneumoniae

Bacterial Cell Wall Recycling

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