Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and rodA protein.

Ishino, Fumitoshi; Park, W; Tomioka, Sadatake; Tamaki, Shigeo; Takase, Izumi; Kunugita, Kiyohiko; Matsuzawa, Hiroshi; Asoh, Sadamitsu; Ohta, Takao; Spratt, Brian G.

doi:10.1016/s0021-9258(19)62717-1

Cited by 140 publications

(26 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The third was a cell membrane division protein designated as rod shape-determining protein RodA (STER_1197). This protein contains the FtsW domain [ 47 ], which appears to be required in crossing peptidoglycan precursors outside the cell membrane and for peptidoglycan biosynthesis, thus being involved in maintaining cell shape and modulating cell-wall morphology [ 48 ]. Furthermore, it has been shown that the RodA protein is essential for the cell viability of Bacillus subtilis and to maintain cell surface shape [ 49 ].…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Identification of Streptococcus thermophilus Genes Specifically Expressed under Simulated Human Digestive Conditions Using R-IVET Technology

et al. 2021

View full text Add to dashboard Cite

Despite promising health effects, the probiotic status of Streptococcus thermophilus, a lactic acid bacterium widely used in dairy industry, requires further documentation of its physiological status during human gastrointestinal passage. This study aimed to apply recombinant-based in vivo technology (R-IVET) to identify genes triggered in a S. thermophilus LMD-9 reference strain under simulated digestive conditions. First, the R-IVET chromosomal cassette and plasmid genomic library were designed to positively select activated genes. Second, recombinant clones were introduced into complementary models mimicking the human gut, the Netherlands Organization for Applied Scientific Research (TNO) gastrointestinal model imitating the human stomach and small intestine, the Caco-2 TC7 cell line as a model of intestinal epithelium, and anaerobic batch cultures of human feces as a colon model. All inserts of activated clones displayed a promoter activity that differed from one digestive condition to another. Our results also showed that S. thermophilus adapted its metabolism to stressful conditions found in the gastric and colonic competitive environment and modified its surface proteins during adhesion to Caco-2 TC7 cells. Activated genes were investigated in a collection of S. thermophilus strains showing various resistance levels to gastrointestinal stresses, a first stage in the identification of gut resistance markers and a key step in probiotic selection.

show abstract

Section: Discussionmentioning

confidence: 99%

“… Synthetic view of main genes from S. thermophilus LMD-9 specifically induced in each GI models and their possible involvement in cell functions [ 43 , 46 , 47 , 48 , 50 , 52 , 53 , 58 , 59 , 60 , 61 ]. …”

Section: Figurementioning

confidence: 99%

Identification of Streptococcus thermophilus Genes Specifically Expressed under Simulated Human Digestive Conditions Using R-IVET Technology

et al. 2021

View full text Add to dashboard Cite

show abstract

“…However, recent landmark studies have identified RodA as a major TGase of the elongasome complex. Although RodA has long been known to be essential for peptidoglycan synthesis and maintenance of rod shape, its role was not well defined (138)(139)(140). RodA was recently discovered to be a TGase that is insensitive to moenomycin, a molecule that inhibits the glycosyltransferase activity of aPBPs.…”

Section: Elongation Synthesis: Scaffold Formation By Rod Complexmentioning

confidence: 99%

“…RodA, encoded by mrdB, belongs to the SEDS (shape, elongation, division, and sporulation) family of proteins (144). Glycan polymerization by RodA is followed by cross-linking of peptide stems by the cognate TPase PBP2 (penicillin binding protein 2), encoded by mrdA (140,143,145,146). PBP2 is a member of the class B PBPs (bPBPs), which comprise monofunctional high-molecular-weight PBPs.…”

Section: Elongation Synthesis: Scaffold Formation By Rod Complexmentioning

confidence: 99%

“…Beta-lactam antibiotics inhibit the transpeptidase domains of all PBPs by covalent modification of the active site (6). TPase activity of PBP2 is specifically inhibited by the beta-lactam mecillinam, leading to ovoid cells, making mecillinam a useful tool to study cell wall elongation processes (140,145,149,150). Physical interaction between the transmembrane domains of RodA and PBP2 lead to the activation of RodA TGase activity by PBP2 (151,152).…”

Section: Elongation Synthesis: Scaffold Formation By Rod Complexmentioning

confidence: 99%

See 1 more Smart Citation

Peptidoglycan: Structure, Synthesis, and Regulation

2021

View full text Add to dashboard Cite

Peptidoglycan is a defining feature of the bacterial cell wall. Initially identified as a target of the revolutionary beta-lactam antibiotics, peptidoglycan has become a subject of much interest for its biology, its potential for the discovery of novel antibiotic targets, and its role in infection. Peptidoglycan is a large polymer that forms a mesh-like scaffold around the bacterial cytoplasmic membrane. Peptidoglycan synthesis is vital at several stages of the bacterial cell cycle: for expansion of the scaffold during cell elongation and for formation of a septum during cell division. It is a complex multifactorial process that includes formation of monomeric precursors in the cytoplasm, their transport to the periplasm, and polymerization to form a functional peptidoglycan sacculus. These processes require spatio-temporal regulation for successful assembly of a robust sacculus to protect the cell from turgor and determine cell shape. A century of research has uncovered the fundamentals of peptidoglycan biology, and recent studies employing advanced technologies have shed new light on the molecular interactions that govern peptidoglycan synthesis. Here, we describe the peptidoglycan structure, synthesis, and regulation in rod-shaped bacteria, particularly Escherichia coli , with a few examples from Salmonella and other diverse organisms. We focus on the pathway of peptidoglycan sacculus elongation, with special emphasis on discoveries of the past decade that have shaped our understanding of peptidoglycan biology.

show abstract

Peptides

Wise

2000

Kirk-Othmer Encyclopedia of Chemical Technology

View full text Add to dashboard Cite

Peptide antibiotics are classified according to their overall shape, which can be linear or cyclic, and by the nature of the bonds joining the constituent amino acids and other carboxylic acids, which can be all amide bonds or amide plus ester bonds. Most peptide antibiotics are cyclic peptides that do not contain disulfide linkages. Peptide antibiotics differ in many respects from proteins. The vast majority of peptide antibiotics have molecular weights in the 500–1500 range, whereas the average protein has a mol wt of 40,000. Many peptide antibiotics have unusual fatty acids and amino acids, such as D ‐amino acids, N ‐methyl amino acids, or imino acids, and they usually lack methionine and histidine. Ring closure in cyclic peptide antibiotics is by amide or ester bonds. Peptide antibiotics are normally resistant to the usual proteases and peptidases. They are usually synthesized on multienzyme complexes much as are fatty acids, and not on ribosomes as are proteins. Most peptide antibiotics are synthesized as groups of closely related structures. Even the small fraction of peptide antibiotics that have therapeutic usefulness are quite toxic. The ratio of the minimum toxic dose to the maximum effective dose is smaller than for most nonpeptide antibiotics. Peptide antibiotics are not often the drugs of first choice for systemic therapy of important human disease. However, the World Health Organization, which chooses drugs especially for Third World use based on efficacy, safety, quality, price, and availability, includes such peptide antibiotics as bleomycin, dactinomycin, and bacitracin, plus several β‐lactams. The complex structure of peptide antibiotics adds considerably to the problems of synthesis, but more recent efforts toward improved peptide antibiotics are encouraging.

show abstract

Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and rodA protein.

Cited by 140 publications

References 29 publications

Identification of Streptococcus thermophilus Genes Specifically Expressed under Simulated Human Digestive Conditions Using R-IVET Technology

Identification of Streptococcus thermophilus Genes Specifically Expressed under Simulated Human Digestive Conditions Using R-IVET Technology

Peptidoglycan: Structure, Synthesis, and Regulation

Peptides

Contact Info

Product

Resources

About