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1. Full Text Suppression and syntheticā€lethal genetic relationships of Ī”gpsB mutations indicate that GpsB mediates protein phosphorylation and penicillinā€binding protein interactions in Streptococcus pneumoniae D39
by Rued, Britta E and Zheng, Jiaqi J and Mura, Andrea and Tsui, Hoā€Ching T and Boersma, Michael J and Mazny, Jeffrey L and Corona, Federico and Perez, Amilcar J and Fadda, Daniela and DoubravovĆ”, Linda and BuriĆ”nkovĆ”, KarolĆ­na and Branny, Pavel and Massidda, Orietta and Winkler, Malcolm E
Molecular Microbiology, ISSN 0950-382X, 03/2017, Volume 103, Issue 6, pp. 931 - 957
Summary GpsB regulatory protein and StkP protein kinase have been proposed as molecular switches that balance septal and peripheral (sideā€wall like)... 
Cell Division - genetics | Phosphorylation | Virulence Factors - genetics | Membrane Proteins - genetics | Aminoacyltransferases - genetics | Bacterial Proteins - genetics | Penicillin-Binding Proteins - genetics | Penicillin-Binding Proteins - metabolism | Mutation - genetics | Cell Division - physiology | Peptidoglycan - biosynthesis | Streptococcus pneumoniae - metabolism | Cell Wall - metabolism | Streptococcus pneumoniae - genetics | Aminoacyltransferases - metabolism | Bacterial Proteins - metabolism | Virulence Factors - metabolism | Membrane Proteins - metabolism | Base Composition - genetics | DivIVA function | bacterial protein phosphorylation | bacterial protein phosphatases | penicillin-binding protein (PBP) regulation | pneumococcal cell division
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2. Full Text Evolution of Pseudomonas aeruginosa antimicrobial resistance and fitness under low and high mutation rates
by Cabot, Gabriel and Zamorano, Laura and MoyĆ , BartolomĆ© and Juan, Carlos and Navas, Alfonso and BlĆ”zquez, JesĆŗs and Oliver, Antonio
Antimicrobial Agents and Chemotherapy, ISSN 0066-4804, 03/2016, Volume 60, Issue 3, pp. 1767 - 1778
Pseudomonas aeruginosa, a major cause of nosocomial and chronic infections, is considered a paradigm of antimicrobial resistance development. However, the... 
BETA-LACTAM RESISTANCE | OVEREXPRESSION | HIGH-RISK CLONES | GENETIC-DETERMINANTS | CYSTIC-FIBROSIS PATIENTS | MUTANT LIBRARY | ESCHERICHIA-COLI | PENICILLIN-BINDING PROTEINS | MICROBIOLOGY | PHARMACOLOGY & PHARMACY | LUNG INFECTION | HUMAN HOST ENVIRONMENT | Penicillin-Binding Proteins - genetics | DNA Mismatch Repair - genetics | Microbial Sensitivity Tests | Carbapenems - pharmacology | beta-Lactamases - genetics | Pseudomonas aeruginosa - pathogenicity | Membrane Transport Proteins - genetics | Base Sequence | Membrane Transport Proteins - metabolism | beta-Lactamases - metabolism | Cephalosporins - pharmacology | Porins - genetics | Bacterial Proteins - genetics | Mutation Rate | Pseudomonas aeruginosa - drug effects | Mutation - genetics | Sequence Analysis, DNA | DNA, Bacterial - genetics | Mutation - drug effects | DNA Gyrase - genetics | Pseudomonas aeruginosa - genetics | Fluoroquinolones - pharmacology | Bacterial Proteins - metabolism | Anti-Bacterial Agents - pharmacology | Drug Resistance, Multiple, Bacterial - genetics
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3. Full Text A widespread family of bacterial cell wall assembly proteins
by Kawai, Yoshikazu and Marlesā€Wright, Jon and Cleverley, Robert M and Emmins, Robyn and Ishikawa, Shu and Kuwano, Masayoshi and Heinz, Nadja and Bui, Nhat Khai and Hoyland, Christopher N and Ogasawara, Naotake and Lewis, Richard J and Vollmer, Waldemar and Daniel, Richard A and Errington, Jeff
The EMBO Journal, ISSN 0261-4189, 12/2011, Volume 30, Issue 24, pp. 4931 - 4941
Teichoic acids and acidic capsular polysaccharides are major anionic cell wall polymers (APs) in many bacteria, with various critical cell functions, including... 
peptidoglycan | LytRā€“CpsAā€“Psr proteins | capsular polysaccharide | MreB | teichoic acids | LytR-CpsA-Psr proteins | LOCALIZATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | DIVISION | CELL BIOLOGY | MORPHOGENESIS | SHAPE | BACILLUS-SUBTILIS | TEICHOIC-ACID BIOSYNTHESIS | PENICILLIN-BINDING PROTEINS | ACTIN HOMOLOG | Teichoic Acids - genetics | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Polysaccharides - genetics | Cell Wall - genetics | Bacillus subtilis - enzymology | Cell Wall - chemistry | Cytoskeleton - ultrastructure | Teichoic Acids - chemistry | Polysaccharides - biosynthesis | Bacillus subtilis - genetics | Genes, Lethal | Teichoic Acids - biosynthesis | Cell Wall - metabolism | Cytoskeleton - metabolism | Polysaccharides - chemistry | Bacterial Proteins - metabolism | Mutation | Bacillus subtilis - ultrastructure | Cytoskeleton - chemistry | Proteins | Cytoskeleton | Molecular biology | Polymers | Cells
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4. Full Text Movement dynamics of divisome proteins and PBP2x: FtsW in cells of Streptococcus pneumoniae
by Perez, Amilcar J and Cesbron, Yann and Shaw, Sidney L and Villicana, Jesus Bazan and Tsui, Ho-Ching T and Boersma, Michael J and Ye, Ziyun A and Tovpeko, Yanina and Dekker, Cees and Holden, Seamus and Winkler, Malcolm E
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 02/2019, Volume 116, Issue 8, pp. 3211 - 3220
Bacterial cell division and peptidoglycan (PG) synthesis are orchestrated by the coordinated dynamic movement of essential protein complexes. Recent studies... 
Microhole vertical imaging | FtsZ treadmilling | Nascent ring formation | TIRF microscopy | PBP2x:FtsW shared dynamics | microhole vertical imaging | WILD-TYPE | LOCALIZATION | ORGANIZES | WALL SYNTHESIS MACHINERY | DRIVES | MULTIDISCIPLINARY SCIENCES | PBP2x: FtsW shared dynamics | SUPPRESSION | DIVISION | nascent ring formation | MUTANTS | PEPTIDOGLYCAN SYNTHESIS | REVEALS | Cell Division - genetics | Cytoskeletal Proteins - genetics | Membrane Proteins - genetics | Humans | Streptococcus pneumoniae - ultrastructure | Bacterial Proteins - genetics | Cytoskeleton - genetics | Penicillin-Binding Proteins - genetics | Peptidoglycan - genetics | Cytoskeleton - ultrastructure | Cytoskeletal Proteins - ultrastructure | Peptidoglycan - biosynthesis | Streptococcus pneumoniae - pathogenicity | Escherichia coli - genetics | GTP Phosphohydrolases - genetics | Pneumococcal Infections - genetics | Streptococcus pneumoniae - genetics | Pneumococcal Infections - microbiology | Microscopy, Fluorescence | Streaming | Peptidoglycans | Cell division | Septum | Fluorescence | Bundles | Mutants | Streptococcus infections | Bundling | Proteins | Streptococcus | Synthesis | Filaments | Penicillin | Anchoring | Fluorescence microscopy | Guanosinetriphosphatase | Biological Sciences | PNAS Plus
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5. Full Text SEDS proteins are a widespread family of bacterial cell wall polymerases
by Meeske, Alexander J and Riley, Eammon P and Robins, William P and Uehara, Tsuyoshi and Mekalanos, John J and Kahne, Daniel and Walker, Suzanne and Kruse, Andrew C and Bernhardt, Thomas G and Rudner, David Z
Nature, ISSN 0028-0836, 08/2016, Volume 537, Issue 7622, pp. 634 - 638
Elongation of rod-shaped bacteria is mediated by a dynamic peptidoglycan-synthetizing machinery called the Rod complex. Here we report that, in Bacillus... 
BETA-LACTAM RESISTANCE | GENE | BACILLUS-SUBTILIS | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | PENICILLIN-BINDING PROTEINS | DYNAMICS | FLIPPASE | PEPTIDOGLYCAN SYNTHESIS | PRECURSORS | DIVISION | Peptidoglycan Glycosyltransferase - metabolism | Bacillus subtilis - cytology | Peptidoglycan Glycosyltransferase - chemistry | Penicillin-Binding Proteins - classification | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Polymerization | Penicillin-Binding Proteins - genetics | Bacillus subtilis - enzymology | Cell Wall - chemistry | Penicillin-Binding Proteins - metabolism | Oligosaccharides - pharmacology | Peptidoglycan - biosynthesis | Peptidoglycan Glycosyltransferase - genetics | Phenotype | Bacillus subtilis - growth & development | Cell Division | Cell Wall - metabolism | Drug Design | Bacterial Proteins - metabolism | Anti-Bacterial Agents - pharmacology | Drug Resistance, Bacterial - drug effects | Mutation | Bacillus subtilis - drug effects | Physiological aspects | Bacillus subtilis | Bacterial cell walls | Proteins | Antigens | Enzymes | Bacterial infections | Peptides | Penicillin | Bacteria | Lipids | Biosynthesis
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6. Full Text ZipA Is Required for FtsZ-Dependent Preseptal Peptidoglycan Synthesis prior to Invagination during Cell Division
by Lakshmi-Prasad Potluri and Suresh Kannan and Kevin D. Young
Journal of Bacteriology, ISSN 0021-9193, 10/2012, Volume 194, Issue 19, pp. 5334 - 5342
Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
ESCHERICHIA-COLI LOCALIZES | CAULOBACTER-CRESCENTUS | MUREIN SACCULUS | MREB | PENICILLIN-BINDING PROTEINS | MONOFUNCTIONAL GLYCOSYLTRANSFERASE | POLAR-CAP FORMATION | LATERAL WALL | MICROBIOLOGY | SEPTAL RING | BACTERIAL-CELL | Cytoskeletal Proteins - genetics | Penicillin-Binding Proteins - genetics | Escherichia coli - cytology | Serine-Type D-Ala-D-Ala Carboxypeptidase - genetics | Cell Division | Escherichia coli - metabolism | Cell Cycle Proteins - genetics | Cytoskeletal Proteins - metabolism | Serine-Type D-Ala-D-Ala Carboxypeptidase - metabolism | Endopeptidases - metabolism | Peptidoglycan Glycosyltransferase - metabolism | Bacterial Proteins - genetics | Cell Cycle Proteins - metabolism | Escherichia coli Proteins - metabolism | Penicillin-Binding Proteins - metabolism | N-Acetylmuramoyl-L-alanine Amidase - genetics | Gene Expression Regulation, Bacterial - physiology | N-Acetylmuramoyl-L-alanine Amidase - metabolism | Peptidoglycan - biosynthesis | Peptidoglycan Glycosyltransferase - genetics | Carrier Proteins - genetics | Carrier Proteins - metabolism | Endopeptidases - genetics | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Bacterial Proteins - metabolism | Bacterial growth | Proteobacteria | Growth | Physiological aspects | Cell division | Microbiological synthesis | Bacterial cell walls | Research | Chemical properties | Microbial polysaccharides
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7. Full Text The cell cycle regulator GpsB functions as cytosolic adaptor for multiple cell wall enzymes
by Cleverley, Robert M and Rutter, Zoe J and Rismondo, Jeanine and Corona, Federico and Tsui, Ho-Ching Tiffany and Alatawi, Fuad A and Daniel, Richard A and Halbedel, Sven and Massidda, Orietta and Winkler, Malcolm E and Winkler, Malcolm E and Lewis, Richard J
Nature Communications, ISSN 2041-1723, 12/2019, Volume 10, Issue 1, pp. 261 - 17
Bacterial growth and cell division requires precise spatiotemporal regulation of the synthesis and remodelling of the peptidoglycan layer that surrounds the... 
MINICELL LOCUS | STREPTOCOCCUS-PNEUMONIAE | FTSZ | MULTIDISCIPLINARY SCIENCES | GROWTH | PENICILLIN-BINDING PROTEIN | COMPONENT | IDENTIFICATION | PEPTIDOGLYCAN SYNTHESIS | DIVISION | REQUIREMENT | Virulence Factors - genetics | Bacterial Proteins - chemistry | Crystallography, X-Ray | Penicillin-Binding Proteins - genetics | Protein Interaction Maps | Cell Cycle Proteins - chemistry | Recombinant Proteins - isolation & purification | Penicillin-Binding Proteins - chemistry | Streptococcus pneumoniae - metabolism | Cell Division | Cell Cycle Proteins - genetics | Listeria monocytogenes - metabolism | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Recombinant Proteins - metabolism | Cell Cycle Proteins - isolation & purification | Bacterial Proteins - genetics | Cell Cycle Proteins - metabolism | Recombinant Proteins - chemistry | Virulence Factors - isolation & purification | Recombinant Proteins - genetics | Virulence Factors - chemistry | Penicillin-Binding Proteins - metabolism | Amino Acid Motifs | Peptidoglycan - biosynthesis | Penicillin-Binding Proteins - isolation & purification | Mutagenesis | Cell Wall - metabolism | Bacterial Proteins - metabolism | Cytosol - metabolism | Virulence Factors - metabolism | Bacterial Proteins - isolation & purification | Bacillus subtilis - metabolism | Enzymes | Cell walls | Peptidoglycans | Cell division | Listeria monocytogenes | Membrane proteins | Streptococcus infections | Proteins | Domains | Synthesis | Listeria | Scaffolding | Penicillin | Cell cycle | Bacteria | Viability
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8. Full Text The TIR Homologue Lies near Resistance Genes in Staphylococcus aureus, Coupling Modulation of Virulence and Antimicrobial Susceptibility
by Patot, Sabine and Imbert, Paul R.C and Baude, Jessica and Martins SimƵes, Patricia and Campergue, Jean-Baptiste and Louche, Arthur and Nijland, Reindert and BĆØs, MichĆØle and Tristan, Anne and Laurent, FrĆ©dĆ©ric and Fischer, Aien and Schrenzel, Jacques and Vandenesch, FranƧois and Salcedo, Suzana P and FranƧois, Patrice and Lina, GĆ©rard and Prince, Alice
PLoS Pathogens, ISSN 1553-7366, 2017, Volume 13, Issue 1, p. e1006092
Toll/interleukin-1 receptor (TIR) domains in Toll-like receptors are essential for initiating and propagating the eukaryotic innate immune signaling cascade.... 
STRAINS | SYSTEM | CONTAINING PROTEINS | MICROBIOLOGY | CASSETTE CHROMOSOME MEC | VECTOR | FAMILY | EVOLUTION | VIROLOGY | GENOMES | BTPB | CLONES | PARASITOLOGY | Virulence Factors - genetics | Humans | Receptors, Interleukin-1 - genetics | Penicillin-Binding Proteins - genetics | Virulence Factors - immunology | Signal Transduction - immunology | Staphylococcal Skin Infections - drug therapy | HEK293 Cells | Bacterial Proteins - immunology | Fusidic Acid - pharmacology | Membrane Glycoproteins - immunology | Macrophages - immunology | Disease Models, Animal | Staphylococcus aureus - genetics | Cell Line | Receptors, Interleukin-1 - immunology | Mice, Inbred C57BL | Bacterial Proteins - genetics | Myeloid Differentiation Factor 88 - genetics | Neutrophils - immunology | Staphylococcus aureus - pathogenicity | Membrane Glycoproteins - genetics | Mice, Knockout | Animals | Myeloid Differentiation Factor 88 - deficiency | Toll-Like Receptors - genetics | Staphylococcus aureus - immunology | Mice | Staphylococcal Skin Infections - microbiology | Bacterial infections | Disease transmission | Gene mutations | Analysis | Genetic aspects | Research | Bacterial genetics | Epidemiology | Risk factors | Studies | Pathogens | Medical research | Enzymes | Cytokines | Laboratories | Genes | Antimicrobial agents | Staphylococcus infections | Genetic engineering | Experiments | Life Sciences | Microbiology and Parasitology | Immunology | Bacteriology | Virology | Laboratory of Phytopathology | EPS | Laboratorium voor Phytopathologie | Laboratorium voor Fytopathologie
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9. Full Text Genes sufficient for synthesizing peptidoglycan are retained in gymnosperm genomes, and MurE from Larix gmelinii can rescue the albino phenotype of arabidopsis MurE mutation
by Lin, Xiaofei and Li, Ningning and Kudo, Hiromi and Zhang, Zhe and Li, Jinyu and Wang, Li and Zhang, Wenbo and Takechi, Katsuaki and Takano, Hiroyoshi
Plant and Cell Physiology, ISSN 0032-0781, 03/2017, Volume 58, Issue 3, pp. 587 - 597
The endosymbiotic theory states that plastids are derived from a single cyanobacterial ancestor that possessed a cell wall. Peptidoglycan ( PG), the main... 
Gymnosperm | Larix gmelinii | Evolution | Plastid peptidoglycan | Chloroplast | MurE | ANTIBIOTICS | MOSS | CYANELLE PEPTIDOGLYCAN | SYNTHESIS PATHWAY | PLANT SCIENCES | CELL BIOLOGY | CYANOPHORA-PARADOXA | CELL-WALL | PLASTID DIVISION | PHYSCOMITRELLA-PATENS | CHLOROPLAST DIVISION | N-ACETYLPUTRESCINE | Cyanobacteria - genetics | Peptidoglycan - metabolism | Green Fluorescent Proteins | Pinus taeda - genetics | Arabidopsis - enzymology | Genes, Plant | Cyanobacteria - metabolism | Penicillin-Binding Proteins - genetics | Magnoliopsida - genetics | DNA, Bacterial | Arabidopsis Proteins - metabolism | Bryopsida - metabolism | Bryopsida - genetics | Gene Expression Regulation, Plant | Plastids - genetics | Plastids - metabolism | Plant Proteins - metabolism | Chloroplasts - genetics | Genes, Bacterial | Arabidopsis Proteins - genetics | Seeds - metabolism | Seeds - genetics | Bacterial Proteins - genetics | Cell Wall - genetics | Larix - metabolism | Peptidoglycan - genetics | Cycadopsida - genetics | Genome, Plant | Penicillin-Binding Proteins - metabolism | Gene Knockout Techniques | Chloroplasts - metabolism | Arabidopsis - metabolism | Cycadopsida - metabolism | Larix - genetics | Arabidopsis - genetics | Plant Proteins - genetics | Phenotype | Plant Leaves - genetics | Cell Wall - metabolism | Picea - genetics | Mutation
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10. Full Text Control of the cell elongationā€“division cycle by shuttling of PBP1 protein in Bacillus subtilis
by Claessen, Dennis and Emmins, Robyn and Hamoen, Leendert W and Daniel, Richard A and Errington, Jeff and Edwards, David H
Molecular Microbiology, ISSN 0950-382X, 05/2008, Volume 68, Issue 4, pp. 1029 - 1046
Summary The characteristic shape of bacterial cells is mainly determined by the cell wall, the synthesis of which is orchestrated by penicillinā€binding... 
PENICILLIN-BINDING-PROTEINS | SHAPE DETERMINATION | CAULOBACTER-CRESCENTUS | SYNTHETIC LETHAL | PLASMID PLS20 | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | BACTERIAL CYTOSKELETON | MICROBIOLOGY | CHROMOSOME SEGREGATION | ACTIN HOMOLOG | WALL SYNTHESIS | Cell Division - genetics | Amino Acid Sequence | Cell Cycle - genetics | Cell Cycle Proteins - analysis | Green Fluorescent Proteins - analysis | Bacillus subtilis - cytology | Bacterial Proteins - genetics | Cell Cycle Proteins - metabolism | Molecular Sequence Data | Penicillin-Binding Proteins - genetics | Green Fluorescent Proteins - genetics | Penicillin-Binding Proteins - metabolism | Bacterial Proteins - analysis | Bacillus subtilis - genetics | Genes, Lethal | Two-Hybrid System Techniques | Penicillin-Binding Proteins - analysis | Cell Cycle Proteins - genetics | Bacterial Proteins - metabolism | Mutation | Bacillus subtilis - metabolism | Proteins
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