Maturing Mycobacterium smegmatis peptidoglycan requires non-canonical crosslinks to maintain shape

• Main Authors: Baranowski, C, Welsh, M.A, Sham, L.-T, Eskandarian, H.A, Lim, H.C, Kieser, K.J, Wagner, J.C, McKinney, J.D, Fantner, G.E, Ioerger, T.R, Walker, S, Bernhardt, T.G, Rubin, E.J, Rego, E.H
• Other Authors: MICROBIOLOGY AND IMMUNOLOGY
• Format: Article
• Published: 2020
• Subjects: amoxicillin; amoxicillin plus clavulanic acid; beta lactam; binding protein; carbapenem; carboxypeptidase D; carboxypeptidase transpeptidase; hygromycin; meropenem; peptidoglycan; amino acid; aminoacyltransferase; cross linking reagent; penicillin binding protein; peptidoglycan transpeptidase; Agrobacterium tumefaciens; Article; atomic force microscopy; bacterial strain; bacterium culture; canonical analysis; cell division; controlled study; CRISPR Cas system; cross linking; daughter cell; Escherichia coli; fluorescence; fluorescence activated cell sorting; fractional anisotropy; genetic analysis; genetic linkage; genetic manipulation; MIC50; microscopy; minimum inhibitory concentration; morphological trait; Mycobacterium smegmatis; nonhuman; organelle shape; osmolarity; polymerization; population; protein expression; real time polymerase chain reaction; sequence analysis; single cell analysis; sputum analysis; time-lapse microscopy; tuberculosis; Bacillus; biological model; cell wall; chemistry; drug effect; kinetics; metabolism; microbial viability; Amino Acids; Aminoacyltransferases; Amoxicillin; Cell Wall; Cross-Linking Reagents; Fluorescence; Kinetics; Meropenem; Microbial Viability; Models, Biological; Penicillin-Binding Proteins; Peptidoglycan
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/177836
• Institution: National University of Singapore

10.7554/eLife.37516