@article{89866, keywords = {Bacterial Proteins, Mutation, Escherichia coli, Genes, Bacterial, Anti-Bacterial Agents, Microbial Sensitivity Tests, Genetic Complementation Test, Phenotype, Oligosaccharides, Lipoproteins, Enzyme Inhibitors, Glycosylation, Peptidoglycan, Vancomycin, Drug Resistance, Microbial, Vancomycin Resistance, Drug Resistance, Multiple, Hexosyltransferases, N-Acetylmuramoyl-L-alanine Amidase, Peptidoglycan Glycosyltransferase}, author = {Eggert and Ruiz and Falcone and Branstrom and Goldman and Silhavy and Kahne}, title = {Genetic basis for activity differences between vancomycin and glycolipid derivatives of vancomycin}, abstract = {
Small molecules that affect specific protein functions can be valuable tools for dissecting complex cellular processes. Peptidoglycan synthesis and degradation is a process in bacteria that involves multiple enzymes under strict temporal and spatial regulation. We used a set of small molecules that inhibit the transglycosylation step of peptidoglycan synthesis to discover genes that help to regulate this process. We identified a gene responsible for the susceptibility of Escherichia coli cells to killing by glycolipid derivatives of vancomycin, thus establishing a genetic basis for activity differences between these compounds and vancomycin.
}, year = {2001}, journal = {Science}, volume = {294}, pages = {361-4}, month = {10/2001}, issn = {0036-8075}, doi = {10.1126/science.1063611}, language = {eng}, }