Download

Full Text

• Adachi, H., Ohta, T., Matsuzawa, H. 1987. A water-soluble form of penicillin-binding protein 2 of Escherichia coli constructed by site-directed mutagenesis. FEBS Lett. 226:150-54
• Adam, M., Damblon, C., Plaiton, B., Christiaens, L., Frère, J. M. 1990. Chromogenic depsipeptide substrates for β-lactamases and penicillin-sensitive DD-peptidases. Biochem. J. 270:525-29
• Adriaens, P., Meesschaert, B., Frère, J.-M., Vanderhaege, H., Degelaen, J., et al. 1978. Stability of D-5,5-dimethyl-Δ2-thiazolidine-4-carboxylic acid in relation to its possible occurrence as a degradation product of penicillin by the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61 and the membrane-bound DD-carboxypeptidase from Bacillus stearothermophilus. J. Biol. Chem. 253:3660-65
• Ambler, R. P., Frère, J.-M., Ghuysen, J.-M., Jaurin, B., Levesque, R. C., et al. 1991. A standard numbering scheme for the class A β-lactamases. Biochem. J. In press
• Asoh, S., Matsuzawa, H., Ishino, F., Strominger, J. L., Matsuhashi, M., et al. 1986. Nucleotide sequence of the pbpA gene and characteristics of the deduced amino acid sequence of penicillin-binding protein 2 of Escherichia coli K12. Eur. J. Biochem. 160:231-38
• Bartholomé-De Belder, J., Nguyen-Distèche, M., Houba-Herin, N., Ghuysen, J.-M., Maruyama, I. N., et al. 1988. Overexpression, solubilization and refolding of a genetically engineered derivative of the penicillin-binding protein 3 of Escherichia coli K12. Mol. Microbiol. 2:519-25
• Beall, B., Lowe, M., Lutkenhaus, J. 1988. Cloning and characterization of Bacillus subtilis homologs of Escherichia coli cell division genes ftsZ and ftsA. J. Bacteriol. 170:4855-64
• Begg, K. J., Spratt, B. G., Donachie, W. D. 1986. Interaction between membrane proteins PBP3 and RodA is required for normal cell shape and division in Escherichia coli. J. Bacteriol. 167: 1004-8
• Begg, K. J., Takasuga, A., Edwards, D. H., Dewar, S. J., Spratt, B. G., et al. 1990. The balance between different peptidoglycan precursors determines whether Escherichia coli will elongate or divide. J. Bacteriol. 172:6697-6703
• Bentley, P. H., Stachulski, A. V. 1983. Synthesis and biological activity of some fused β-lactam peptidoglycan analogues. J. Chem. Soc. Perkin Trans. 1:1187-92
• Boissinot, M., Levesque, R. C. 1990. Nucleotide sequence of the PSE-4 carbenicillinase gene and correlations with the Staphylococcus aureus PC1 β-lactamase crystal structure. J. Biol. Chem. 265:1225-30
• Bouloc, P., Jaffé, A., D'Ari, R. 1989. The Escherichia coli lov gene product connects peptidoglycan synthesis, ribosomes and growth rate. EMBO J. 8:317-23
• Bowler, L. D., Spratt, G. D. 1989. Membrane topology of penicillin-binding protein 3 of Escherichia coli. Mol. Microbiol. 3:1277-86
• Brannigan, J. A., Tirodimos, I. A., Zhang, Q.-Y., Dowson, C. G., Spratt, B. G. 1990. Insertion of an extra amino acid is the main cause of the low affinity of penicillin-binding protein 2 in penicillin-resistant strains of Neisseria gonorrhoeae. Mol. Microbiol. 4:913-19
• Broome-Smith, J. K., Edelman, A., Yousif, S., Spratt, B. G. 1985. The nucleotide sequences of the ponA and ponB genes encoding penicillin-binding proteins 1A and 1B of Escherichia coli. Eur. J. Biochem. 147:437-46
• Broome-Smith, J. K., Ioannidis, I., Edelman, A., Spratt, B. G. 1988. Nucleotide sequences of the penicillin-binding protein 5 and 6 genes of Escherichia coli. Nucleic Acids Res. 16: 1617
• Buchanan, C. E., Neyman, S. L. 1986. Correlation of penicillin-binding protein composition with different functions of two membranes in Bacillus subtilis forespores. J. Bacteriol. 165:498-503
• Cartwright, S. J., Coulson, A. E. W. 1980. Active-site of staphylococcal β-lactamase. Phil. Trans. R. Soc. London B289:370-72
• Cartwright, S. J., Waley, S. G. 1983. β-Lactamase inhibitors. Med. Res. Rev. 3:341-82
• Chan, P. T. 1986. Nucleotide sequence of the Staphylococcus aureus PC1 β-lactamase gene. Nucleic Acids Res. 14:5940
• Cohen, S. A., Pratt, R. F. 1980. Inactivation of Bacillus cereus β-lactamase I by 6β-bromopenicillanic acid. Mechanism. Biochemistry 19:3996-4003
• Collatz, E., Labia, R., Gutman, L. 1990. Molecular evolution of ubiquitous β-lactamases toward extended-spectrum enzymes active against newer β-lactam antibiotics. Mol. Microbiol. 4:1615-20
• Dale, J. W., Godwin, D., Mossakouska, D., Stephenson, P., Wall, S. 1985. Sequence of the Oxa-2 β-lactamase: comparison with other penicillin-reactive enzymes. FEBS Lett. 191:39-42
• Dehottay, P., Dusart, J., De Meester, F., Joris, B., Van Beeumen, J., et al. 1987. Nucleotide sequence of the gene encoding the Streptomyces albus G β-lactamase precursor. Eur. J. Biochem. 166:345-50
• den Blaauven, T., Aarsman, M., Nanninga, N. 1990. Interaction of monoclonal antibodies with the enzymatic domains of penicillin-binding protein 1b of Escherichia coli. J. Bacteriol. 172:63-70
• Dideberg, O., Charlier, P., Wéry, J. P., Dehottay, P., Dusart, J., et al. 1987. The crystal structure of the β-lactamase of Streptomyces albus G at 0.3 nm resolution. Biochem. J. 245:911-13
• Dowson, C. G., Hutchison, A., Brannigan, J. A., George, R. C., Hansman, D., et al. 1989. Horizontal transfer of penicillin-binding protein genes in penicillin-resistant clinical isolates of Streptococcus pneumoniae. Proc. Natl. Acad. Sci. USA 86:8842-46
• Dowson, C. G., Hutchison, A., Spratt, B. G. 1989. Extensive re-modelling of the transpeptidase domain of penicillin-binding protein 2B of a penicillin-resistant South African isolate of Streptococcus pneumoniae. Mol. Microbiol. 3:95-102
• Dowson, C. G., Hutchison, A., Spratt, B. G. 1989. Nucleotide sequence of penicillin-binding protein 2B gene of Streptococcus pneumoniae strain R6. Nucleic Acids Res. 17:7518
• Dowson, C. G., Hutchison, A., Woodford, N., Johnson, A. P., George, R. C., et al. 1990. Penicillin-resistant viridans streptococci have obtained altered penicillin-binding protein genes from penicillin-resistant strains of Streptococcus pneumoniae. Proc. Natl. Acad. Sci. USA 87:5858-62
• Duez, C., Piron-Fraipont, C., Joris, B., Dusart, J., Urdea, M. S., et al. 1987. Primary structure of the Streptomyces R61 extracellular DD-peptidase. I. Cloning into Streptomyces lividans and nucleotide sequence of the gene. Eur. J. Biochem. 162:509-18
• Edelman, A., Bowler, L., Broome-Smith, J. K., Spratt, B. G. 1987. Use of a β-lactamase fusion vector to investigate the organization of penicillin-binding protein 1B in the cytoplasmic membrane of Escherichia coli. Mol. Microbiol. 1:101-6
• El Kharroubi, A., Jacques, P., Piras, G., Coyette, J., Van Beeumen, J., et al. 1991. The penicillin-binding proteins 5 of Enterococcus hirae R40 and the penicillin-binding protein 2′ of the methicillin-resistant Staphylococcus aureus are homologs. J. Bacteriol. In press
• El Kharroubi, A., Piras, G., Jacques, P., Szabo, I., Van Beeumen, J., et al. 1989. Active-site and membrane topology of the DD-peptidase/penicillin-binding protein no6 of Enterococcus hirae (Streptococcus faecium) ATCC9790. Biochem. J. 262:457-62
• Ferreira, L. C. S., Schwarz, U., Keck, W., Charlier, P., Dideberg, O., et al. 1988. Properties and crystallization of a genetically engineered, water-soluble derivative of the penicillin-binding protein no5 of Escherichia coli K12. Eur. J. Biochem. 171:11-16
• Fisher, J., Charnas, P. L., Bradley, S. M., Knowles, J. R. 1981. Inactivation of the RTEM β-lactamase from Escherichia coli. Interaction of penam sulfones with enzyme. Biochemistry 20: 2726-31
• Frère, J.-M., Duez, C., Ghuysen, J.-M., Vandekerkhove, J. 1976. Occurrence of a serine residue in the penicillin-binding site of the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61. FEBS Lett. 70:257-60
• Frère, J.-M., Ghuysen, J.-M., Degelaen, J., Loffet, A., Perkins, H. R. 1975. Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39. Nature 258:168-70
• Frère, J.-M., Ghuysen, J.-M., De Graeve, J. 1978. Fragmentation of penicillin catalysed by the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61. Isotopic study of hydrogen fixation on carbon 6. FEBS Lett. 88:147-50
• Frère, J.-M., Ghuysen, J.-M., Vanderhaeghe, H., Adriaens, P., Degelaen, J. 1976. Fate of thiazolidine ring during fragmentation of penicillin by exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61. Nature 260:451-54
• Frère, J.-M., Ghuysen, J.-M., Perkins, H. R., Nieto, M. 1973. Kinetics of concomitant transfer and hydrolysis reactions catalysed by the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61. Biochem. J. 135: 483-92
• Frère, J.-M., Joris, B. 1985. Penicillin-sensitive enzymes in peptidoglycan biosynthesis. CRC Crit. Rev. Microbiol. 11:299-396
• Galleni, M., Amicosante, G., Frère, J.-M. 1988. A survey of the kinetic parameters of class C β-lactamases. Biochem. J. 255:119-22
• Garcia-Bustos, J., Tomasz, A. 1990. A biological price of antibiotic resistance: major changes in the peptidoglycan structure of penicillin-resistant pneumococci. Proc. Natl. Acad. Sci. USA 87: 5415-19
• Ghuysen, J.-M. 1977. The bacterial DD-carboxypeptidase-transpeptidase enzyme system. A new insight into the mode of action of penicillin. E. R. Squibb Lectures on Chemistry of Microbial Products, series ed. W. E. Brown. Tokyo: Univ. Tokyo Press. 162 pp.
• Ghuysen, J.-M., Frère, J.-M., Leyh-Bouille, M., Coyette, J., Dusart, J., et al. 1979. Use of model enzymes in the determination of the mode of action of penicillins and Δ3-cephalosporins. Annu. Rev. Biochem. 48:73-101
• Ghuysen, J.-M., Frère, J.-M., Leyh-Bouille, M., Nguyen-Distèche, M., Coyette, J. 1986. Active-site serine D-alanyl-D-alanine-cleaving peptidases-catalysed acyl transfer reactions. Procedures for studying the penicillin-binding proteins of bacterial plasma membranes. Biochem. J. 235:159-65
• Ghuysen, J.-M., Leyh-Bouille, M., Campbell, J. N., Moreno, R., Frère, J.-M., et al. 1973. Structure of the wall peptidoglycan of Streptomyces R39 and the specificity profile of its exocellular DD-carboxypeptidase-transpeptidase for peptide acceptors. Biochemistry 12: 1243-51
• Ghuysen, J.-M., Reynolds, P. E., Perkins, H. R., Frère, J.-M., Moreno, R. 1974. Effects of donor and acceptor peptides on concomitant hydrolysis and transfer reactions catalysed by the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R39. Biochemistry 13:2539-47
• Gibson, R. S., Christensen, H., Waley, S. G. 1990. Site-directed mutagenesis of β-lactamase I. Single and double mutants of Glu166 and Lys73. Biochem. J. 272:613-19
• Gutherie, B., Wickner, W. 1990. Trigger factor depletion and overproduction causes defective cell division but does not block protein export. J. Bacteriol. 172:5555-62
• Hall, A., Knowles, J. R. 1976. Directed selective pressure on a β-lactamase to analyse molecular changes involved in development of enzyme function. Nature London 264:803-4
• Hara, H., Nishimura, Y., Kato, J. I., Suzuki, H., Nagasawa, H., et al. 1989. Genetic analysis of processing involving C-terminal cleavage in penicillin-binding protein 3 of Escherichia coli. J. Bacteriol. 171:5882-89
• Hedge, P. J., Spratt, B. G. 1985. Resistance to β-lactam antibiotics by remodelling the active site of an E. coli penicillin-binding protein. Nature 318: 478-80
• Hedge, P. J., Spratt, B. G. 1985. Amino acid alterations that reduce the affinity of penicillin-binding protein 3 of Escherichia coli for cephalexin. Eur. J. Biochem. 151:111-21
• Hedge, P. J., Spratt, B. G. 1988. A gene fusion that localises the penicillin-binding domains of penicillin-binding protein 3. J. Bacteriol. 170:5392-95
• Herzberg, O., Moult, J. 1987. Bacterial resistance to β-lactam antibiotics: crystal structure of β-lactamase from Staphylococcus aureus PC1 at 2.5 Å resolution. Science 236:694-701
• Hussain, M., Pastor, F. I. J., Lampen, J. O. 1987. Cloning and sequencing of the blaZ gene encoding β-lactamase III, a lipoprotein of Bacillus cereus 569/H. J. Bacteriol. 169:579-86
• Ikeda, M., Sato, T., Wachi, M., Jung, H. K., Ishino, F., et al. 1989. Structural similarity among Escherichia coli FtsW and RodA proteins and Bacillus subtilis SpoVE protein, which function in cell division, cell elongation, and spore formation, respectively. J. Bacteriol. 171:6375-78
• Ishino, F., Mitsui, S., Tamaki, S., Matsuhashi, M. 1980. Dual enzymatic activities of cell wall peptidoglycan synthesis, peptidoglycan transglycosylase and penicillin-sensitive transpeptidase in purified preparations of Escherichia coli penicillin-binding protein 1A. Biochem. Biophys. Res. Commun. 97:287-93
• Ishino, F., Park, W., Tomioka, S., Tamaki, S., Takase, I., et al. 1986. Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and RodA protein. J. Biol. Chem. 262:7024-31
• Jackson, M. E., Pratt, J. M. 1988. Analysis of the membrane-binding domain of penicillin-binding protein 5 of Escherichia coli. Mol. Microbiol. 2:563-68
• Jacob, F., Joris, B., Dideberg, O., Dusart, J., Ghuysen, J.-M., et al. 1990. Engineering of a novel β-lactamase by a single point mutation. Protein Eng. 4:223:6427-37
• Jacob, F., Joris, B., Lepage, S., Dusart, J., Frère, J.-M. 1990. Role of the conserved amino acids of the "SDN" loop in a class A β-lactamase studied by site-directed mutagenesis. Biochem. J. 271: 399-406
• Jones, C. A., Holland, I. B. 1985. Role of the SfiB (FtsZ) protein in division inhibition during the SDS response in E. coli. FtsZ stabilizes the inhibitor SfiA in maxicells. Proc. Natl. Acad. Sci. USA 82:6045-49
• Joris, B., Dive, G., Henriques, A., Piggot, P. J., Ghuysen, J.-M. 1990. The life-cycle proteins RodA of Escherichia coli and SpoVE of Bacillus subtilis have very similar primary structures. Mol. Microbiol. 4:513-17
• Joris, B., Ghuysen, J.-M., Dive, G., Renard, A., Dideberg, O. et al. 1988. The active-site serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family. Biochem. J. 250:313-24
• Joris, B., Ledent, P., Dideberg, O., Fonzé, E., Lamotte-Brasseur, J., et al. 1991. A comparison of the sequences of class A β-lactamases and of the secondary structure elements of penicillin-recognizing proteins. Biochem. J. In press
• Joris, B., Ledent, P., Kobayashi, T., Lampen, J. O., Ghuysen, J.-M. 1990. Expression in Escherichia coli of the Met346-Arg601 carboxy terminal domain of the BLAR sensory transducer protein of Bacillus licheniformis as a water-soluble 26,000-Mr penicillin-binding protein. FEMS Microbiol. Lett. 70:107-14
• Kelly, J. A., Dideberg, O., Charlier, P., Wéry, J. P., Libert, M., et al. 1986. On the origin of bacterial resistance to penicillin. Comparison of a β-lactamase and a penicillin target. Science 231:1429-37
• Kelly, J. A., Knox, J. R., Zhao, H., Frère, J.-M., Ghuysen, J.-M. 1989. Crystallographic mapping of β-lactams bound to a D-alanyl-D-alanine peptidase target enzyme. J. Mol. Biol. 209:281-95
• Knott-Hunziker, V., Waley, S. G., Orlek, B. S., Sammes, P. G. 1979. Penicillinase active sites: labelling of serine-44 in β-lactamase I by 6β-bromopenicillanic acid. FEBS Lett. 99:59-61
• Knox, J. R., Pratt, R. F. 1990. Different modes of vancomycin and D-alanyl-D-alanine peptidase binding to cell wall peptide and a possible role for the vancomycin resistance protein. Antimicrob. Agents Chemother. 34:1342-47
• Kobayashi, T., Zhu, Y., Nicholls, N., Lampen, J. O. 1987. A second regulatory gene, BLAR1, encoding a potential penicillin-binding protein required for induction of β-lactamase in Bacillus licheniformis. J. Bacteriol. 169:3873-78
• Laible, G., Hakenbeck, R., Sicard, M. A., Joris, B., Ghuysen, J.-M. 1989. Nucleotide sequences of the pbpX genes encoding the penicillin-binding proteins 2X from Streptococcus pneumoniae R6 and a cefotaxime resistant mutant, C50G. Mol. Microbiol. 3:1337-48
• Lamotte-Brasseur, J., Dive, G., Dehareng, D., Ghuysen, J.-M. 1990. Electrostatic potential maps at the quantum chemistry level of the active sites of the serine peptidases, α-chymotrypsin and subtilisin. J. Theor. Biol. 145:183-98
• Lamotte-Brasseur, J., Dive, G., Ghuysen, J.-M. 1991. Conformational analysis of β- and -lactam antibiotics. Eur. J. Med. Chem. In press
• Leyh-Bouille, M., Nguyen-Distèche, M., Bellefroid-Bourguignon, C., Ghuysen, J.-M. 1987. Effects of thiol reagents on the Streptomyces K15 DD-peptidase-catalysed reactions. Biochem. J. 241:893-97
• Leyh-Bouille, M., Nguyen-Distèche, M., Pirlot, S., Veithen, A., Bourguignon, C., et al. 1986. Streptomyces K15 DD-peptidase-catalysed reaction with suicide β-lactam carbonyl donors. Biochem. J. 235:177-82
• Lindberg, F., Normark, S. 1986. Sequence of the Citrobacter freundii chromosomal ampC β-lactamase gene. Eur. J. Biochem. 156:441-15
• Marquet, A., Frère, J.-M., Ghuysen, J.-M., Loffet, A. 1979. Effects of nucleophiles on the breakdown of the benzylpenicilloyl-enzyme complex EI* formed between benzylpenicillin and the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces strain R61. Biochem. J. 177:909-16
• Matsuzawa, H., Asoh, S., Kunai, K., Muraiso, K., Takasuga, A., et al. 1989. Nucleotide sequence of the rodA gene, responsible for the rod shape of Escherichia coli: rodA and the pbpA gene, encoding penicillin-binding protein 2, constitute the rodA operon. J. Bacteriol. 171:558-60
• Moews, P. C., Knox, J. R., Dideberg, O., Charlier, P., Frère, J.-M. 1990. β-Lactamase of Bacillus licheniformis 749/ C at 2 Å resolution. Proteins Struct. Funct. Genet. 7:156-71
• Mottl, H., Terpstra, P., Keck, W. 1991. Penicillin-binding protein 4 of Escherichia coli shows a novel type of primary structure among penicillin-interacting proteins. FEMS Microbiol. Lett. 78:213-20
• Nagasawa, H., Sakagami, Y., Suzuki, A., Suzuki, H., Hara, H., et al. 1989. Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli. J. Bacteriol. 171:5890-93
• Nakagawa, J.-I., Tamaki, S., Matsuhashi, M. 1979. Purified penicillin-binding protein 1Bs from Escherichia coli membranes showing activities of both peptidoglycan polymerase and peptidoglycan crosslinking enzyme. Agric. Biol. Chem. 43:1379-80
• Nakamura, M., Maruyama, I. N., Soma, M., Kato, J. I., Suzuki, H., et al. 1983. On the process of cellular division in Escherichia coli: nucleotide sequence of the gene for penicillin-binding protein 3. Mol. Gen. Genet. 191:1-9
• Neugebauer, K., Sprengl, R., Shaller, H. 1981. Penicillinase from Bacillus licheniformis: nucleotide sequence of the gene and implications for the biosynthesis of a secretory protein in a Gram-positive bacteria. Nucleic Acids Res. 9:2577-88
• Nguyen-Distèche, M., Leyh-Bouille, M., Pirlot, S., Frère, J.-M., Ghuysen, J.-M. 1986. Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors. Biochem. J. 235:167-76
• Oefner, C., D'Arcy, A., Daly, J. J., Gubernator, K., Charnas, R. L., et al. 1990. Refined crystal structure of β-lactamase from Citrobacter freundii indicates a mechanism for β-lactam hydrolysis. Nature 343:284-88
• Ogura, T., Bouloc, P., Niki, H., D'Ari, R., Horaga, S., et al. 1989. Penicillin-binding protein 2 is essential in wild-type Escherichia coli but not in lov and cya mutants. J. Bacteriol. 171:3025-30
• Pazhanisamy, S., Govardhan, C. P., Pratt, R. F. 1989. β-Lactamase-catalysed aminolysis of depsipeptides: amine specificity and steady-state kinetics. Biochemistry 28:6863-70
• Pazhanisamy, S., Pratt, R. F. 1989. β-Lactamase-catalysed aminolysis of depsipeptides: proof of the nonexistence of a specific D-phenylalanine/enzyme complex by double-label isotope trapping. Biochemistry 28:6870-75
• Pazhanisamy, S., Pratt, R. F. 1989. β-Lactamase-catalysed aminolysis of depsipeptides: peptide inhibition and a new kinetic mechanism. Biochemistry 28: 6875-82
• Perkins, H. R., Nieto, M., Frère, J.-M., Leyh-Bouille, M., Ghuysen, J.-M. 1973. Streptomyces DD-carboxypeptidases as transpeptidases. The specificity for amino compounds acting as carboxyl acceptors. Biochem. J. 131:707-18
• Pigott, J. J., Coote, J. G. 1976. Genetic aspects of bacterial endospore formation. Bacteriol. Rev. 40:908-62
• Piras, G., El Kharroubi, A., Van Beeumen, J., Coeme, E., Coyette, J., et al. 1990. Occurrence and characterization of a penicillin-binding protein 3 of low penicillin affinity in Enterococcus hirae. J. Bacteriol. 172:6856-62
• Pratt, J. M., Jackson, M. E., Holland, I. B. 1986. The C-terminus of penicillin-binding protein 5 is essential for localisation to the E. coli inner membrane. EMBO J. 5:2399-2405
• Robinson, A. C., Begg, K. J., Sweeney, J., Condie, A., Donachie, W. D. 1988. Mapping and characterization of mutants of the Escherichia coli cell division gene, ftsA. Mol. Microbiol. 2: 581-88
• Samuni, A., Citri, N. 1979. How specific is the effect of penicillins on the conformation of penicillinase? An experimental model. Mol. Pharmacol. 16:250-55
• Schuster, C., Dobrinkski, B., Hakenbeck, R. 1990. Unusual septum formation in Streptococcus pneumoniae mutants with an alteration in the D, D-carboxypeptidase penicillin-binding protein 3. J. Bacteriol. 172:6499-6505
• Song, M. D., Wachi, M., Doi, M., Ishino, F., Matsuhashi, M. 1987. Evolution of an inducible penicillin-target protein in methicillin-resistant Staphylococcus aureus by gene fusion. FEBS Lett. 221:167-71
• Sougakoff, W., Petit, A., Goussard, S., Sirot, D., Bure, A., et al. 1989. Characterization of the plasmid genes blaT-4 and blaT-5 which encode the brood-spectrum β-lactamases TEM-4 and TEM-5 in Enterobacteriaceae. Gene 78:339-48
• Spratt, B. G. 1988. Hybrid penicillin-binding proteins in penicillin-resistant strains of Neisseria gonorrhoeae. Nature 332:173-76
• Spratt, B. G., Cromie, K. D. 1988. Penicillin-binding proteins of Gram-negative bacteria. Rev. Infect. Dis. 10: 699-711
• Spratt, B. G., Pardee, A. B. 1975. Penicillin-binding proteins and cell shape in E. coli. Nature 254:516-17
• Spratt, B. G., Zhang, Q.-Y., Jones, D. M., Hutchison, A., Brannigan, J. A., et al. 1989. Recruitment of a penicillin-binding protein gene from Neisseria flavescens during the emergence of penicillin-resistance in Neisseria meningitidis. Proc. Natl. Acad. Sci. USA 86: 8988-92
• Stoker, N. G., Broome-Smith, J. K., Edelman, A., Spratt, B. G. 1983. Organization and subcloning of the dacA-rodA-pbpA cluster of cell shape genes in Escherichia coli. J. Bacteriol. 155:847-59
• Suzuki, S., van Heijenoort, Y., Tamura, T., Mizoguchi, J., Hirota, Y., et al. 1980. In vitro peptidoglycan polymerization catalysed by penicillin-binding protein 1b of Escherichia coli K12. FEBS Lett. 110:245-49
• Tamaki, S., Nakajima, S., Matsuhashi, M. 1978. Thermosensitive mutation in Escherichia coli simultaneously causing defects in penicillin-binding protein-1Bs and in enzyme activity for peptidoglycan synthesis in vitro. Proc. Natl. Acad. Sci. USA 74:5472-76
• Taschner, P. E. M., Huls, P. G., Pas, E., Woldringh, C. L. 1988. Division behavior and shape changes in isogenic ftsZ, ftsQ, ftsA, pbpB and ftsE cell division mutants of Escherichia coli during temperature shift experiments. J. Bacteriol. 170:1533-40
• Taschner, P. E. M., Ypenburg, N., Spratt, B. G., Woldringh, C. L. 1988. An amino acid substitution in penicillin-binding protein 3 creates pointed polar caps in Escherichia coli. J. Bacteriol. 170:4828-37
• Tesch, W., Ryffel, C., Strässle, A., Kayser, F. H., Berger-Bächi, B. 1990. Evidence of a novel staphylococcal mecencoded element (mecR) controlling expression of penicillin-binding protein 2′. Antimicrob. Agents Chemother. 34: 1703-6
• Tipper, D. J., Strominger, J. L. 1965. Mechanism of action of penicillins: a proposal based on the structural similarity to acyl-D-alanyl-D-alanine. Proc. Natl. Acad. Sci. USA 54:1131-41
• Todd, J. A., Bone, E. J., Ellar, D. J. 1985. The sporulation-specific penicillin-binding protein 5a from Bacillus subtilis is a DD-carboxypeptidase in vitro. Biochem. J. 230:825-28
• Todd, J. A., Bone, E. J., Piggot, P. J., Ellar, D. J. 1983. Differential expression of penicillin-binding protein structural genes during Bacillus subtilis sporulation. FEMS Microbiol. Lett. 18:197-202
• Todd, J. A., Roberts, A. N., Johnston, K., Piggot, P. J., Winter, G., et al. 1986. Reduced heat resistance of mutant scores after cloning and mutagenesis of the Bacillus subtilis gene encoding penicillin-binding protein 5. J. Bacteriol. 167:257-64
• Tormo, A., Vicente, M. 1984. The ftsA gene product participates in formation of the Escherichia coli septum structure. J. Bacteriol. 157:779-84
• Tsukamoto, K., Kihura, R., Ohno, R., Sawai, T. 1990. Substitution of aspartic acid-217 of Citrobacter freundii cephalosporinase and properties of the mutant enzymes. FEBS Lett. 264:211-14
• Tsukamoto, K., Ohno, R., Saway, T. 1990. Extension of the substrate spectrum by an amino acid substitution at residue 219 in the Citrobacter freundii cephalosporinase. J. Bacteriol. 172: 4348-51
• Ubukata, K., Nonoguchi, R., Matsuhashi, M., Song, M. D., Konno, M. 1989. Restriction maps of the regions coding for methicillin and tobramycin resistances on chromosomal DNA in methicillin-resistant staphylococci. Antimicrob. Agents Chemother. 33:1624-26
• van Heijenoort, Y., Leduc, M., Singer, H., van Heijenoort, J. 1987. Effect of moemycin on Escherichia coli. J. Gen. Microbiol. 133:667-74
• Varetto, L., Bellefroid-Bourguignon, C., Frère, J.-M., Nguyen-Distèche, M., Ghuysen, J.-M., et al. 1987. The pH-dependence of the active-site serine DD-peptidase of Streptomyces R61. Eur. J. Biochem. 162:525-31
• Ward, J. E., Lutkenhaus, J. F. 1985. Overproduction of FtsZ induces mini-cells in Escherichia coli. Cell 42:941-49
• Waxman, D. J., Strominger, J. L. 1981. Primary structure of the COOH-terminal membranous segment of a penicillin-sensitive enzyme purified from two Bacilli. J. Biol. Chem. 256:2067-77
• Yi, Q. M., Lutkenhaus, J. F. 1985. The nucleotide sequence of the essential cell division gene ftsZ. Gene 36:241-47
• Zhu, Y. F., Curran, I. J., Joris, B., Ghuysen, J.-M., Lampen, J. O. 1990. Identification of BlaR, signal transducer for β-lactamase production in Bacillus licheniformis as a penicillin-binding protein with strong homology to the Oxa-2 β-lactamase (class D) of Salmonella typhimurium. J. Bacteriol. 172:1137-41