Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: Presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent

Microbiology and Molecular Biology Reviews

Volumn 66, Issue 4, 2002, Pages 702-738

  Goffin, Colette ^a   Ghuysen, Jean Marie ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

6 EPOXYPENICILLIN; ACYLTRANSFERASE; AZETIDINONE DERIVATIVE; BACTERIAL PROTEIN; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CELL PROTEIN; CEPHALOSPORIN DERIVATIVE; CEPHAMYCIN DERIVATIVE; CEPHEM DERIVATIVE; CLAVULANIC ACID; HYBRID PROTEIN; IMIPENEM; LATAMOXEF; MECILLINAM; PENAM DERIVATIVE; PENEM DERIVATIVE; PENICILLIN G; PEPTIDOGLYCAN; POLYPEPTIDE; PROTEIN PBP; PROTEIN PEN; PROTEIN PRECURSOR; PROTEIN SXXK; UNCLASSIFIED DRUG;

ANTIBIOTIC RESISTANCE; ANTIBIOTIC SENSITIVITY; CELL CYCLE; CORYNEBACTERIUM DIPHTHERIAE; DRUG EFFICACY; DRUG TARGETING; GENOME ANALYSIS; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; MYCOBACTERIUM; MYCOBACTERIUM LEPRAE; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PROTEIN ASSEMBLY; PROTEIN FAMILY; REVIEW; STREPTOMYCES COELICOLOR; STRUCTURE ACTIVITY RELATION;

ACYLTRANSFERASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CARRIER PROTEINS; HEXOSYLTRANSFERASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MURAMOYLPENTAPEPTIDE CARBOXYPEPTIDASE; MYCOBACTERIUM TUBERCULOSIS; PENICILLIN RESISTANCE; PENICILLIN-BINDING PROTEINS; PENICILLINS; PEPTIDOGLYCAN; PEPTIDYL TRANSFERASES;

BACTERIA (MICROORGANISMS); CORYNEBACTERIUM; CORYNEBACTERIUM DIPHTHERIAE; MYCOBACTERIUM; MYCOBACTERIUM LEPRAE; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NEGIBACTERIA; POSIBACTERIA; STREPTOMYCES; STREPTOMYCES COELICOLOR;

EID: 0036898699     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/MMBR.66.4.702-738.2002     Document Type: Review

References (259)

1. Adam, M., C. Fraipont, N. Rhazi, M. Nguyen-Distèche, B. Lakaye, J. M. Frère, B. Devreese, J. Van Beeumen, Y. van Heijenoort, J. van Heijenoort, and J. M. Ghuysen. 1997. The bimodular G57-V577 polypeptide chain of the class B penicillin-binding protein 3 of Escherichia coli catalyzes peptide bond formation from thiolesters and does not catalyze glycan chain polymerization from lipid II intermediate. J. Bacteriol. 179:6005-6009.
2. Addinall, S. G., and J. Lutkenhaus. 1996. FtsZ-spirals and -arcs determine the shape of the invaginating septa in some mutants of Escherichia coli. Mol. Microbiol. 22:231-237.
3. Altschul, S. F., and W. Gish. 1996. Local alignment statistics. Methods Enzymol. 266:460-480.
4. Altschul, S. F., T. L. Madden, A. A. Schaffer, J. Zhang, Z. Zhang, W. Miller, and D. J. Lipman. 1997. Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res. 25:3389-3402.
5. Ambler, R. P., A. F. W. Coulson, J. M. Frère, J. M. Ghuysen, B. Joris, M. Forsman, R. C. Levesque, G. Tiraby, and S. G. Waley. 1991. A standard numbering scheme for the class A β-lactamases. Biochem. J. 276:269-272.
6. Amoroso, A., D. Demares, M. Mollerach, G. Gutkind, and J. Coyette. 2001. All detectable high-molecular-mass penicillin-binding proteins are modified in a high-level β-lactam-resistant clinical isolate of Streptococcus mitis. Antimicrob. Agents Chemother. 45:2075-2081.
7. Andersson, J. O., and S. G. Andersson. 2001. Pseudogenes, junk DNA, and the dynamics of Rickettsia genomes. Mol. Biol. Evol. 18:829-839.
8. Arthur, M., F. Depardieu, L. Cabanié, P. Reynolds, and P. Courvalin. 1998. Requirement of the VanY and VanX DD-peptidases for glycopeptide resistance in enterococci. Mol. Microbiol. 30:819-830.
9. Arthur, M., F. Depardieu, H. A. Snaith, P.E. Reynolds, and P. Courvalin. 1994. Contribution of VanY DD-carboxypeptidase to glycopeptide resistance in Enterococcus faecalis by hydrolysis of peptidoglycan precursors. Antimicrob. Agents Chemother. 38:1899-1903.
10. Asano, Y., H. Ito, T. Dairi, and Y. Kato. 1996. An alkaline D-stereospecific endopeptidase with β-lactamase activity from Bacillus cereus. J. Biol. Chem. 22:30256-30262.
11. Asano, Y., Y. Kato, A. Yamada, and K. Kondo. 1992. Structural similarity of D-aminopeptidase to carboxypeptidases DD and β-lactamases. Biochemistry 31:2316-2328.
12. Azuma, I., D. W. Thomas, A. Adam, J. M. Ghuysen, R. Bonaly, J. F. Petit, and E. Lederer. 1970. Occurrence of N-glycolylmuramic acid in bacterial cell walls. A preliminary survey. Biochim. Biophys. Acta 208:444-451.
13. Baquero, M. R., M. Bouzon, J. C. Quintela, J. A. Ayala, and F. Moreno. 1996. dacD, an Escherichia coli gene encoding a novel penicillin-binding protein (PBP6b) with DD-carboxypeptidase activity. J. Bacteriol. 178:7106-7111.
14. Barbour, A. G. 1981. Properties of penicillin-binding proteins in Neisseria gonorrhoeae. Antimicrob. Agents Chemother. 19:316-322.
15. Basu, J., R. Chattopadhyay, M. Kundu, and P. Chakrabarti. 1992. Purification and partial characterization of a penicillin-binding protein from Mycobacterium smegmatis. J. Bacteriol. 174:4829-4832.
16. Basu, J., S. Mahapatra, M. Kundu, S. Mukhopadhyay, M. Nguyen-Distèche, P. Dubois, B. Joris, J. Van Beeumen, S. T. Cole, P. Chakrabarti, and J. M. Ghuysen. 1996. Identification and overexpression in Escherichia coli of a Mycobacterium leprae gene, pon1, encoding a high-molecular-mass class A penicillin-binding protein, PBP1. J. Bacteriol. 178:1707-1711.
17. Beck, B. D., and J. T. Park. 1977. Basis for the observed fluctuation of carboxypeptidase II activity during the cell cycle in BUG 6, a temperature-sensitive division mutant of Escherichia coli. J. Bacteriol. 130:1292-1302.
18. Begg, K. J., S. J. Dewar, and W. O. Donachie. 1995. A new Escherichia coli cell division gene risk. J. Bacteriol. 177:6211-6222.
19. Begg, K. J., A. Takasuga, D. H. Edwards, S. J. Dewar, B. G. Spratt, H. Adachi, T. Ohta, H. Matsuzawa, and W. D. Donachie. 1990. The balance between different peptidoglycan precursors determines whether Escherichia coli cells will elongate or divide. J. Bacteriol. 172:6697-6703.
20. Berthet, F. X., J. Rauzier, E. M. Lim, W. Philipp, B. Gicquel, and D. Portnoï. 1995. Characterization of the Mycobacterium tuberculosis erp gene encoding a potential cell surface protein with repetitive structures. Microbiology 141:2123-2130.
21. Bhakta, S., and J. Basu. 2002. Overexpression, purification and biochemical characterization of a class A high-molecular-mass penicillin-binding protein (PBP), PBP1* and its soluble derivative from Mycobacterium tuberculosis. Biochem. J. 361:635-639.
22. Billman-Jacobe, H., R. E. Haites, and R. L. Coppel. 1999. Characterization of a Mycobacterium smegmatis mutant lacking penicillin binding protein 1. Antimicrob. Agents Chemother. 43:3011-3013.
23. Blasco, B., A. G. Pisabarro, and M. A. de Pedro. 1988. Peptidoglycan biosynthesis in stationary-phase cells of Escherichia coli. J. Bacteriol. 170: 5224-5228.
24. rd, C. A. Bloch, N. T. Perna, V. Burland, M. Riley, J. Collado-Vides, J. D. Glasner, C. K. Rode, G. F. Mayhew, J. Gregor, N. W. Davis, H. A. Kirkpatrick, M. A. Goeden, D. J. Rose, B. Mau, and Y. Shao. 1997. The complete genome sequence of Escherichia coli K-12. Science 277:1453-1474.
25. Bloom, B. R. 1992. Back to a frightening future. Nature 358:538-539.
26. Bompard-Gilles, C., H. Remaut, V. Villeret, T. Prange, L. Fanuel, M. Delmarcelle, B. Joris, J. M. Frère, and J. Van Beeumen. 2000. Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the penicillin-recognizing enzyme family. Structure Fold. Des. 15: 971-980.
27. Botta, G. A., and J. T. Park. 1981. Evidence of involvement of penicillin-binding protein 3 in murein synthesis during septation, but not during cell elongation. J. Bacteriol. 145:333-340.
28. Boyle, D. S., M. M. Khattar, S. G. Addinall, J. Lutkenhaus, and W. D. Donachie. 1997. ftsW is an essential cell-division gene in Escherichia coli. Mol. Microbiol. 24:1263-1273.
29. Braun, V. 1975. Covalent lipoprotein from the outer membrane of Escherichia coli. Biochim. Biophys. Acta 415:335-377.
30. Brennan, P. J., and H. Nikaido. 1995. The envelope of mycobacteria. Annu. Rev. Biochem. 64:29-63.
31. Buddelmeijer, N., N. Judson, D. Boyd, J. J. Mekalanos, and J. Beckwith. 2002. YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae, localizes in codependent fashion with FtsL to the division site. Proc. Natl. Acad. Sci. USA 99:6316-6321.
32. Burger, A., K. Sichler, G. Kelemen, M. Buttner, and W. Wohlleben. 2000. Identification and characterization of the mre gene region of Streptomyces coelicolor A3(2). Mol. Gen. Genet. 263:1053-1060.
33. Cashel, M., D. R. Gentry, V. J. Hernandez, and D. Vinella. 1996. The stringent response, p. 1488-1496. In F. C. Neidhardt, R. Curtis, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd Ed., vol. 1. ASM Press, Washington, D.C.
34. Chalut, C., X. Charpentier, M. H. Remy, and J. M. Masson. 2001. Differential responses of Escherichia coli cells expressing cytoplasmic domain mutants of penicillin-binding protein lb after impairment of penicillin-binding proteins 1a and 3. J. Bacteriol. 183:200-206.
35. Chambers, H. F., D. Moreau, D. Yajko, C. Miick, C. Wagner, C. Hackbarth, S. Kocagöz, E. Rosenberg, W. K. Hadley, and H. Nikaido. 1995. Can penicillins and other β-lactam antibiotics be used to treat tuberculosis? Antimicrob. Agents Chemother. 39:2620-2624.
36. Chen, J. C., M. Minev, and J. Beckwith. 2002. Analysis of ftsQ mutant alleles in Escherichia coli: Complementation, septal localization, and recruitment of downstream cell division proteins. J. Bacteriol. 184:695-705.
37. Claverys, J. P., M. Prudhomme, I. Mortier-Barrière, and B. Martin. 2000. Adaptation to the environment: Streptococcus pneumoniae, a paradigm for recombination-mediated genetic plasticity? Mol. Microbiol. 35:251-259.
38. Cole, S. T., et al. 1998. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393:537-544.
39. Cole, S. T., et al. 2001. Massive gene decay in the leprosy bacillus. Nature 409:1007-1011.
40. Coyette, J., H. R. Perkins, I. Polacheck, G. D. Shockman, and J. M. Ghuysen. 1974. Membrane-bound DD-carboxypeptidase and LD-transpeptidase of Streptococcus faecalis ATCC 9790. Eur. J. Biochem. 44:459-468.
41. Curtis, N. A., D. Orr, G. W. Ross, and M. G. Boulton. 1979. Affinities of penicillins and cephalosporins for the penicillin-binding proteins of Escherichia coli K-12 and their antibacterial activity. Antimicrob. Agents Chemother. 16:533-539.
42. Daniel, R. A., S. Drake, C. E. Buchanan, R. Scholle, and J. Errington. 1994. The Bacillus subtilis spoVD gene encodes a mother-cell-specific penicillin-binding protein required for spore morphogenesis. J. Mol. Biol. 235:209-220.
43. Daniel, R. A., E. J. Harry, and J. Errington. 2000. Role of penicillin-binding protein PBP2B in assembly and functioning of the division machinery of Bacillus subtilis. Mol. Microbiol. 35:299-311.
44. DasGupta, H., and D. P. Fan. 1979. Purification and characterization of a carboxypeptidase-transpeptidase of Bacillus megaterium acting on the tetrapeptide moiety of the peptidoglycan. J. Biol. Chem. 254:5672-5683.
45. Davies, C., S. W. White, and R. A. Nicholas. 2001. Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-Å resolution. J. Biol. Chem. 276:616-623.
46. de Jonge, B. L. M., and A. Tomasz. 1993. Abnormal peptidoglycan produced in a methicillin-resistant strain of Staphylococcus aureus grown in the presence of methicillin: Functional role for penicillin-binding protein 2A in cell wall synthesis. Antimicrob. Agents Chemother. 37:342-346.
47. de la Rosa, E. J., M. A. de Pedro, and D. Vázquez. 1982. Modification of penicillin-binding proteins of Escherichia coli associated with changes in the state of growth of the cells. FEMS Microbiol. Lett. 14:91-94.
48. Denome, S. A., P. K. Elf, T. A. Henderson, D. E. Nelson, and K. D. Young. 1999. Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: Viability, characteristics, and implications for peptidoglycan synthesis. J. Bacteriol. 181:3981-3993.
49. de Pedro, M. A., W. D. Donachie, J. V. Höltje, and H. Schwarz. 2001. Constitutive septal murein synthesis in Escherichia coli with impaired activity of the morphogenetic proteins RodA and penicillin-binding protein 2. J. Bacteriol. 183:4115-4126.
50. Deretic, V., and R. A. Fratti. 1999. Mycobacterium tuberculosis phagosome. Mol. Microbiol. 31:1603-1609.
51. de Rosa, R., and B. Labedan. 1998. The evolutionary relationships between the two bacteria Escherichia coli and Haemophilus influenzae and their putative last common ancestor. Mol. Biol. Evol. 15:17-27.
52. ++-containing D-alanyl-D-alanine-cleaving carboxypeptidase. Nature 299:469-470.
53. Dive, G., D. Dehareng, and J. M. Ghuysen. 1994. A detailed study of a molecule into a molecule: The N-acetyl-L-tryptophanamide in active site model of the α-chymotrypsin. J. Am. Chem. Soc. 116:2548-2556.
54. Dive, G., D. Dehareng, and D. Peeters. 1996. Proposition for the acylation mechanism of serine proteases: A one-step process? Int. J. Quantum Chem. 58:85-107.
55. Donachie, W. D. 2001. Co-ordinate regulation of the Escherichia coli cell cycle; or, the cloud of unknowing. Mol. Microbiol. 40:779-785.
56. Dowson, C. G., T. J. Goffey, and B. G. Spratt. 1994. Origin and molecular epidemiology of penicillin binding protein-mediated resistance to β-lactam antibiotics. Trends Microbiol. 2:361-366.
57. Duez, C., C. Piron-Fraipont, B. Joris, J. Dusart, M. S. Urdea, J. A. Martial, J. M. Frère, and J. M. Ghuysen. 1987. Primary structure of the Streptomyces R61 exocellular DD-peptidase. 1. Cloning into Streptomyces lividans and nucleotide sequence of the gene. Eur. J. Biochem. 162:509-518.
58. Duez, C., W. Zorzi, F. Sapunaric, A. Amoroso, I. Thamm, and J. Coyette. 2001. The penicillin resistance of Enterococcus faecalis JH2-2r results from an overproduction of the low affinity penicillin-binding protein PBP4 and does not involve a psr-like gene. Microbiology 147:2561-2569.
59. Edwards, D. H., and W. D. Donachie. 1993. Construction of a triple deletion of penicillin-binding proteins 4, 5, and 6 in Escherichia coli, p. 369-374. In M. A. de Pedro, J. V. Höltje, and W. Löffelhardt (ed.), Bacterial Growth and Lysis. Plenum Press, New York, N.Y.
60. Ehlert, K., M. Tschierske, C. Mopi, W. Schröder, and B. Berger-Bächi. 2000. Site-specific serine incorporation by Lif and Epr into positions 3 and 5 of the staphylococcal peptidoglycan interpeptide bridge. J. Bacteriol. 182:2635-2638.
61. El Kharroubi, A., P. Jacques, G. Piras, J. Van Beeumen, J. Coyette, and J. M. Ghuysen. 1991. The Enterococcus hirae R40 penicillin-binding protein 5 and the methicillin-resistant Staphylococcus aureus penicillin-binding protein 2′ are similar. Biochem. J. 280:463-469.
62. Fanuel, L., B. Granier, J. M. Wilkin, C. Bellefroid-Bourguignon, B. Joris, J. Knowles, E. Komives, J. Van Beeumen, J. M. Ghuysen, and J. M. Frère. 1994. The precursor of the Streptomyces R61 DD-peptidase containing a C-terminal extension is inactive. FEBS Lett. 351:49-52.
63. Fattorini, L., G. Orefici, S. H. Jin, G. Scardaci, G. Amicosante, N. Franceschini, and I. Chopra. 1992. Resistance to β-lactams in Mycobacterium fortuitum. Antimicrob. Agents Chemother. 36:1068-1072.
64. Filipe, S. R., E. Severina, and A. Tomasz. 2000. Distribution of the mosaic structured murM genes among natural populations of Streptococcus pneumoniae. J. Bacteriol. 182:6798-6805.
65. Filipe, S. R., and A. Tomasz. 2000. Inhibition of the expression of penicillin resistance in Streptococcus pneumoniae by inactivation of cell wall muropeptide branching genes, Proc. Natl. Acad. Sci. USA 97:4891-4896.
66. Flärdh, K., E. Leibovitz, M. J. Buttner, and K. F. Chater. 2000. Generation of a nonsporulating strain of Streptomyces coelicolor A3(2) by the manipulation of a developmentally controlled ftsZ promoter. Mol. Microbiol. 38: 737-749.
67. Fontana, R., A. Grossato, L. Rossi, Y. R. Cheng, and G. Satta. 1985. Transition from resistance to hypersusceptibility to β-lactam antibiotics associated with loss of a low-affinity penicillin-binding protein in a Streptococcus faecium mutant highly resistant to penicillin. Antimicrob. Agents Chemother. 28:678-683.
68. Fonzé, E., M. Vermeire, M. Nguyen-Distèche, R. Brasseur, and P. Charlier. 1999. The crystal structure of a penicilloyl-serine transferase of intermediate penicillin-sensitivity. The DD-transpeptidase of Streptomyces K15. J. Biol. Chem. 274:21853-21860.
69. Frère, J. M., C. Duez, J. M. Ghuysen, and J. Vandekerkhove. 1976. Occurrence of a serine residue in the penicillin-binding site of the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61. FEBS Lett. 70:257-260.
70. Frère, J. M., J. M. Ghuysen, and H. R. Perkins. 1975. Interaction between the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61, substrate and β-lactam antibiotics. A choice of models. Eur. J. Biochem. 57:353-359.
71. Frère, J. M., J. M. Ghuysen, J. Degelaen, A. Loffet, and H. R. Perkins. 1975. Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidases-transpeptidases of Streptomyces R61 and R39. Nature 258:168-170.
72. Frère, J. M., J. M. Ghuysen, H. Vanderhaeghe, P. Adriaens, and J. Degelaen. 1976. Fate of thiazolidine ring during fragmentation of penicillin by the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61. Nature 260:451-454.
73. 2155 genome. Microbiology 147:3281-3294.
74. Galleni, M., G. Amicosante, and J. M. Frère. 1988. A survey of the kinetic parameters of class C β-lactamases. Cephalosporins and other β-lactam compounds. Biochem. J. 255:123-129.
75. Gatfield, J., and J. Pieters. 2000. Essential role for cholesterol in entry of mycobacteria into macrophages. Science 288:1647-1650.
76. Gérard, P., T. Vernet, and A. Zapun. 2002. Membrane topology of the Streptococcus pneumoniae FtsW division protein. J. Bacteriol. 184:1925-1931.
77. Ghuysen, J. M. 1968. Use of bacteriolytic enzymes in determination of wall structure and their role in cell metabolism. Bacteriol. Rev. 32:425-464.
78. Ghuysen, J. M. 1991. Serine β-lactamases and penicillin-binding proteins. Annu. Rev. Microbiol. 45:37-67.
79. Ghuysen, J. M. 1994. Molecular structures of penicillin-binding proteins and β-lactamases. Trends Microbiol. 2:372-380.
80. Ghuysen, J. M., and G. Dive. 1994. Biochemistry of the penicilloyl serine transferases. New Comprehensive Biochem. Bacterial Cell Wall 27:103-130.
81. Ghuysen, J. M., and C. Goffin. 1999. Lack of cell wall peptidoglycan versus penicillin sensitivity: New insights into the chlamydial anomaly. Antimicrob. Agents Chemother. 43:2339-2344.
82. Ghuysen, J. M., J. M. Frère, M. Leyh-Bouille, M. Nguyen-Distèche, and J. Coyette. 1986. Active-site-serine D-alanyl-D-alanine-cleaving-peptidase-catalyzed acyl-transfer reactions. Procedures for studying the penicillin-binding proteins of bacterial plasma membranes. Biochem. J. 235:159-165.
83. Ghuysen, J. M., J. Lamotte-Brasseur, B. Joris, and G. D. Shockman. 1994. Binding site-shaped repeated sequences of Streptomyces albus G D-peptidase, Bacillus subtilis Cwla amidase. Corynebacterium acetobutylicum lysozyme and Bacillus spp. ORF-L 3 gene product. FEBS Lett. 342:23-28.
84. Goffin, C., and J. M. Ghuysen. 1998. Multimodular penicillin-binding proteins: An enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. 62:1079-1093.
85. Gondrd, B., B. Flouret, and J. van Heijenoort. 1973. Release of D-alanyl-D-alanine from the precursor of the cell wall peptidoglycan by a peptidase of Escherichia coli K12. Biochimie 55:685-691.
86. Gordon, E., N. Mouz, E. Dude, and O. Dideberg. 2000. The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: Implication in drug resistance. J. Mol. Biol. 299:477-485.
87. Granier, B., C. Duez, S. Lepage, S. Englebert, J. Dusart, O. Dideberg, J. Van Beeumen, J. M. Frère, and J. M. Ghuysen. 1992. Primary and predicted secondary structures of the Actinomadura R39 extracellular DD-peptidase, a penicillin-binding protein (PBP) related to the Escherichia coli PBP4. Biochem. J. 282:781-788.
88. Gustafson, J., A. Strässle, H. Hächler, T. H. Kayser, and B. Berger-Bächi. 1994. The femC locus of Staphylococcus aureus required for methicillin resistance includes the glutamine synthetase operon. J. Bacteriol. 176:1460-1467.
89. Hakenbeek, R., and J. Coyette. 1998. Resistant penicillin-binding proteins. Cell. Mol. Life Sci. 54:332-340.
90. Hakenbeck, R., T. Grebe, D. Zähner, and J. B. Stock. 1999. β-lactam resistance in Streptococcus pneumoniae: Penicillin-binding proteins and non-penicillin-binding proteins. Mol. Microbiol. 33:673-678.
91. r penicillin-binding protein variants during transfer of high-level β-lactam resistance from Streptococcus mitis to Streptococcus pneumoniae. J. Bacteriol. 180:1831-1840.
92. Hamid, M. E., D. E. Minnikin, and M. Goodfellow. 1993. A simple chemical test to distinguish mycobacteria from other mycolic acid-containing actinomycetes. J. Gen. Microbiol. 139:2203-2213.
93. Hammes, W. P. 1978. The LD-carboxypeptidase activity in Gaffkya homari. The target of the action of D-amino acids or glycine on the formation of wall-bound peptidoglycan. Eur. J. Biochem. 91:501-507.
94. Hammes, W. P., and H. Seidel. 1978. The activities in vitro of DD-carboxypeptidase and LD-carboxypeptidase of Gaffkya homari during biosynthesis of peptidoglycan. Eur. J. Biochem. 84:141-147.
95. Hammes, W. P., and H. Seidel. 1978. The LD-carboxypeptidase activity in Gaffkya homari. The target of the action of certain β-lactam antibiotics on the formation of wall-bound peptidoglycan. Eur. J. Biochem. 91:509-515.
96. Hardt, K., B. Joris, S. Lepage, R. Brasseur, J. O. Lampen, J. M. Frère, A. L. Fink, and J. M. Ghuysen. 1997. The penicillin sensory-transducer BlaR involved in the inducibility of β-lactamase synthesis in Bacillus licheniformis is embedded in the plasma membrane via a four a-helix bundle. Mol. Microbiol. 23:935-944.
97. Harry, E. J. 2001. Bacterial cell division: Regulating Z-ring formation. Mol. Microbiol. 40:795-803.
98. Hartman, B. J., and A. Tomasz. 1984. Low-affinity penicillin-binding protein associated with β-lactam resistance in Staphylococcus aureus. J. Bacteriol. 158:513-516.
99. Henderson, T. A., K. D. Young, S. A. Denome, and P. K. Elf. 1997. AmpC and AmpH, proteins related to the class C β-lactamases, bind penicillin and contribute to the normal morphology of Escherichia coli. J. Bacteriol. 179: 6112-6121.
100. Henriques, A. O., P. Glaser, P. J. Piggot, and C. P. Moran Jr. 1998. Control of cell shape and elongation by the rodA gene in Bacillus subtilis. Mol. Microbiol. 28:235-247.
101. Herbert, D., C. N. Paramasivan, P. Venkatesan, G. Kubendiran, R. Prabhakar, and D. A. Mitchison. 1996. Bactericidal action of ofloxacin, sulbactam-ampicillin, rifampin, and isoniazid on logarithmic- and stationary-phase cultures of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 40:2296-2299.
102. 55 isoprenoid alcohol. Proc. Natl. Acad. Sci. USA 65:441-447.
103. Holland, P. W. 1999. The effect of gene duplication on homology. Novartis Found. Symp. 222:226-236.
104. Hopwood, D. A. 1999. Forty years of genetics with Streptomyces: From in vivo through in vitro to in silico. Microbiology 145:2183-2202.
105. Hoskins, J., et al. 2001. Genome of the bacterium Streptococcus pneumoniae strain R6. J. Bacteriol. 183:5709-5717.
106. Hu, Y., and A. R. M. Coates. 2001. Increased levels of sigJ mRNA in late stationary phase cultures of Mycobacterium tuberculosis detected by DNA array hybridisation. FEMS Microbiol. Lett. 202:59-65.
107. Hu, Y., J. A. Mangan, J. Dhillon, K. M. Sole, D. A. Mitchison, P. D. Butcher, and A. R. M. Coates. 2000. Detection of mRNA transcripts and active transcription in persistent Mycobacterium tuberculosis induced by exposure to rifampin or pyrazinamide. J. Bacteriol. 182:6358-6365.
108. Ikeda, M., T, Sato, M. Wachi, H. K. Jung, F, Ishino, Y. Kobayashi, and M. Matsuhashi. 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. 171:6375-6378.
109. Ilangovan, U., H, Ton-That, J. Iwahara, O. Schneewind, and R. T. Clubb. 2001. Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus. Proc. Natl. Acad. Sci. USA 98:6056-6061.
110. Ito, T., Y. Katayama, K. Asada, N. Mori, K. Tsutsumimoto, C. Tiensasitorn, and K. Hiramatsu. 2001. Structural comparison of three types of staphylococcal cassette chromosome mec integrated in the chromosome in methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 45:1323-1336.
111. Janezura, E., M. Leyh-Bouille, C. Cocito, and J. M. Ghuysen. 1981. Primary structure of the wall peptidoglycan of leprosy-derived corynebacteria. J. Bacteriol. 145:775-779.
112. Jarlier, V., and H. Nikaido. 1994. Mycobacterial cell wall: Structure and role in natural resistance to antibiotics. FEMS Microbiol. Lett. 123:11-18.
113. Jelseh, C., L. Mourey, J. M. Masson, and J. P. Samama. 1993. Crystal structure of E. coli TEM1 β-lactamase at 1.8 Å resolution. Proteins 16:364-383.
114. Jiang, H., and K. E. Kendrick. 2000. Cloning and characterization of the gene encoding penicillin-binding protein A of Streptomyces griseus. FEMS Microbiol. Lett. 193:63-68.
115. Joseleau-Petit, D., D. Thévenet, and R. D'Ari. 1994. ppGpp Concentration, growth without PBP2 activity, and growth-rate control in Escherichia coli. Mol. Microbiol. 13:911-917.
116. Kaneda, K., S. Imaizumi, S. Mizuno, T. Baba, M. Tsukamura, and I. Yano. 1988. Structure and molecular species composition of three homologous series of α-mycolic acids from Mycobacteria spp. J. Gen. Microbiol. 134: 2213-2229.
117. Kaneko, T., et al. 2000. Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti. DNA Res. 7:331-338.
118. Karlin, S., and S. F. Altschul. 1993. Applications and statistics for multiple high-scoring segments in molecular sequences. Proc. Natl. Acad. Sci. USA 90:5873-5877.
119. Kato, J.-I., H. Suzuki, and Y. Hirota. 1985. Dispensability of either penicillin-binding protein-1a or -1b involved in the essential process for cell elongation in Escherichia coli. Mol. Gen. Genet. 200:272-277.
120. Keck, W., A. M. van Leeuwen, M. Huber, and E. Wm. Goodell. 1990. Cloning and characterization of mepA, the structural gene of the penicillin-insensitive murein endopeptidase from Escherichia coli. Mol. Microbiol. 4:209-219.
121. Keer, J., M. J. Smeulders, K. M. Gray, and H. D. Williams. 2000. Mutants of Mycobacterium smegmatis impaired in stationary-phase survival. Microbiology 146:2209-2217.
122. Kelly, J. A., O. Dideberg, P. Charlier, J. P. Wéhry, M. Libert, P. C. Moews, J. R. Knox, C. Duez, C. Fraipont, B. Joris, J. Dusart, J. M. Frère, and J. M. Ghuysen. 1986. On the origin of bacterial resistance to penicillin. Comparison of a β-lactamase and a penicillin target. Science 231:1429-1437.
123. Kelly, J. A., and A. P. Kuzin. 1995. Refined crystallographic structure of a DD-peptidase penicillin target enzyme at 1.6 Å resolution. J. Mol. Biol. 254:223-236.
124. Kelly, J. A., A. P. Kuzin, P. Charlier, and E. Fonzé. 1998. X-ray studies of enzymes that interact with penicillin. Cell. Mol. Life Sci. 54:353-358.
125. Knott-Hunziker, V., K. Redhead, S. Petursson, and S. G. Waley. 1980. β-lactamase action: Isolation of an active-site serine peptide from the Pseudomonas enzyme and a penicillin. FEBS Lett. 121:8-10.
126. Knott-Hunziker, V., S. G. Waley, B. S. Orlek, and P. G. Sammes. 1979. Penicillinase active sites: Labelling of serine-44 in β-lactamase I by 6βbromopenicillanic acid. FEBS Lett. 99:59-61.
127. Kohlrausch, U., and J. V. Höltje. 1991. Analysis of murein and murein precursors during antibiotic-induced lysis of Escherichia coli. J. Bacteriol. 173:3425-3431.
128. Kopp, U., M. Roos, J. Wecke, and H. Labischinski. 1996. Staphylococcal peptidoglycan interpeptide bridge biosynthesis: A novel antistaphylococcal target? Microb. Drug Resist. 2:29-41.
129. Korat, B., H. Mottl, and W. Keck. 1991. Penicillin-binding protein 4 of Escherichia coli: Molecular cloning of the dacB gene, controlled overexpression, and alterations in murein composition. Mol. Microbiol. 5:675-684.
130. Kraulis, P. J. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-950.
131. Lamotte-Brasseur, J., G. Dive, and J. M. Ghuysen. 1984. On the structural analogy between D-alanyl-D-alanine terminated peptides and β-lactam antibiotics. Eur. J. Med. Chem. 19:319-330.
132. Lamotte, J., G. Dive, and J. M. Ghuysen. 1991. Conformational analysis of β and γ-lactam antibiotics. Eur. J. Med. Chem. 26:43-50.
133. Lazar, S. W., M, Almirón, A. Tormo, and R. Kolter. 1998. Role of the Escherichia coli SurA protein in stationary-phase survival. J. Bacteriol. 180:5704-5711.
134. Lázaro, S., F. Fernández-Piñas, E. Fernández-Valiente, A. Blanco-Rivero, and F. Leganés. 2001. pbpB, a gene coding for a putative penicillin-binding protein, is required for aerobic nitrogen fixation in the Cyanobacterium anabaena spp. strain PCC7120. J. Bacteriol. 183:628-636.
135. Lepage, S., P. Dubois, T. K. Ghosh, B. Joris, S. Mahapatra, M. Kundu, J. Basu, P. Chakrabarti, S. T. Cole, M. Nguyen-Distèche, and J. M. Ghuysen. 1997. Dual multimodular class A penicillin-binding proteins in Mycobacterium leprae. J. Bacteriol. 179:4627-4630.
136. Lessard, I. A. D., S. D. Pratt, D. G. McCafferty, D. E. Bussiere, C. Hutchins, B. L. Wanner, L. Katz, and C. T. Walsh. 1998. Homologs of the vancomycin resistance D-Ala-D-Ala dipeptidase VanX in Streptomyces toyocaensis, Escherichia coli and Synechocystis: Attributes of catalytic efficiency, stereoselectivity and regulation with implications for function. Chem. Biol. 5:489-504.
137. Lessard, I. A. D., and C. T. Walsh. 1999. Mutational analysis of active-site residues of the enterococcal D-Ala-D-Ala dipeptidase VanX and comparison with Escherichia coli D-Ala-D-Ala ligase and D-Ala-D-Ala carboxypeptidase Van Y. Chem. Biol. 6:177-187.
138. Lessard, I. A. D., and C. T. Walsh. 1999. VanX, a bacterial D-alanyl-D-alanine dipeptidase: Resistance, immunity, or survival function? Proc. Natl. Acad. Sci. USA 96:11028-11032.
139. Leyh-Bouille, M., R. Bonaly, J. M. Ghuysen, R. Tinelli, and D. Tipper. 1970. LL-Diaminopimelic acid containing peptidoglycans in walls of Streptomyces spp. and of Clostridium perfringens (type A). Biochemistry 9:2944-2952.
140. Leyh-Bouille, M., M. Nguyen-Distèche, S. Pirlot, A. Veithen, C. Bourguignon, and J. M. Ghuysen. 1986. Streptomyces K15 DD-peptidase-catalyzed reactions with suicide β-lactam carbonyl donors. Biochem. J. 235:177-182.
141. Liao, X., and R. E. W. Hancock. 1997. Identification of a penicillin-binding protein 3 homolog, PBP3x, in Pseudomonas aeruginosa: Gene cloning and growth phase-dependent expression. J. Bacteriol. 179:1490-1496.
142. Löwe, J., and L. A. Amos. 1998. Crystal structure of the bacterial cell-division protein FtsZ. Nature 391:203-206.
143. Lutkenhaus, J., and S. G. Addinall. 1997. Bacterial cell division and the Z ring. Annu. Rev. Biochem. 66:93-116.
144. Mahapatra, S., S. Bhakta, J. Ahamed, and J. Basu. 2000. Characterization of derivatives of the high-molecular-mass penicillin-binding protein (PBP) 1 of Mycobacterium leprae. Biochem. J. 350:75-80.
145. Mainardi, J. L., R. Legrand, M. Arthur, B. Schoot, J. van Heijenoort, and L. Gutmann. 2000. Novel mechanism of β-lactam resistance due to by-pass of DD-transpeptidation in Enterococcus faecium. J. Biol. Chem. 275:16490-16496.
146. Margolin, W. 2000. Themes and variations in prokaryotic cell division. FEMS Microbiol. Rev. 24:531-548.
147. Markiewicz, Z., J. K. Broome-Smith, U. Schwarz, and B. G. Spratt. 1982. Spherical Escherichia coli due to elevate levels of D-alanine carboxypeptidase. Nature 297:702-704.
148. Marrec-Fairley, M., A. Piette, X. Gallet, R. Brasseur, H. Hara, C. Fraipont, J. M. Ghuysen, and M. Nguyen-Distèche. 2000. Differential functions of amphiphilic peptide segments of the cell septation penicillin-binding protein 3 of Escherichia coli. Mol. Microbiol. 37:1019-1031.
149. May, B. J., Q. Zhang, L. L. Li, M. L. Paustian, T. S. Whittam, and V. Kapur. 2001. Complete genomic sequence of Pasteurella multocida, Pm70. Proc. Natl. Acad. Sci. USA 98:3460-3465.
150. Mazmanian, S. K., H. Ton-That, and O. Schneewind. 2001. Sortase-catalyzed anchoring of surface proteins to the cell call of Staphylococcus aureus. Mol. Microbiol. 40:1049-1057.
151. McCafferty, D. G., I. A. D. Lessard, and C. T. Walsh. 1997. Mutational analysis of potential zinc-binding residues in the active site of the enterococcal D-Ala-D-Ala dipeptidase VanX. Biochemistry 36:10498-10505.
152. McCormick, J. R., E. P. Su, A. Driks, and R. Losick. 1994. Growth and viability of Streptomyces coelicolor mutant for the cell division gene ftsZ. Mol. Microbiol. 14:243-254.
153. McKinney, J. D., K. Höner zu Bentrup, E. J. Muñoz-Elias, A. Miczak, B. Chen, W. T. Chan, D. Swenson, J. C. Sacchettini, W. R. Jacobs, Jr., and D. G. Russell. 2000. Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase. Nature 406:735-738.
154. Mercer, K. L. N., and D. S. Weiss. 2002. The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site. J. Bacteriol. 184:904-912.
155. Merritt, E. A., and D. J. Bacon. 1997. Raster3D: Photorealistic molecular graphics. Methods Enzymol. 277:505-524.
156. Metz, R., S. Henning, and W. P. Hammes. 1986. LD-carboxypeptidase activity in Escherichia coil. II. Isolation, purification and characterization of the enzyme from E. coli K12. Arch. Microbiol. 144:181-186.
157. Mollerach, M., P. Partoune, J. Coyette, and J. M. Ghuysen. 1996. Importance of the E46-D160 polypeptide segment of the non-penicillin-binding module for the stability of the low-affinity, multimodular class B penicillin-binding protein 5 of Enterococcus hirae. J. Bacteriol. 178:1774-1775.
158. Moreau, P. L., F. Gérard, N. W. Lutz, and P. Cozzone. 2001. Non-growing Escherichia coli cells starved for glucose or phosphate use different mechanisms to survive oxidative stress. Mol. Microbiol. 39:1048-1060.
159. Mukherjee, T., D. Basu, S. Mahapatra, C. Goffin, J. Van Beeumen, and J. Basu. 1996. Biochemical characterization of the 49 kDa penicillin-binding protein of Mycobacterium smegmatis. Biochem. J. 320:197-200.
160. Murray, T., D. L. Popham, and P. Setlow. 1996. Identification and characterization of pbpC, the gene encoding Bacillus subtilis penicillin-binding protein 3. J. Bacteriol. 178:6001-6005.
161. Nagasawa, H., Y. Sakagami, A. Suzuki, H. Suzuki, H. Hara, and Y. Hirota. 1989. Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli. J. Bacteriol. 171:5890-5893.
162. Nakagawa, J., S. Tamaki, S. Tomioka, and M. Matsuhashi. 1984. Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides. Penicillin-binding protein IBs of Escherichia coli with activities of transglycosylase and transpeptidase. J. Biol. Chem. 259:13937-13946.
163. Nanninga, N. 2001. Cytokinesis in prokaryotes and eukaryotes: Common principles and different solutions. Microbiol. Mol. Biol. Rev. 65:319-333.
164. Nelson, D. E., and K. D. Young. 2001. Contributions of PBP5 and DD-carboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coli. J. Bacteriol. 183:3055-3064.
165. Nguyen-Distèche, M., M. Leyh-Bouille, S. Pirlot, J. M. Frère, and J. M. Ghuysen. 1986. Streptomyces K15 DD-peptidase-catalyzed reactions with ester and amide carbonyl donors. Biochem. J. 235:167-176.
166. Nierman, W. C., et al. 2001. Complete genome sequence of Caulobacter crescentus. Proc. Natl. Acad. Sci. USA 98: 4136-4141.
167. Nyström, T. 1999. Starvation, cessation of growth and bacterial aging. Curr. Opin. Microbiol. 2:214-219.
168. Oefner, C., A. D'Arcy, J. J. Daly, K. Gubernator, R. L. Charnas, I. Heinze, C. Hubschwerlen, and F. K. Winkler. 1990. Refined crystal structure of β-lactamase of Citrobacter freundii indicates a mechanism for β-lactam hydrolysis. Nature (London) 343:284-288.
169. Orengo, C. A., D. T. Jones, and J. M. Thornton. 1994. Protein superfamilies and domain superfolds. Nature (London) 372:631-634.
170. Paetzel, M., F. Danel, L. de Castro, S. C. Mosimann, M. G. P. Page, and N. C. J. Strynadka. 2000. Crystal structure of the class D β-lactamase Oxa-10. Nat. Struct. Biol. 7:918-925.
171. r penicillin-binding proteins of class A. Biochem. J. 279:223-230.
172. Paradkar, A. S., K. A. Aidoo, A. Wong, and S. E. Jensen. 1996. Molecular analysis of a β-lactam resistance gene encoded within the cephamycin gene cluster of Streptomyces clavuligerus. J. Bacteriol. 178:6266-6274.
173. Paris, S., N. Mouz, Y. Pétillot, R. Hakenbeck, and O. Dideberg. 1996. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nat. Struct. Biol. 3:284-289.
174. Park, W., and M. Matsuhashi. 1984. Staphylococcus aureus and Micrococcus luteus peptidoglycan transglycosylases that are not penicillin-binding proteins. J. Bacteriol. 157:538-544.
175. Pedersen, L. B., E. R. Angert, and P. Setlow. 1999. Septal localization of penicillin-binding protein 1 in Bacillus subtilis. J. Bacteriol. 181:3201-3211.
176. Pinho, M. G., S. R. Filipe, H. De Lancastre, and A. Tomasz. 2001. Complementation of the essential peptidoglycan transpeptidase function of penicillin-binding protein 2 (PBP2) by the drug resistance protein PBP2A in Staphylococcus aureus. J. Bacteriol. 183:6525-6531.
177. r-encoding gene of Enterococcus hirae S185: Modular design and structural organization of the protein. J. Bacteriol. 175:2844-2852.
178. Pisabarro, A. G., M. A. de Pedro, and D. Vazquez. 1985. Structural modifications in the peptidoglycan of Escherichia coli associated with changes in the state of growth of the culture. J. Bacteriol. 161:238-242.
179. Pisabarro, A. G., R. Prats, D. Vazquez, and A. Rodriguez-Tébar. 1986. Activity of penicillin-binding protein 3 from Escherichia coli. J. Bacteriol. 168:199-206.
180. Prabhakaran, K., E. B. Harris, and B. Randhawa. 1999. Bactericidal action of ampicillin/sulbactam against intracellular mycobacteria. Int. J. Antimicrob. Agents 13:133-135.
181. Prabhakaran, K., E. B. Harris, R. M. Sanchez, and R. C. Hastings. 1987. β-lactamase synthesis in Mycobacterium leprae. Microbios 49:183-188.
182. Primm, T. P., S. J. Andersen, V. Mizrahi, D. Avarbock, H. Rubin, and C. E. Barry III. 2000. The stringent response of Mycobacterium tuberculosis is required for long-term survival. J. Bacteriol. 182:4889-4898.
183. Quintela, J. C., M. Caparrós, and M. A. de Pedro. 1995. Variability of peptidoglycan structural parameters in Gram-negative bacteria. FEMS Microbiol. Lett. 125:95-100.
184. Quintela, J. C., M. A. de Pedro, P. Zollner, G. Allmaier, and F. Garcia-del Portillo. 1997. Peptidoglycan structure of Salmonella typhimurium growing within cultured mammalian cells. Mol. Microbiol. 23:693-704.
185. Quinting, B., J. M. Reyrat, D. Monnaie, G. Amicosante, V. Pelicic, B. Gicquel, J. M. Frère, and M. Galleni. 1997. Contribution of β-lactamase production to the resistance of mycobacteria to β-lactam antibiotics. FEBS Lett. 406:275-278.
186. Ramakrishnan, L., N. A. Federspiel, and S. Falkow. 2000. Granuloma-specific expression of Mycobacterium virulence proteins from the glycinerich PE-PGRS family. Science 288:1436-1439.
187. Rambukkana, A. 2001. Molecular basis for the peripheral nerve predilection of Mycobacterium leprae. Curr. Opin. Microbiol. 4:21-27.
188. Rambukkana, I. 2000. How does Mycobacterium leprae target the peripheral nervous system? Trends Microbiol. 8:23-28.
189. Randhawa, B., E. B. Harrris, and K. Prabhakaran. 1999. Bactericidal action of oral ampicillin/sulbactam against Mycobacterium leprae. J. Antimicrob. Chemother. 44:279-281.
190. Rawlings, N. D., and A. J. Barrett. 2000. MEROPS: The peptidase database. Nucleic Acids Res. 28:323-325.
191. Reddy, P. S., A. Raghavan, and D. Chatterjee. 1995. Evidence of a ppGpp-binding site in Escherichia coli RNA polymerase: Proximity relationship with the rifampicin-binding domain. Mol. Microbiol. 15:255-265.
192. Redenbach, M., H. M. Kieser, D. Denapaite, A. Eichner, J. Cullum, H. Kinashi, and D. A. Hopwood. 1996. A set of ordered cosmids and a detailed genetic and physical map for the 8 Mb Streptomyces coelicolor A3(2) chromosome. Mol. Microbiol. 21:77-96.
193. Reeck, G. R., C. de Haën, D. C. Teller, R. F. Doolittle, W. M. Fitch, R. E. Dickerson, P. Chambon, A. D. McLachlan, E. Margoliash, T. H. Jukes, and E. Zuckerland. 1987. «Homology» in proteins and nucleic acids: A terminology muddle and a way out of it. Cell 50:667.
194. Rhazi, N. 2000. Etude du Mécanisme Catalytique des DD-Peptidases Bactériennes. Ph.D. thesis. University of Liège, Liège, Belgium.
195. Rhazi, N., M. Galleni, M. I. Page, and J. M. Frère. 1999. Peptidase activity of β-lactamases. Biochem. J. 341:409-413.
196. Rice, L. B., L. L. Carias, R. Hutton-Thomas, F. Sifaoui, L. Gutmann, and S. D. Rudin. 2001. Penicillin-binding protein 5 and expression of ampicillin resistance in Enterococcus faecium. Antimicrob. Agents Chemother. 45: 1480-1486.
197. Rohrer, S., K. Ehlert, M. Tschierske, H. Labischinski, and B. Berger-Bächi. 1999. The essential Staphylococcus aureus gene fmhB is involved in the first step of peptidoglycan pentaglycine interpeptide formation. Proc. Natl. Acad. Sci. USA 96:9351-9356.
198. Romeis, T., and J. V. Höltje. 1994. Penicillin-binding protein 7/8 of Escherichia coli is a DD-endopeptidase. Eur. J. Biochem. 224:597-604.
199. Ropp, P. A., and R. A. Nicholas. 1997. Cloning and characterization of the ponA gene encoding penicillin-binding protein 1 from Neisseria gonorrhoeae and Neisseria meningitidis. J. Bacteriol. 179:2783-2787.
200. Salton, M. R. J. 1994. The bacterial cell envelope - A historical perspective. New Comprehensive Biochem. Bacterial Cell Wall 27:1-22.
201. Schaible, U. E., K. Hagens, K. Fischer, H. L. Collins, and S. H. E. Kaufmann. 2000. Intersection of group I CD1 molecules and mycobacteria in different intracellular compartments of dendritic cells. J. Immunol. 164: 4843-4852.
202. Schiffer, G., and J. V. Höltje. 2039. 1999. Cloning and characterization of PBP1C, a third member of the multimodular class A penicillin-binding proteins of Escherichia coli. J. Biol. Chem. 274:32031-32033.
203. Schleifer, K. H., and O. Kandler. 1972. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev. 36:407-477.
204. 125I-derivative of ampicillin. FEMS Microbiol. Lett. 10:107-109.
205. Sifaoui, F., M. Arthur, L. Rice, and L. Gutmann. 2001. Role of penicillin-binding protein 5 in expression of ampicillin resistance and peptidoglycan structure in Enterococcus faecium. Antimicrob. Agents Chemother. 45: 2594-2597.
206. Signoretto, C., M. Boaretti, and P. Canepari. 1994. Cloning, sequencing and expression in Escherichia coli of the low-affinity penicillin-binding protein of Enterococcus faecalis. FEMS Microbiol. Lett. 123:99-106.
207. Signoretto, C., M. Boaretti, and P. Canepari. 1998. Peptidoglycan synthesis by Enterococcus faecalis penicillin binding protein 5. Arch. Microbiol. 170: 185-190.
208. Simpson, A. J. et al. 2000. The genome sequence of the plant pathogen Xylella fastidiosa. The Xylella fastidiosa consortium of the organization for nucleotide sequencing and analysis. Nature 406:151-157.
209. Smeulders, M. J., J. Keer, R. A. Speight, and H. D. Williams. 1999. Adaptation of Mycobacterium smegmatis to stationary phase. J. Bacteriol. 181: 270-283.
210. Song, M. D., M. Wachi, M. Doi, F. Ishino, and M. Matsuhashi. 1987. Evolution of an inducible penicillin-target protein in methicillin-resistant Staphylococcus aureus by gene fusion. FEBS Lett. 221:167-171.
211. Spratt, B. G. 1975. Distinct penicillin-binding proteins involved in the division, elongation, and shape of Escherichia coli K-12. Proc. Natl. Acad. Sci. USA 72:2999-3003.
212. Spratt, B. G. 1988. Hybrid penicillin-binding proteins in penicillin-resistant strains of Neisseria gonorrhoeae. Nature 332:173-176.
213. Spratt, B. G., V. Jobanputra, and W. Zimmermann. 1977. Binding of thienamycin and clavulanic acid to the penicillin-binding proteins of Escherichia coli K-12. Antimicrob. Agents Chemother. 12:406-409.
214. Spratt, B. G., and A. B. Pardee. 1975. Penicillin-binding proteins and cell shape in Escherichia coli. Nature 254:516-517.
215. Spratt, B. G., J, Zhou, M. Taylor, and M. J. Merrick. 1996. Monofunctional biosynthetic peptidoglycan transglycosylases. Mol. Microbiol. 19:639-640.
216. Storey, C., and I. Chopra. 2001. Affinities of β-lactams for penicillin binding proteins of Chlamydia trachomatis and their antichlamydial activities. Antimicrob. Agents Chemother. 45:303-305.
217. Strynadka, N. C. J., H. Adachi, S. E. Jensen, K. Johns, A, Sielecki, C. Betzel, K. Sutoh, and M. N. James. 1992. Molecular structure of the acylenzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution. Nature 359:700-705.
218. Sturgill-Koszycki, S., P. H. Schlesinger, P. Chakraborty, P. L. Haddix, H. L. Collins, A. K. Fok, R. D. Allen, S. L. Gluck, J. Heuser, and D. G. Russel. 1994. Lack of acidification in Mycobacterium phagosomes produced by exclusion of the vesicular proton-ATPase. Science 263:678-681.
219. Suzuki, H., J. Kato, Y. Sakagami, M. Mori, A. Suzuki, and Y. Hirota. 1987. Conversion of the α component of penicillin-binding protein 1b to the β component in Escherichia coli. J. Bacteriol. 169:891-893.
220. Suzuki, H., Y. Nishimura, and Y. Hirota. 1978. On the process of cellular division in Escherichia coli: A series of mutants of E. coli altered in the penicillin-binding proteins. Proc. Natl. Acad. Sci. USA 75:664-668.
221. Templin, M. F., A. Ursinus, and J. V. Höltje. 1999. A defect in cell wall recycling triggers autolysis during the stationary growth phase of Escherichia coli. EMBO J. 18:4108-4117.
222. Terrak, M., T. K. Gosh, J. van Heijenoort, J. Van Beeumen, M. Lampilas, J. Aszodi, J. A. Ayala, J. M. Ghuysen, and M. Nguyen-Distèche. 1999. The catalytic, glycosyltransferase and acyltransferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli. Mol. Microbiol. 34:350-364.
223. Tettelin, H., et al. 2000. Complete genome sequence of Neisseria meningitidis serogroup B strain MC58. Science 287:1809-1815.
224. Tipper, D. J., and J. L. Strominger. 1965. Mechanism of action of penicillins: A proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc. Natl. Acad. Sci. USA 54:1133-1141.
225. Tormo, A., M. Almirón, and R. Kolter. 1990. surA, an Escherichia coli gene essential for survival in stationary phase. J. Bacteriol. 172:4339-4347.
226. Tsuruoka, T., A. Tamura, A. Miyata, T. Takei, S. Inouye, and M. Matsuhashi. 1985. Second lytic target of β-lactam compounds that have a terminal D-amino acid residue. Eur. J. Biochem. 151:209-216.
227. Tuomanen, E., and R. Cozens. 1987. Changes in peptidoglycan composition and penicillin-binding proteins in slowly growing Escherichia coli. J. Bacteriol. 169:5308-5310.
228. Ursinus, A., H. Steinhaus, and J. V. Höltje. 1992. Purification of a nocardicin A-sensitive LD-carboxypeptidase from Escherichia coli by affinity chromatography. J. Bacteriol. 174:441-446.
229. van den Ent, F., L. A. Amos, and J. Löwe. 2001. Prokaryotic origin of the actin cytoskeleton. Nature 413:39-41.
230. Van der Linden, M. P. G., L. Hoan, M. A. Hoyer, and W. Keck. 1992. Possible role of Escherichia coli penicillin-binding protein 6 in stabilization of stationary-phase peptidoglycan. J. Bacteriol. 174:7572-7578.
231. van Heijenoort, J. 1996. Murein synthesis, p. 1025-1034. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. ASM Press, Washington, D.C.
232. van Heijenoort, J. 2001. Formation of the glycan chains in the synthesis of bacterial peptidoglycan. Glycobiology 11:25R-36R.
233. van Heljenoort, Y., M. Gómez, M. Derrien, J. Ayala, and J. van Heijenoort. 1992. Membrane intermediates in the peptidoglycan metabolism of Escherichia coli: Possible roles of PBPlb and PBP3. J. Bacteriol. 174:3549-3557.
234. van Heijenoort, J., and L. Gutmann. 2000. Correlation between the structure of the bacterial peptidoglycan monomer unit, the specificity of transpeptidation, and susceptibility to β-lactams. Proc. Natl. Acad. Sci. USA 97:5028-5030.
235. van Heijenoort, Y., and J. van Heijenoort. 1980. Biosynthesis of the peptidoglycan of Escherichia coli K-12: Properties of the in vitro polymerization by transglycosylation. FEBS Lett. 110:241-244.
236. via, L. E., D. Deretic, R. J. Ulmer, N. S. Hibler, L. A. Huber, and V. Deretic. 1997. Arrest of mycobacterial phagosome maturation is caused by a block in vesicle fusion between stages controlled by rab5 and rab7. J. Biol. Chem. 272:13326-13331.
237. Vicente, M., and J. Errington. 1996. Structure, function and controls in microbial division. Mol. Microbiol. 20:1-7.
238. Vinella, D., R. D'Ari, and P. Bouloc. 1992. Penicillin binding protein 2 is dispensible in Escherichia coli when ppGpp synthesis is induced. EMBO J. 11:1493-1501.
239. Vocadlo, D. J., G. J. Davies, R. Laine, and S. G. Withers. 2001. Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature 412: 835-838.
240. Voladri, R. K., D. L. Lakey, S. H. Hennigan, B. E. Menzies, K. M. Edwards, and D. S. Kernodle. 1998. Recombinant expression and characterization of the major β-lactamase of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 42:1375-1381.
241. Wachi, M., M. Doi, Y. Okada, and M. Matsuhashi. 1989. New mre genes mreC and mreD, responsible for formation of the rod shape of Escherichia coli cells. J. Bacteriol. 171:6511-6516.
242. Weber, B., K. Ehlert, A, Diehl, P. Reichmann, H. Labischinski, and R. Hakenbeck. 2000. The fib locus in Streptococcuspneumoniae is required for peptidoglycan crosslinking and PBP-mediated β-lactam resistance. FEMS Microbiol. Lett. 188:81-85.
243. Weiss, D. S., J. C. Chen, J. M. Ghigo, D. Boyd, and J. Beckwith. 1999. Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL. J. Bacteriol. 181:508-520.
244. Wietzerbin, J., B. C, Das, J. F. Petit, E. Lederer, M. Leyh-Bouille, and J. M. Ghuysen. 1974. Occurrence of D-alanyl-(D)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in the peptidoglycan of Mycobacteria. Biochemistry 13:3471-3476.
245. Wright, G. D., C. Molinas, M. Arthur, P. Courvalin, and C. T. Walsh. 1992. Characterization of VanY, a DD-carboxypeptidase from vancomycin-resistant Enterococcus faecium BM4147. Antimicrob. Agents Chemother. 36: 1514-1518.
246. Wu, C. Y. E., W. E. Alborn, Jr., J. E. Flokowitsch, J. Hoskins, S. Ünal, L. C. Blaszczak, D. A. Preston, and P. L. Skatrud. 1994. Site-directed mutagenesis of the meca gene from a methicillin-resistant strain of Staphylococcus aureus. J. Bacteriol. 176:443-449.
247. Wu, S. W., H. de Lencastre, and A. Tomasz. 2001. Recruitment of the mecA gene homologue of Staphylococcus sciuri into a resistance determinant and expression of the resistant phenotype in Staphylococcus aureus. J. Bacteriol. 183:2417-2424.
248. Wu, S., C. Piscitelli, H. de Lencastre, and A. Tomasz. 1996. Tracking the evolutionary origin of the methicillin resistance gene: Cloning and sequencing of a homologue of meca from a methicillin susceptible strain of Staphylococcus sciuri. Drug Resist. 2:435-441.
249. Yanouri, A., R. A. Daniel, J. Errington, and C. E. Buchanan. 1993. Cloning and sequencing of the cell division gene pbpB, which encodes penicillin-binding protein 2B in Bacillus subtilis. J. Bacteriol. 175:7604-7616.
250. Young, D. B., and K. Duncan. 1995. Prospects for new interventions in the treatment and prevention of mycobacterial disease. Annu. Rev. Microbiol. 49:641-673.
251. Young, K. D. 2001. Approaching the physiological functions of penicillin-binding proteins in Escherichia coli. Biochimie 83:99-102.
252. Yousif, S. Y., J. K. Broome-Smith, and B. G. Spratt. 1985. Lysis of Escherichia coli by β-lactam antibiotics: Deletion analysis of the role of penicillin-binding proteins 1A and 1B. J. Gen. Microbiol. 131:2839-2845.
253. Zambrano, M. M., D. A. Siegele, M. Almirón, A. Tormo, and R. Kolter. 1993. Microbial competition: Escherichia coli mutants that take over stationary-phase cultures. Science 259:1757-1759.
254. Zhang, H. Z., C. J. Hackbarth, K. M. Chansky, and H. F. Chambers. 2001. A proteolytic transmembrane signaling pathway and resistance to β-lactams in staphylococci. Science 291:1962-1965.
255. Zhang, Q. Y., and B. G. Spratt. 1989. Nucleotide sequence of the penicillin-binding protein 2 gene of Neisseria meningitidis. Nucleic Acids Res. 17:5383.
256. Zhu, J., K. Jäger, T. Black, K. Zarka, O. Koksharova, and C. P. Wolk. 2001. HcwA, an autolysin, is required for heterocyst maturation in Anabaena spp. strain PCC7120. J. Bacteriol. 183:6841-6851.
257. Zighelboim, S., and A. Tomasz. 1980. Penicillin-binding proteins of multiply antibiotic-resistant South African strains of Streptococcus pneumoniae. Antimicrob. Agents Chemother. 17:434-442.
258. Zimmer, D. P., E. Soupene, H. L. Lee, V. F. Wendisch, A. B. Khodursky, B. J. Peter, R. A. Bender, and S. Kustu. 2000. Nitrogen regulatory protein C-controlled genes of Escherichia coli: Scavenging as a defense against nitrogen limitation. Proc. Natl. Acad. Sci. USA 97:14674-14679.
259. Zorzi, W., X. Y. Zhou, O. Dardenne, J. Lamotte, D. Raze, J. Pierre, L. Gutmann, and J. Coyette. 1996. Structure of the low-allinity penicillin-binding protein 5 PBP5fm in wild-type and highly penicillin-resistant strains of Enterococcus faecium. J. Bacteriol. 178:4948-4957.