Cell wall branches, penicillin resistance and the secrets of the MurM protein

Trends in Microbiology

Volumn 11, Issue 12, 2003, Pages 547-553

  Fiser, András ^a   Filipe, Sergio R ^b   Tomasz, Alexander ^c  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; BACTERIAL PROTEIN; PENICILLIN BINDING PROTEIN; PENICILLIN G; PEPTIDE; PROTEIN MURM; PROTEIN MURN; TRANSFERASE; UNCLASSIFIED DRUG;

ALLELE; ANTIBACTERIAL ACTIVITY; BACTERIAL CELL WALL; BACTERIAL GENETICS; CELL PROTECTION; MOLECULAR MODEL; NONHUMAN; PENICILLIN RESISTANCE; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; REVIEW; STREPTOCOCCUS PNEUMONIAE;

BACTERIA (MICROORGANISMS); STREPTOCOCCUS; STREPTOCOCCUS PNEUMONIAE;

EID: 0344628644     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tim.2003.10.003     Document Type: Article

References (31)

1. Schleifer K.H., Kandler O. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev. 36:1972;407-477.
2. Garcia-Bustos J., Tomasz A. A biological price of antibiotic resistance: major changes in the peptidoglycan structure of penicillin-resistant pneumococci. Proc. Natl. Acad. Sci. U. S. A. 87:1990;5415-5419.
3. Rohrer S., Berger-Bachi B. FemABX peptidyl transferases: a link between branched-chain cell wall peptide formation and beta-lactam resistance in gram-positive cocci. Antimicrob. Agents Chemother. 47:2003;837-846.
4. Filipe S.R., et al. Characterization of the murMN operon involved in the synthesis of branched peptidoglycan peptides in Streptococcus pneumoniae. J. Biol. Chem. 275:2000;27768-27774.
5. Filipe S.R., Tomasz A. Inhibition of the expression of penicillin resistance in Streptococcus pneumoniae by inactivation of cell wall muropeptide branching genes. Proc. Natl. Acad. Sci. U. S. A. 97:2000;4891-4896.
6. Filipe S.R., et al. The murMN operon: a functional link between antibiotic resistance and antibiotic tolerance in Streptococcus pneumoniae. Proc. Natl. Acad. Sci. U. S. A. 99:2002;1550-1555.
7. Jedrzejas M.J. Pneumococcal virulence factors: structure and function. Microbiol. Mol. Biol. Rev. 65:2001;187-207.
8. Klein D.L. Pneumococcal disease and the role of conjugate vaccines. Microb. Drug Resist. 5:1999;147-157.
9. Bouhss A., et al. Synthesis of the L-alanyl-L-alanine Cross-bridge of Enterococcus faecalis Peptidoglycan. J. Biol. Chem. 277:2002;45935-45941.
10. Matsuhashi M., et al. Incorporation of glycine into the cell wall glycopeptide in Staphylococcus aureus: role of sRNA and lipid intermediates. Proc. Natl. Acad. Sci. U. S. A. 54:1965;587-594.
11. Plapp R., Strominger J.L. Biosynthesis of the peptidoglycan of bacterial cell walls. XVII. Biosynthesis of peptidoglycan and of interpeptide bridges in Lactobacillus viridescens. J. Biol. Chem. 245:1970;3667-3674.
12. Filipe S.R., et al. Functional analysis of Streptococcus pneumoniae MurM reveals the region responsible for its specificity in the synthesis of branched cell wall peptides. J. Biol. Chem. 276:2001;39618-39628.
13. Filipe S.R., et al. Distribution of the mosaic structured murM genes among natural populations of Streptococcus pneumoniae. J. Bacteriol. 182:2000;6798-6805.
14. Benson T.E., et al. X-ray crystal structure of Staphylococcus aureus FemA. Structure (Camb). 10:2002;1107-1115.
15. Holm L., Sander C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20:1995;478-480.
16. Shindyalov I.N., Bourne P.E. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11:1998;739-747.
17. Berman H.M., et al. The protein data bank. Nucleic Acids Res. 28:2000;235-242.
18. Hegde S.S., Shrader T.E. FemABX family members are novel nonribosomal peptidyltransferases and important pathogen-specific drug targets. J. Biol. Chem. 276:2001;6998-7003.
19. Farazi T.A., et al. Structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoylCoA and peptide provide insights about substrate recognition and catalysis. Biochemistry. 40:2001;6335-6343.
20. Ehlert K., et al. Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain formation. J. Bacteriol. 179:1997;7573-7576.
21. Wu G., et al. Convergent evolution of Trichomonas vaginalis lactate dehydrogenase from malate dehydrogenase. Proc. Natl. Acad. Sci. U.S.A. 96:1999;6285-6290.
22. Ray S.S., et al. X-ray structure of an M. jannaschii DNA-binding protein: implications for antibiotic resistance in S. aureus. Proteins. 50:2003;170-173.
23. de Lencastre H., et al. Antibiotic resistance as a stress response: complete sequencing of a large number of chromosomal loci in Staphylococcus aureus strain COL that impact on the expression of resistance to methicillin. Microb. Drug Resist. 5:1999;163-175.
24. Altschul S.F., Koonin E.V. Iterated profile searches with PSI-BLAST-a tool for discovery in protein databases. Trends Biochem. Sci. 23:1998;444-447.
25. Jeanmougin F., et al. Multiple sequence alignment with Clustal X. Trends Biochem. Sci. 23:1998;403-405.
26. Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:1993;779-815.
27. Sippl M.J. Recognition of errors in three-dimensional structures of proteins. Proteins. 17:1993;355-362.
28. Ibba M., Soll D. Aminoacyl-tRNA synthesis. Annu. Rev. Biochem. 69:2000;617-650.
29. Ribas D.P., et al. Functional analysis of peptide motif for RNA microhelix binding suggests new family of RNA-binding domains. EMBO J. 17:1998;5449-5457.
30. Armon A., et al. ConSurf: an algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic information. J. Mol. Biol. 307:2001;447-463.
31. Lo C.L., et al. SCOP: a structural classification of proteins database. Nucleic Acids Res. 28:2000;257-259.