|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 276, Issue 43, 39618-39628, October 26, 2001
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the The recently identified murMN operon
of Streptococcus pneumoniae encodes enzymes involved in the
synthesis of branched structured muropeptides of the pneumococcal cell
wall peptidoglycan. Its inactivation was shown to cause production of a
peptidoglycan composed exclusively of linear muropeptides and a
virtually complete loss of resistance in penicillin-resistant strains.
The studies described in this communication follow up these
observations in several directions. The substrate of the MurM-catalyzed
reaction (addition of alanine or serine) was identified as the
lipid-linked N-acetylglucosamine-muramyl pentapeptide.
Different murM alleles from several
penicillin-resistant S. pneumoniae strains, each with a
characteristic branched peptide pattern, were cloned into pLS578, a
pneumococcal plasmid capable of replicating in S. pneumoniae, and transformed into the penicillin-susceptible
laboratory strain R36A. All transformants remained
penicillin-susceptible; however, their cell wall composition changed in
directions corresponding to the muropeptide pattern of the strain from
which the murM allele was derived. This suggests that the
muropeptide composition of the pneumococcal cell walls is determined by
the particular murM allele carried by the cells. A 30-amino
acid long sequence within the MurM protein was shown to be the main
determinant of the specificity of the reaction (addition of alanine
versus serine).
Functional Analysis of Streptococcus pneumoniae MurM
Reveals the Region Responsible for Its Specificity in the Synthesis of
Branched Cell Wall Peptides*
§¶,
, and**
Laboratory of Microbiology, The Rockefeller
University, New York, New York 10021 and the § Molecular
Genetics Unit, Instituto de Tecnologia Química e
Biológica, Universidade Nova de Lisboa, 2780 Oeiras,
Portugal
*
This work was supported in part by a grant from the National
Institutes of Health RO1-AI37275 and by the Irene Diamond Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Permanent address: Institute of Theoretical and Experimental
Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region 142292, Russia.
**
To whom correspondence should be addressed: Laboratory of
Microbiology, The Rockefeller University, 1230 York Ave., New York, NY
10021. Tel.: 212-327-8278; Fax: 212-327-8688; E-mail:
tomasz@mail.rockefeller.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  G. De Pascale, A. J. Lloyd, J. A. Schouten, A. M. Gilbey, D. I. Roper, C. G. Dowson, and T. D. H. Bugg Kinetic Characterization of Lipid II-Ala:Alanyl-tRNA Ligase (MurN) from Streptococcus pneumoniae using Semisynthetic Aminoacyl-lipid II Substrates J. Biol. Chem., December 12, 2008; 283(50): 34571 - 34579. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. J. Lloyd, A. M. Gilbey, A. M. Blewett, G. De Pascale, A. El Zoeiby, R. C. Levesque, A. C. Catherwood, A. Tomasz, T. D. H. Bugg, D. I. Roper, et al. Characterization of tRNA-dependent Peptide Bond Formation by MurM in the Synthesis of Streptococcus pneumoniae Peptidoglycan J. Biol. Chem., March 7, 2008; 283(10): 6402 - 6417. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. van Heijenoort Lipid Intermediates in the Biosynthesis of Bacterial Peptidoglycan Microbiol. Mol. Biol. Rev., December 1, 2007; 71(4): 620 - 635. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. S. Kharat and A. Tomasz Inactivation of the srtA Gene Affects Localization of Surface Proteins and Decreases Adhesion of Streptococcus pneumoniae to Human Pharyngeal Cells In Vitro Infect. Immun., May 1, 2003; 71(5): 2758 - 2765. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Rohrer and B. Berger-Bachi FemABX Peptidyl Transferases: a Link between Branched-Chain Cell Wall Peptide Formation and {beta}-Lactam Resistance in Gram-Positive Cocci Antimicrob. Agents Chemother., March 1, 2003; 47(3): 837 - 846. [Full Text] [PDF]
|
|
|
|
 |
|
 S. R. Filipe, E. Severina, and A. Tomasz The murMN operon: A functional link between antibiotic resistance and antibiotic tolerance in Streptococcuspneumoniae PNAS, February 5, 2002; 99(3): 1550 - 1555. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |