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EcoSal Plus

Domain 4:

Synthesis and Processing of Macromolecules

Peptidoglycan Recycling

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  • Authors: Tsuyoshi Uehara1,4, and James T. Park2
  • Editor: James M. Slauch3
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111; 2: Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111; 3: The Schoold of Molecular and Cellular Biology, University of Illinois at Urbana-Champaign, Urbana, IL
  • Received 15 June 2008 Accepted 04 August 2008 Published 15 October 2008
  • Address correspondence to James T. Park james.park@tufts.edu
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  • Abstract:

    Peptidoglycan (PG) recycling allows to reuse the massive amounts of sacculus components that are released during elongation. Goodell and Schwarz, in 1985, labeled cells with 3H-diaminopimelic acid (DAP) and chased. During the chase, the DAP pool dropped dramatically, whereas the precursor pool dropped only slightly. This could only occur if DAP from the sacculi was being used to produce more precursor. They calculated that the cells were recycling about 45% of their wall DAP (actually, 60% of the side walls, since the poles are stable). Thus, recycling was discovered. Goodell went on to show that the tripeptide, -Ala--Glu-DAP, could be taken up via opp and used directly to form PG. It was subsequently shown that uptake was predominantly via a permease, AmpG, that was specific for GlcNAc-anhMurNAc with attached peptides. Eleven genes have been identified which appear to have as their sole function the recovery of degradation products from PG. PG represents only 2.5% of the cell mass, so the reason for this investment in recycling is obscure. Recycling enzymes exist that are specific for every bond in the principal product taken up by AmpG, namely, GlcNAc-anh-MurNAc-tetrapeptide. However, most of the tripeptide, -Ala--Glu-DAP, is used by murein peptide ligase (Mpl) to form the precursor intermediate UDP-MurNAc-tripeptide. anh-MurNAc can be converted to GlcNAc by a two-step process and thus is available for use. Surprisingly, in the absence of AmpD, an enzyme that cleaves the anh-MurNAc--Ala bond, anh-MurNAc-tripeptide accumulates, resulting in induction of beta-lactamase. However, this has nothing to do with the induction of beta-lactamase by beta-lactam antibiotics. Uehara, Suefuji, and Park (unpublished data) have some evidence suggesting that murein pentapeptide may be involved. The presence of orthologs suggests that recycling also exists in many Gram-negative bacteria. Surprisingly, the ortholog search also revealed that all mammals may have an AmpG ortholog! Hence, mammalian AmpG may be involved in the process of innate immunity.

  • Citation: Uehara T, Park J. 2008. Peptidoglycan Recycling, EcoSal Plus 2008; doi:10.1128/ecosalplus.4.7.1.5

Key Concept Ranking

beta-Lactam Antibiotics
0.5170359
Pseudomonas aeruginosa
0.49352276
0.5170359

References

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26. Schmidt DM, Hubbard BK, Gerlt JA. 2001. Evolution of enzymatic activities in the enolase superfamily: functional assignment of unknown proteins in Bacillus subtilis and Escherichia coli as L-Ala-D/L-Glu epimerases. Biochemistry 40:15707–15715. [PubMed][CrossRef]
27. Cheng Q, Li H, Merdek K, Park JT. 2000. Molecular characterization of the β-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling. J Bacteriol 182:4836–4840. [PubMed][CrossRef]
28. Vötsch W, Templin MF. 2000. Characterization of a β-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and β-lactamase induction. J Biol Chem 275:39032–39038. [PubMed][CrossRef]
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36. Jacobs C, Joris B, Jamin M, Klarsov K, Van Beeumen J, Mengin-Lecreulx D, van Heijenoort J, Park JT, Normark S, Frère JM. 1995. AmpD, essential for both β-lactamase regulation and cell wall recycling, is a novel cytosolic N-acetylmuramyl-L-alanine amidase. Mol Microbiol 15:553–559. [PubMed][CrossRef]
37. Park JT, Uehara T. 2008. How bacteria consume their own exoskeletons (turnover and recycling of the cell wall peptidoglycan). Microbiol Mol Biol Rev 72:211–227. [PubMed][CrossRef]
38. Park JT. 2001. Identification of a dedicated recycling pathway for anhydro-N-acetylmuramic acid and N-acetylglucosamine derived from Escherichia coli cell wall murein. J Bacteriol 183:3842–3847. [CrossRef]
39. Mengin-Lecreulx D, van Heijenoort J. 1996. Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli. J Biol Chem 271:32–39. [PubMed][CrossRef]
40. Mengin-Lecreulx D, van Heijenoort J. 1994. Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis. J Bacteriol 176:5788–5795.[PubMed]
41. Mengin-Lecreulx D, van Heijenoort J. 1993. Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate uridyltransferase in Escherichia coli. J Bacteriol 175:6150–6157.[PubMed]
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43. Parquet C, Flouret B, Leduc M, Hirota Y, van Heijenoort J. 1983. N-Acetylmuramoyl-L-alanine amidase of Escherichia coli K12. Possible physiological functions. Eur J Biochem 133:371–377. [PubMed][CrossRef]
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2008-10-15
2017-06-23

Abstract:

Peptidoglycan (PG) recycling allows to reuse the massive amounts of sacculus components that are released during elongation. Goodell and Schwarz, in 1985, labeled cells with 3H-diaminopimelic acid (DAP) and chased. During the chase, the DAP pool dropped dramatically, whereas the precursor pool dropped only slightly. This could only occur if DAP from the sacculi was being used to produce more precursor. They calculated that the cells were recycling about 45% of their wall DAP (actually, 60% of the side walls, since the poles are stable). Thus, recycling was discovered. Goodell went on to show that the tripeptide, -Ala--Glu-DAP, could be taken up via opp and used directly to form PG. It was subsequently shown that uptake was predominantly via a permease, AmpG, that was specific for GlcNAc-anhMurNAc with attached peptides. Eleven genes have been identified which appear to have as their sole function the recovery of degradation products from PG. PG represents only 2.5% of the cell mass, so the reason for this investment in recycling is obscure. Recycling enzymes exist that are specific for every bond in the principal product taken up by AmpG, namely, GlcNAc-anh-MurNAc-tetrapeptide. However, most of the tripeptide, -Ala--Glu-DAP, is used by murein peptide ligase (Mpl) to form the precursor intermediate UDP-MurNAc-tripeptide. anh-MurNAc can be converted to GlcNAc by a two-step process and thus is available for use. Surprisingly, in the absence of AmpD, an enzyme that cleaves the anh-MurNAc--Ala bond, anh-MurNAc-tripeptide accumulates, resulting in induction of beta-lactamase. However, this has nothing to do with the induction of beta-lactamase by beta-lactam antibiotics. Uehara, Suefuji, and Park (unpublished data) have some evidence suggesting that murein pentapeptide may be involved. The presence of orthologs suggests that recycling also exists in many Gram-negative bacteria. Surprisingly, the ortholog search also revealed that all mammals may have an AmpG ortholog! Hence, mammalian AmpG may be involved in the process of innate immunity.

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Figure 1

Reprinted from reference 37 with permission.

Citation: Uehara T, Park J. 2008. Peptidoglycan Recycling, EcoSal Plus 2008; doi:10.1128/ecosalplus.4.7.1.5
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Reprinted from reference 37 with permission.

Citation: Uehara T, Park J. 2008. Peptidoglycan Recycling, EcoSal Plus 2008; doi:10.1128/ecosalplus.4.7.1.5
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Tables

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Table 1

Murein recycling enzymes

Citation: Uehara T, Park J. 2008. Peptidoglycan Recycling, EcoSal Plus 2008; doi:10.1128/ecosalplus.4.7.1.5

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