Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1983 Oct;156(1):136–140. doi: 10.1128/jb.156.1.136-140.1983

Cleavage and resynthesis of peptide cross bridges in Escherichia coli murein.

E W Goodell, U Schwarz
PMCID: PMC215061  PMID: 6352673

Abstract

In Escherichia coli, peptide cross bridges in the murein undergo turnover after they are synthesized. Peptide cross bridges formed in the presence of [3H]diaminopimelic acid were found to lose 3H label from their donor peptides after the [3H]diaminopimelic acid was removed from the growth medium. There was a corresponding increase in the amount of 3H label in acceptor peptides so that the total amount of label in the peptide cross bridges remained constant. Our explanation of this observation is that the cross bridges are cleaved by the cell, and the original 3H-labeled donor peptides are incorporated into new cross bridges. Since these 3H-labeled peptides are now only tetrapeptides, they can only be used as acceptors when new cross bridges are formed.

Full text

PDF
136

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Braun V., Wolff H. Attachment of lipoprotein to murein (peptidoglycan) of Escherichia coli in the presence and absence of penicillin FL 1060. J Bacteriol. 1975 Sep;123(3):888–897. doi: 10.1128/jb.123.3.888-897.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Fordham W. D., Gilvarg C. Kinetics of cross-linking of peptidoglycan in Bacillus megaterium. J Biol Chem. 1974 Apr 25;249(8):2478–2482. [PubMed] [Google Scholar]
  3. Gmeiner J., Essig P., Martin H. H. Characterization of minor fragments after digestion of Escherichia coli murein with endo-N,O-diacetylmuramidase from Chalaropsis, and determination of glycan chain length. FEBS Lett. 1982 Feb 8;138(1):109–112. doi: 10.1016/0014-5793(82)80406-7. [DOI] [PubMed] [Google Scholar]
  4. Gmeiner J. Identification of peptide-cross-linked trisdisaccharide peptide trimers in murein of Escherichia coli. J Bacteriol. 1980 Jul;143(1):510–512. doi: 10.1128/jb.143.1.510-512.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hartmann R., Höltje J. V., Schwarz U. Targets of penicillin action in Escherichia coli. Nature. 1972 Feb 25;235(5339):426–429. doi: 10.1038/235426a0. [DOI] [PubMed] [Google Scholar]
  6. Keck W., Schwarz U. Escherichia coli murein-DD-endopeptidase insensitive to beta-lactam antibiotics. J Bacteriol. 1979 Sep;139(3):770–774. doi: 10.1128/jb.139.3.770-774.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Koch A. L., Higgins M. L., Doyle R. J. Surface tension-like forces determine bacterial shapes: Streptococcus faecium. J Gen Microbiol. 1981 Mar;123(1):151–161. doi: 10.1099/00221287-123-1-151. [DOI] [PubMed] [Google Scholar]
  8. Matsuhashi M., Takagaki Y., Maruyama I. N., Tamaki S., Nishimura Y., Suzuki H., Ogino U., Hirota Y. Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity. Proc Natl Acad Sci U S A. 1977 Jul;74(7):2976–2979. doi: 10.1073/pnas.74.7.2976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Ryter A., Hirota Y., Schwarz U. Process of cellular division in Escherichia coli growth pattern of E. coli murein. J Mol Biol. 1973 Jun 25;78(1):185–195. doi: 10.1016/0022-2836(73)90437-3. [DOI] [PubMed] [Google Scholar]
  10. Schwarz U., Ryter A., Rambach A., Hellio R., Hirota Y. Process of cellular division in Escherichia coli: differention of growth zones in the Sacculus. J Mol Biol. 1975 Nov 15;98(4):749–759. doi: 10.1016/s0022-2836(75)80008-8. [DOI] [PubMed] [Google Scholar]
  11. Suzuki H., Nishimura Y., Yasuda S., Nishimura A., Yamada M., Hirota Y. Murein-lipoprotein of Escherichia coli: a protein involved in the stabilization of bacterial cell envelope. Mol Gen Genet. 1978 Nov 16;167(1):1–9. doi: 10.1007/BF00270315. [DOI] [PubMed] [Google Scholar]
  12. Tamura T., Imae Y., Strominger J. L. Purification to homogeneity and properties of two D-alanine carboxypeptidases I From Escherichia coli. J Biol Chem. 1976 Jan 25;251(2):414–423. [PubMed] [Google Scholar]
  13. Verwer R. W., Nanninga N., Keck W., Schwarz U. Arrangement of glycan chains in the sacculus of Escherichia coli. J Bacteriol. 1978 Nov;136(2):723–729. doi: 10.1128/jb.136.2.723-729.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. WEIDEL W., PELZER H. BAGSHAPED MACROMOLECULES--A NEW OUTLOOK ON BACTERIAL CELL WALLS. Adv Enzymol Relat Areas Mol Biol. 1964;26:193–232. doi: 10.1002/9780470122716.ch5. [DOI] [PubMed] [Google Scholar]
  15. de Pedro M. A., Schwarz U. Heterogeneity of newly inserted and preexisting murein in the sacculus of Escherichia coli. Proc Natl Acad Sci U S A. 1981 Sep;78(9):5856–5860. doi: 10.1073/pnas.78.9.5856. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES