Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1995 Apr;177(7):1860–1863. doi: 10.1128/jb.177.7.1860-1863.1995

Differences between inner membrane and peptidoglycan-associated PBP1B dimers of Escherichia coli.

C A Zijderveld 1, M E Aarsman 1, N Nanninga 1
PMCID: PMC176817  PMID: 7896712

Abstract

Earlier studies revealed that PBP1B of Escherichia coli occurred as a monomeric as well as a dimeric form (C.A.L. Zijderveld, M.E.G. Aarsman, T. den Blaauwen, and N. Nanninga, J. Bacteriol. 173:5740-5746, 1991). In this study, the dimer of PBP1B was further analyzed. It appeared that the dimeric form could be divided into two classes. One class, which cofractionated with the cell wall fraction, could be artificially cross-linked to peptidoglycan, indicating a close association with the latter. This class of PBP1B dimers was sensitive to beta-mercaptoethanol. The second class, like the monomeric form of PBP1B, could be isolated with the inner membrane fraction. This dimeric form dissociated in the presence of zinc in combination with beta-mercaptoethanol.

Full Text

The Full Text of this article is available as a PDF (225.9 KB).

Selected References

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

  1. Bardwell J. C., McGovern K., Beckwith J. Identification of a protein required for disulfide bond formation in vivo. Cell. 1991 Nov 1;67(3):581–589. doi: 10.1016/0092-8674(91)90532-4. [DOI] [PubMed] [Google Scholar]
  2. Broome-Smith J. K., Edelman A., Yousif S., Spratt B. G. The nucleotide sequences of the ponA and ponB genes encoding penicillin-binding protein 1A and 1B of Escherichia coli K12. Eur J Biochem. 1985 Mar 1;147(2):437–446. doi: 10.1111/j.1432-1033.1985.tb08768.x. [DOI] [PubMed] [Google Scholar]
  3. Casadaban M. J. Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J Mol Biol. 1976 Jul 5;104(3):541–555. doi: 10.1016/0022-2836(76)90119-4. [DOI] [PubMed] [Google Scholar]
  4. Den Blaauwen T., Wientjes F. B., Kolk A. H., Spratt B. G., Nanninga N. Preparation and characterization of monoclonal antibodies against native membrane-bound penicillin-binding protein 1B of Escherichia coli. J Bacteriol. 1989 Mar;171(3):1394–1401. doi: 10.1128/jb.171.3.1394-1401.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Filip C., Fletcher G., Wulff J. L., Earhart C. F. Solubilization of the cytoplasmic membrane of Escherichia coli by the ionic detergent sodium-lauryl sarcosinate. J Bacteriol. 1973 Sep;115(3):717–722. doi: 10.1128/jb.115.3.717-722.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hawkins H. C., Blackburn E. C., Freedman R. B. Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate. Biochem J. 1991 Apr 15;275(Pt 2):349–353. doi: 10.1042/bj2750349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Ioannides C. G., Itoh K., Fox F. E., Pahwa R., Good R. A., Platsoucas C. D. Identification of a second T-cell antigen receptor in human and mouse by an anti-peptide gamma-chain-specific monoclonal antibody. Proc Natl Acad Sci U S A. 1987 Jun;84(12):4244–4248. doi: 10.1073/pnas.84.12.4244. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Ishino F., Mitsui K., Tamaki S., Matsuhashi M. Dual enzyme activities of cell wall peptidoglycan synthesis, peptidoglycan transglycosylase and penicillin-sensitive transpeptidase, in purified preparations of Escherichia coli penicillin-binding protein 1A. Biochem Biophys Res Commun. 1980 Nov 17;97(1):287–293. doi: 10.1016/s0006-291x(80)80166-5. [DOI] [PubMed] [Google Scholar]
  9. Ishino F., Park W., Tomioka S., Tamaki S., Takase I., Kunugita K., Matsuzawa H., Asoh S., Ohta T., Spratt B. G. Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and rodA protein. J Biol Chem. 1986 May 25;261(15):7024–7031. [PubMed] [Google Scholar]
  10. Ishino F., Tamaki S., Spratt B. G., Matsuhashi M. A mecillinam-sensitive peptidoglycan crosslinking reaction in Escherichia coli. Biochem Biophys Res Commun. 1982 Dec 15;109(3):689–696. doi: 10.1016/0006-291x(82)91995-7. [DOI] [PubMed] [Google Scholar]
  11. Jefferson J. R., Hunt J. B., Ginsburg A. Zinc interactions with regulatory dimers from Escherichia coli aspartate transcarbamoylase. Biochemistry. 1990 Jul 17;29(28):6687–6698. doi: 10.1021/bi00480a019. [DOI] [PubMed] [Google Scholar]
  12. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  13. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  14. Le Moual H., Devault A., Roques B. P., Crine P., Boileau G. Identification of glutamic acid 646 as a zinc-coordinating residue in endopeptidase-24.11. J Biol Chem. 1991 Aug 25;266(24):15670–15674. [PubMed] [Google Scholar]
  15. Matsuzawa H., Datta P., Matsuhashi M. Behavior of penicillin-binding proteins in Escherichia coli upon heat and detergent treatments and partial purification of penicillin-binding proteins 1A and 1B. J Bacteriol. 1979 Jun;138(3):1029–1032. doi: 10.1128/jb.138.3.1029-1032.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Nakagawa J., Matsuhashi M. Molecular divergence of a major peptidoglycan synthetase with transglycosylase-transpeptidase activities in Escherichia coli --- penicillin-binding protein 1Bs. Biochem Biophys Res Commun. 1982 Apr 29;105(4):1546–1553. doi: 10.1016/0006-291x(82)90964-0. [DOI] [PubMed] [Google Scholar]
  17. Rosenbusch J. P. Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding. J Biol Chem. 1974 Dec 25;249(24):8019–8029. [PubMed] [Google Scholar]
  18. Spratt B. G., Cromie K. D. Penicillin-binding proteins of gram-negative bacteria. Rev Infect Dis. 1988 Jul-Aug;10(4):699–711. doi: 10.1093/clinids/10.4.699. [DOI] [PubMed] [Google Scholar]
  19. Spratt B. G. Properties of the penicillin-binding proteins of Escherichia coli K12,. Eur J Biochem. 1977 Jan;72(2):341–352. doi: 10.1111/j.1432-1033.1977.tb11258.x. [DOI] [PubMed] [Google Scholar]
  20. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Zijderveld C. A., Aarsman M. E., den Blaauwen T., Nanninga N. Penicillin-binding protein 1B of Escherichia coli exists in dimeric forms. J Bacteriol. 1991 Sep;173(18):5740–5746. doi: 10.1128/jb.173.18.5740-5746.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. van Heijenoort Y., van Heijenoort J. Biosynthesis of the peptidoglycan of Escherichia coli K-12: properties of the in vitro polymerization by transglycosylation. FEBS Lett. 1980 Feb 11;110(2):241–244. doi: 10.1016/0014-5793(80)80082-2. [DOI] [PubMed] [Google Scholar]

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

RESOURCES