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. 1975 Aug;72(8):2999–3003. doi: 10.1073/pnas.72.8.2999

Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.

B G Spratt
PMCID: PMC432906  PMID: 1103132

Abstract

The varied effects of beta-lactam antibiotics on cell division, cell elongation, and cell shape in E. coli are shown to be due to the presence of three essential penicillin binding proteins with distinct roles in these three processes. (A) Cell shape: beta-Lactams that specifically result in the production of ovoid cells bind to penicillin binding protein 2 (molecular weight 66,000). A mutant has been isolated that fails to bind beta-lactams to protein 2, and that grows as round cells. (B) Cell division: beta-Lactams that specifically inhibit cell division bind preferentially to penicillin binding protein 3 (molecular weight 60,000). A temperature-sensitive cell division mutant has been shown to have a thermolabile protein 3. (C) Cell elongation: One beta-lactam that preferentially inhibits cell elongation and causes cell lysis binds preferentially to binding protein 1 (molecular weight 91,000). Evidence is presented that penicillin bulge formation is due to the inhibition of proteins 2 and 3 in the absence of inhibition of protein 1.

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Selected References

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

  1. Blumberg P. M., Strominger J. L. Interaction of penicillin with the bacterial cell: penicillin-binding proteins and penicillin-sensitive enzymes. Bacteriol Rev. 1974 Sep;38(3):291–335. doi: 10.1128/br.38.3.291-335.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
  3. Burdett I. D., Murray R. G. Electron microscope study of septum formation in Escherichia coli strains B and B-r during synchronous growth. J Bacteriol. 1974 Sep;119(3):1039–1056. doi: 10.1128/jb.119.3.1039-1056.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. 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]
  5. Inouye M., Guthrie J. P. A mutation which changes a membrane protein of E. coli. Proc Natl Acad Sci U S A. 1969 Nov;64(3):957–961. doi: 10.1073/pnas.64.3.957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. James R., Haga J. Y., Pardee A. B. Inhibition of an early event in the cell division cycle of Escherichia coli by FL1060, an amidinopenicillanic acid. J Bacteriol. 1975 Jun;122(3):1283–1292. doi: 10.1128/jb.122.3.1283-1292.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Kamiryo T., Strominger J. L. Penicillin-resistant temperature-sensitive mutants of Escherichia coli which synthesize hypo- or hyper-cross-linked peptidoglycan. J Bacteriol. 1974 Feb;117(2):568–577. doi: 10.1128/jb.117.2.568-577.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. LEDERBERG J. Mechanism of action of penicillin. J Bacteriol. 1957 Jan;73(1):144–144. doi: 10.1128/jb.73.1.144-144.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Lund F., Tybring L. 6 -amidinopenicillanic acids--a new group of antibiotics. Nat New Biol. 1972 Apr 5;236(66):135–137. doi: 10.1038/newbio236135a0. [DOI] [PubMed] [Google Scholar]
  10. Matsuhashi S., Kamiryo T., Blumberg P. M., Linnett P., Willoughby E., Strominger J. L. Mechanism of action and development of resistance to a new amidino penicillin. J Bacteriol. 1974 Feb;117(2):578–587. doi: 10.1128/jb.117.2.578-587.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Melchior N. H., Blom J., Tybring L., Birch-Andersen A. Light and electron microscopy of the early response of Escherichia coli to a 6beta-amidinopenicillanic acid (FL 1060). Acta Pathol Microbiol Scand B Microbiol Immunol. 1973 Aug;81(4):393–407. doi: 10.1111/j.1699-0463.1973.tb02222.x. [DOI] [PubMed] [Google Scholar]
  12. Mirelman D., Bracha R., Sharon N. Studies on the elongation of bacterial cell wall peptidoglycan and its inhibition by penicillin. Ann N Y Acad Sci. 1974 May 10;235(0):326–347. doi: 10.1111/j.1749-6632.1974.tb43275.x. [DOI] [PubMed] [Google Scholar]
  13. Nguyen-Distèche M., Pollock J. J., Ghuysen J. M., Puig J., Reynolds P., Perkins H. R., Coyette J., Salton M. R. Sensitivity to ampicillin and cephalothin of enzymes involved in wall peptide crosslinking in Escherichia coli K12, strain 44. Eur J Biochem. 1974 Feb 1;41(3):457–463. doi: 10.1111/j.1432-1033.1974.tb03287.x. [DOI] [PubMed] [Google Scholar]
  14. Schwarz U., Asmus A., Frank H. Autolytic enzymes and cell division of Escherichia coli. J Mol Biol. 1969 May 14;41(3):419–429. doi: 10.1016/0022-2836(69)90285-x. [DOI] [PubMed] [Google Scholar]
  15. Spratt B. G., Pardee A. B. Penicillin-binding proteins and cell shape in E. coli. Nature. 1975 Apr 10;254(5500):516–517. doi: 10.1038/254516a0. [DOI] [PubMed] [Google Scholar]
  16. Strominger J. L., Blumberg P. M., Suginaka H., Umbreit J., Wickus G. G. How penicillin kills bacteria: progress and problems. Proc R Soc Lond B Biol Sci. 1971 Dec 31;179(1057):369–383. doi: 10.1098/rspb.1971.0103. [DOI] [PubMed] [Google Scholar]
  17. Strominger J. L., Willoughby E., Kamiryo T., Blumberg P. M., Yocum R. R. Penicillin-sensitive enzymes and penicillin-binding components in bacterial cells. Ann N Y Acad Sci. 1974 May 10;235(0):210–224. doi: 10.1111/j.1749-6632.1974.tb43267.x. [DOI] [PubMed] [Google Scholar]
  18. Suginaka H., Blumberg P. M., Strominger J. L. Multiple penicillin-binding components in Bacillus subtilis, Bacillus cereus, Staphylococcus aureus, and Escherichia coli. J Biol Chem. 1972 Sep 10;247(17):5279–5288. [PubMed] [Google Scholar]

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