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. 1980 Jul;18(1):148–157. doi: 10.1128/aac.18.1.148

Penicillin-binding proteins in bacteria.

N H Georgopapadakou, F Y Liu
PMCID: PMC283955  PMID: 7416741

Abstract

The penicilllin-binding proteins (PBPs) of several gram-positive and gram-negative bacteria have been examined. The results indicate that: (i) PBPs are membrane proteins with molecular weights ranging from 40,000 to 120,000. When extracted with Triton X-100 from sonicated cells, they appear to fall into two patterns: one found in rods and the other in spheres. A major difference is in the low-molecular-weight component, which is usually the major PBP in bacilli but a minor one in cocci. (ii) There is a wide variation in both the number and the amount of PBPs in different bacteria, and taxonomically related bacteria tend to have similar PBP patterns. These patterns often correlate with the affinity of PBPs for penicillin and other beta-lactam antibiotics. (iii) The low-molecular-weight component usually releases penicillin spontaneously with a half-life of 10 min or less. Most, but not all, PBPs release bound penicillin in the presence of neutral hydroxylamine (0.2 to 0.8 M).

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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. Inactivation of D-alanine carboxypeptidase by penicillins and cephalosporins is not lethal in Bacillus subtilis. Proc Natl Acad Sci U S A. 1971 Nov;68(11):2814–2817. doi: 10.1073/pnas.68.11.2814. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. 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]
  3. Blumberg P. M., Strominger J. L. Isolation by covalent affinity chromatography of the penicillin-binding components from membranes of Bacillus subtilis. Proc Natl Acad Sci U S A. 1972 Dec;69(12):3751–3755. doi: 10.1073/pnas.69.12.3751. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Blumberg P. M., Yocum R. R., Willoughby E., Strominger J. L. Binding of (14C)penicillin G to the membrane-bound and the purified D-alanine carboxypeptidases from Bacillus stearothermophilus and Bacillus subtilis and its release. J Biol Chem. 1974 Nov 10;249(21):6828–6835. [PubMed] [Google Scholar]
  5. 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]
  6. Buchanan C. E., Strominger J. L. Altered penicillin-binding components in penicillin-resistant mutants of Bacillus subtilis. Proc Natl Acad Sci U S A. 1976 Jun;73(6):1816–1820. doi: 10.1073/pnas.73.6.1816. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Chase H. A., Shepherd S. T., Reynolds P. E. Studies on the penicillin-binding components of Bacillus megaterium. FEBS Lett. 1977 Apr 15;76(2):199–203. doi: 10.1016/0014-5793(77)80151-8. [DOI] [PubMed] [Google Scholar]
  8. Cocks G. T., Wilson A. C. Enzyme evolution in the Enterobacteriaceae. J Bacteriol. 1972 Jun;110(3):793–802. doi: 10.1128/jb.110.3.793-802.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Coyette J., Ghuysen J. M., Fontana R. Solubilization and isolation of the membrane-bound DD-carboxypeptidase of Streptococcus faecalis ATCC9790. Properties of the purified enzyme. Eur J Biochem. 1978 Jul 17;88(1):297–305. doi: 10.1111/j.1432-1033.1978.tb12450.x. [DOI] [PubMed] [Google Scholar]
  10. Forsberg C. W., Ward J. B. N-acetylmuramyl-L-alanine amidase of Bacillus licheniformis and its L-form. J Bacteriol. 1972 Jun;110(3):878–888. doi: 10.1128/jb.110.3.878-888.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Frere J., Ghuysen J., Degelaen J., Loffet A., Perkins H. R. Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39. Nature. 1975 Nov 13;258(5531):168–170. doi: 10.1038/258168a0. [DOI] [PubMed] [Google Scholar]
  12. Grimont P. A., Grimont F. The genus Serratia. Annu Rev Microbiol. 1978;32:221–248. doi: 10.1146/annurev.mi.32.100178.001253. [DOI] [PubMed] [Google Scholar]
  13. Hammarström S., Strominger J. L. Degradation of penicillin G to phenylacetylglycine by D-alanine carboxypeptidase from Bacillus stearothermophilus. Proc Natl Acad Sci U S A. 1975 Sep;72(9):3463–3467. doi: 10.1073/pnas.72.9.3463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Hammes W. P. Biosynthesis of peptidoglycan in Gaffkya homari. The mode of action of penicillin G and mecillinam. Eur J Biochem. 1976 Nov 1;70(1):107–113. doi: 10.1111/j.1432-1033.1976.tb10961.x. [DOI] [PubMed] [Google Scholar]
  15. Iwaya M., Strominger J. L. Simultaneous deletion of D-alanine carboxypeptidase IB-C and penicillin-binding component IV in a mutant of Escherichia coli K12. Proc Natl Acad Sci U S A. 1977 Jul;74(7):2980–2984. doi: 10.1073/pnas.74.7.2980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Kleppe G., Strominger J. L. Studies of the high molecular weight penicillin-binding proteins of Bacillus subtilis. J Biol Chem. 1979 Jun 10;254(11):4856–4862. [PubMed] [Google Scholar]
  17. Kozarich J. W., Strominger J. L. A membrane enzyme from Staphylococcus aureus which catalyzes transpeptidase, carboxypeptidase, and penicillinase activities. J Biol Chem. 1978 Feb 25;253(4):1272–1278. [PubMed] [Google Scholar]
  18. 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]
  19. 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]
  20. Laskey R. A., Mills A. D. Quantitative film detection of 3H and 14C in polyacrylamide gels by fluorography. Eur J Biochem. 1975 Aug 15;56(2):335–341. doi: 10.1111/j.1432-1033.1975.tb02238.x. [DOI] [PubMed] [Google Scholar]
  21. Leyh-Bouille M., Coyette J., Ghuysen J. M., Idczak J., Perkins H. R., Nieto M. Penicillin-sensitive DD-carboxypeptidase from Streptomyces strain R 61. Biochemistry. 1971 May 25;10(11):2163–2170. doi: 10.1021/bi00787a032. [DOI] [PubMed] [Google Scholar]
  22. 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]
  23. Reynolds P. E., Shepherd S. T., Chase H. A. Identification of the binding protein which may be the target of penicillin action in Bacillus megaterium. Nature. 1978 Feb 9;271(5645):568–570. doi: 10.1038/271568a0. [DOI] [PubMed] [Google Scholar]
  24. Shepherd S. T., Chase H. A., Reynolds P. E. The separation and properties of two penicillin-binding proteins from Salmonella typhimurium. Eur J Biochem. 1977 Sep;78(2):521–523. doi: 10.1111/j.1432-1033.1977.tb11765.x. [DOI] [PubMed] [Google Scholar]
  25. Spratt B. G. Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc Natl Acad Sci U S A. 1975 Aug;72(8):2999–3003. doi: 10.1073/pnas.72.8.2999. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. 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]
  27. 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]
  28. Suzuki H., Nishimura Y., Hirota Y. On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins. Proc Natl Acad Sci U S A. 1978 Feb;75(2):664–668. doi: 10.1073/pnas.75.2.664. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. 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]
  30. Tipper D. J., Strominger J. L. Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc Natl Acad Sci U S A. 1965 Oct;54(4):1133–1141. doi: 10.1073/pnas.54.4.1133. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Tomasz A., Waks S. Mechanism of action of penicillin: triggering of the pneumococcal autolytic enzyme by inhibitors of cell wall synthesis. Proc Natl Acad Sci U S A. 1975 Oct;72(10):4162–4166. doi: 10.1073/pnas.72.10.4162. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Wise E. M., Jr, Park J. T. Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis. Proc Natl Acad Sci U S A. 1965 Jul;54(1):75–81. doi: 10.1073/pnas.54.1.75. [DOI] [PMC free article] [PubMed] [Google Scholar]

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