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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1976 Jun;73(6):1882–1886. doi: 10.1073/pnas.73.6.1882

Morphogenesis of the bacterial division septum: a new class of septation-defective mutants.

R A Weigand, K D Vinci, L I Rothfield
PMCID: PMC430411  PMID: 778849

Abstract

A new class of mutants of Salmonella typhimurium (lkyD mutants) are described. The mutants are defective in morphogenesis of the division septum, and are characterized by a failure of the outer membrane to invaginate despite normal ingrowth of the cytoplasmic membrane and murein layers of the growing septum. The cell envelopes of the mutants show a significant decrease in the bound form of murein-lipoprotein and a corresponding increase in the free form of the lipoprotein. This suggests that the morphogenic defect may result from a defect in formation of covalent bonds between the free lipoprotein of the outer membrane and the murein of the nascent septum.

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Selected References

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  1. Braun V., Rehn K. Chemical characterization, spatial distribution and function of a lipoprotein (murein-lipoprotein) of the E. coli cell wall. The specific effect of trypsin on the membrane structure. Eur J Biochem. 1969 Oct;10(3):426–438. doi: 10.1111/j.1432-1033.1969.tb00707.x. [DOI] [PubMed] [Google Scholar]
  2. Braun V., Rehn K., Wolff H. Supramolecular structure of the rigid layer of the cell wall of Salmonella, Serratia, Proteus, and Pseudomonas fluorescens. Number of lipoprotein molecules in a membrane layer. Biochemistry. 1970 Dec 22;9(26):5041–5049. doi: 10.1021/bi00828a001. [DOI] [PubMed] [Google Scholar]
  3. Inouye M., Shaw J., Shen C. The assembly of a structural lipoprotein in the envelope of Escherichia coli. J Biol Chem. 1972 Dec 25;247(24):8154–8159. [PubMed] [Google Scholar]
  4. James R. Identification of an outer membrane protein of Escherichia coli, with a role in the coordination of deoxyribonucleic acid replication and cell elongation. J Bacteriol. 1975 Nov;124(2):918–929. doi: 10.1128/jb.124.2.918-929.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Neville D. M., Jr Molecular weight determination of protein-dodecyl sulfate complexes by gel electrophoresis in a discontinuous buffer system. J Biol Chem. 1971 Oct 25;246(20):6328–6334. [PubMed] [Google Scholar]
  6. Normark S., Boman H. G., Bloom G. D. Cell division in a chain-forming envA mutant of Escherichia coli K12. Fine structure of division sites and effects of EDTA, lysozyme and ampicillin. Acta Pathol Microbiol Scand B Microbiol Immunol. 1971;79(5):651–664. doi: 10.1111/j.1699-0463.1971.tb00093.x. [DOI] [PubMed] [Google Scholar]
  7. Normark S. Genetics of a chain-forming mutant of Escherichia coli. Transduction and dominance of the envA gene mediating increased penetration to some antibacterial agents. Genet Res. 1970 Aug;16(1):63–78. doi: 10.1017/s0016672300002287. [DOI] [PubMed] [Google Scholar]
  8. ROTHFIELD L., OSBORN M. J., HORECKER B. L. BIOSYNTHESIS OF BACTERIAL LIPOPOLYSACCHARIDE. II. INCORPORATION OF GLUCOSE AND GALACTOSE CATALYZED BY PARTICULATE AND SOLUBLE ENZYMES IN SALMONELLA. J Biol Chem. 1964 Sep;239:2788–2795. [PubMed] [Google Scholar]
  9. Weigand R. A., Rothfield L. I. Genetic and physiological classification of periplasmic-leaky mutants of Salmonella typhimurium. J Bacteriol. 1976 Jan;125(1):340–345. doi: 10.1128/jb.125.1.340-345.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]

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