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. 1981 Jun;146(3):1083–1090. doi: 10.1128/jb.146.3.1083-1090.1981

Cell wall proteins of Aquaspirillum serpens.

S F Koval, R G Murray
PMCID: PMC216964  PMID: 6787011

Abstract

The Triton X-100-insoluble wall fraction of Aquaspirillum serpens VHA contained three major proteins: the regularly structured (RS) superficial protein (molecular weight 140,000) and two peptidoglycan-associated proteins (molecular weights, 32,000 and 33,000). The molecular arrangement and interactions of the outer membrane and RS proteins were examined with the use of bifunctional cross-linking reagents. The peptidoglycan-associated and RS proteins were not readily cross-linked in either homo- or heteropolymers. This suggests that the free amino groups are not suitably disposed for cross-linking. Some high-molecular-weight multimers of the RS protein were produced, but the subunit structure of the RS array was not stabilized by cross-linking. The peptidoglycan-associated proteins were cross-linked to high-molecular-weight multimers, but no dimers or trimers were produced. This result suggests that these proteins exist in the outer membrane as multimers larger than trimers.

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Selected References

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

  1. Beveridge T. J., Murray R. G. Surface arrays on the cell wall of Spirillum metamorphum. J Bacteriol. 1975 Dec;124(3):1529–1544. doi: 10.1128/jb.124.3.1529-1544.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Buckmire F. L., Murray R. G. Studies on the cell wall of Spirillum serpens. 1. Isolation and partial purification of the outermost cell wall layer. Can J Microbiol. 1970 Oct;16(10):1011–1022. doi: 10.1139/m70-171. [DOI] [PubMed] [Google Scholar]
  3. Buckmire F. L., Murray R. G. Studies on the cell wall of Spirillum serpens. II. Chemical characterization of the outer structured layer. Can J Microbiol. 1973 Jan;19(1):59–66. doi: 10.1139/m73-009. [DOI] [PubMed] [Google Scholar]
  4. Buckmire F. L., Murray R. G. Substructure and in vitro assembly of the outer, structured layer of Spirillum serpens. J Bacteriol. 1976 Jan;125(1):290–299. doi: 10.1128/jb.125.1.290-299.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Chester I. R., Murray R. G. Analysis of the cell wall and lipopolysaccharide of Spirillum serpens. J Bacteriol. 1975 Dec;124(3):1168–1176. doi: 10.1128/jb.124.3.1168-1176.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Chester I. R., Murray R. G. Protein-lipid-lipopolysaccharide association in the superficial layer of Spirillum serpens cell walls. J Bacteriol. 1978 Feb;133(2):932–941. doi: 10.1128/jb.133.2.932-941.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Coulton J. W., Murray R. G. Membrane-associated components of the bacterial flagellar apparatus. Biochim Biophys Acta. 1977 Mar 1;465(2):290–310. doi: 10.1016/0005-2736(77)90080-3. [DOI] [PubMed] [Google Scholar]
  8. DiRienzo J. M., Nakamura K., Inouye M. The outer membrane proteins of Gram-negative bacteria: biosynthesis, assembly, and functions. Annu Rev Biochem. 1978;47:481–532. doi: 10.1146/annurev.bi.47.070178.002405. [DOI] [PubMed] [Google Scholar]
  9. Endermann R., Henning U. Nearest neighbors of major proteins in the outer membrane of Escherichia coli K12. FEBS Lett. 1979 Jan 15;97(2):339–342. doi: 10.1016/0014-5793(79)80117-9. [DOI] [PubMed] [Google Scholar]
  10. Glaeser R. M., Chiu W., Grano D. Structure of the surface layer protein of the outer membrane of Spirillum serpens. J Ultrastruct Res. 1979 Mar;66(3):235–242. doi: 10.1016/s0022-5320(79)90121-7. [DOI] [PubMed] [Google Scholar]
  11. Hancock R. E., Nikaido H. Outer membranes of gram-negative bacteria. XIX. Isolation from Pseudomonas aeruginosa PAO1 and use in reconstitution and definition of the permeability barrier. J Bacteriol. 1978 Oct;136(1):381–390. doi: 10.1128/jb.136.1.381-390.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Helenius A., Simons K. Solubilization of membranes by detergents. Biochim Biophys Acta. 1975 Mar 25;415(1):29–79. doi: 10.1016/0304-4157(75)90016-7. [DOI] [PubMed] [Google Scholar]
  13. Hess H. H., Lees M. B., Derr J. E. A linear Lowry--Folin assay for both water-soluble and sodium dodecyl sulfate-solubilized proteins. Anal Biochem. 1978 Mar;85(1):295–300. doi: 10.1016/0003-2697(78)90304-4. [DOI] [PubMed] [Google Scholar]
  14. Hofstra H., Dankert J. Antigenic cross-reactivity of major outer membrane proteins in enterobacteriaceae species. J Gen Microbiol. 1979 Apr;111(2):293–302. doi: 10.1099/00221287-111-2-293. [DOI] [PubMed] [Google Scholar]
  15. 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]
  16. Lugtenberg B., Bronstein H., van Selm N., Peters R. Peptidoglycan-associated outer membrane proteins in gammegatine bacteria. Biochim Biophys Acta. 1977 Mar 17;465(3):571–578. doi: 10.1016/0005-2736(77)90274-7. [DOI] [PubMed] [Google Scholar]
  17. Martin H. H., Heilmann H. D., Preusser H. J. State of the rigid-layer in celll walls of some gram-negative Bacteria. Arch Mikrobiol. 1972;83(4):332–346. doi: 10.1007/BF00425246. [DOI] [PubMed] [Google Scholar]
  18. Palva E. T. Protein interactions in the outer membrane of Escherichia coli. Eur J Biochem. 1979 Feb 1;93(3):495–503. doi: 10.1111/j.1432-1033.1979.tb12848.x. [DOI] [PubMed] [Google Scholar]
  19. Palva E. T., Randall L. L. Arrangement of protein I in Escherichia coli outer membrane: cross-linking study. J Bacteriol. 1978 Jan;133(1):279–286. doi: 10.1128/jb.133.1.279-286.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Reithmeier R. A., Bragg P. D. Cross-linking of the proteins in the outer membrane of Escherichia coli. Biochim Biophys Acta. 1977 Apr 18;466(2):245–256. doi: 10.1016/0005-2736(77)90222-x. [DOI] [PubMed] [Google Scholar]
  21. 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]
  22. Schweizer M., Sonntag I., Henning U. Outer cell envelope membrane and shape of Spirillum serpens. J Mol Biol. 1975 Mar 25;93(1):11–21. doi: 10.1016/0022-2836(75)90356-3. [DOI] [PubMed] [Google Scholar]
  23. Sleytr U. B. Regular arrays of macromolecules on bacterial cell walls: structure, chemistry, assembly, and function. Int Rev Cytol. 1978;53:1–62. doi: 10.1016/s0074-7696(08)62240-8. [DOI] [PubMed] [Google Scholar]
  24. Steven A. C., Heggeler B., Müller R., Kistler J., Rosenbusch J. P. Ultrastructure of a periodic protein layer in the outer membrane of Escherichia coli. J Cell Biol. 1977 Feb;72(2):292–301. doi: 10.1083/jcb.72.2.292. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Stewart M., Beveridge T. J., Murray R. G. Structure of the regular surface layer of Spirillum putridiconchylium. J Mol Biol. 1980 Feb 15;137(1):1–8. doi: 10.1016/0022-2836(80)90153-9. [DOI] [PubMed] [Google Scholar]

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