1887

Abstract

Rhapidosomes are tubular microstructures composed of proteins that are found in a variety of bacteria and algae. These structures, which are resistant to disruption by many denaturing agents, have potential application as a biomaterial and may serve as a new model for the study of self assembly. When rhapidosomes were purified and analysed by SDS-PAGE the presence of three proteins with molecular masses of 53, 29 and 18 kDa was revealed. However, lysozyme treatment of the rhapidosome preparations containing the three proteins resulted in the selective release of the 18 kDa protein from the rhapidosome complex. N-Terminal sequence analysis and amino acid composition analysis were performed on all three proteins. The amino acid composition of the 18 kDa protein closely matched the amino acid composition of protein H (a peptidoglycan-associated protein from ). These results suggest that the 18 kDa protein may be a contaminating peptidoglycan-associated protein and not part of the rhapidosome structure. Western blot analysis using antisera raised against rhapidosomes revealed that the 53 kDa component protein does not react with the antisera. We speculate that the 53 kDa protein may form the inner core of the rhapidosomes, whilst the 29 kDa protein forms the outer sheath of these structures.

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/content/journal/micro/10.1099/00221287-139-4-859
1993-04-01
2024-04-19
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References

  1. Chang H. Y., Allen M. M. 1974; The isolation of rhapidosomes from the blue-green alga,Spirulina. Journal of General Microbiology 18:121–130
    [Google Scholar]
  2. Correll D. L., Lewin R. A. 1964; Rod shaped ribonucleoprotein particles from Saprospira. Canadian Journal of Microbiology 10:63–74
    [Google Scholar]
  3. Delk A. S., Dekker C. A. 1972; Characterization of rhapidosomes from Saprospira grandis. Journal of Molecular Biology 64:287–295
    [Google Scholar]
  4. Evers M, Murray R. 1980; The comparison of rhapidosomes and defective bacteriophage particles from Aquaspirillum itersonii. Canadian Journal of Microbiology 26:1312–1319
    [Google Scholar]
  5. Faraldo M. L. M., Pedro M. A., Berenguer J. 1991; Cloning and expression in Escherichia coliof the structural gene coding for the monomeric protein of the S layer ofThermus thermophilusHB8. Journal of Bacteriology 173:5346–5351
    [Google Scholar]
  6. Hylemon P. B., Wells J. S. JR Krieg N. R., Jannasch H. W. 1973; The genusSpirillum: a taxonomic study. International Journal of Systematic Bacteriology 23:340–380
    [Google Scholar]
  7. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature; London: 227680–685
    [Google Scholar]
  8. Matsudaira P. 1987; Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. Journal of Biological Chemistry 262:10035–10038
    [Google Scholar]
  9. Mizuno T. 1987; A novel peptidoglycan-associated lipoprotein found in the cell envelope ofPseudomonas aeruginosaandEscherichia coli. Journal of Biochemistry 86:991–1000
    [Google Scholar]
  10. Mizuno T, Kageyama M. 1979; Isolation and characterization of major outer membrane proteins of Pseudomonas aeruginosa strain PAO with special reference to peptidoglycan associated protein. Journal of Biochemistry 86:979–989
    [Google Scholar]
  11. Parge H. E., Bernstein S. L., Deal C. D., Mcree D. E., Christensen D, Capozza M. A., Kays B. W., Fieser T. M., Draper D, So M, Getzoff E. D., Tainer J. A. 1990; Biochemical purification and crystallographic characterization of the fiber-forming protein pilin fromNeisseria gonorrhoeae. Journal of Biological Chemistry 265:2278–2285
    [Google Scholar]
  12. Pazirandeh M, Baral S, Campbell J. 1992; Metallized nanotubules derived from bacteria. Biomimetics 1:39–48
    [Google Scholar]
  13. Rosenbusch J. P. 1974; Characterization of the major envelope protein from Escherichia coli. Journal of Biological Chemistry 149:8019–8029
    [Google Scholar]
  14. Towbin H, Staehelin T, Gordon J. 1979; Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proceedings of the National Academy of Sciences of the United States of America 74:4350–4354
    [Google Scholar]
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