Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1991 Jun;173(11):3334–3341. doi: 10.1128/jb.173.11.3334-3341.1991

Analysis of Myxococcus xanthus cell types by two-dimensional polyacrylamide gel electrophoresis.

K A O'Connor 1, D R Zusman 1
PMCID: PMC207944  PMID: 1904431

Abstract

Myxococcus xanthus is a gram-negative, soil-dwelling bacterium that undergoes development in response to depletion of nutrients. Whereas most cells aggregate into multicellular mounds in which they differentiate into spores, 10 to 20% of the developing cells remain outside fruiting bodies as peripheral rods. We used two-dimensional polyacrylamide gel electrophoresis to analyze the global expression of polypeptides in cells taken from six stages in the life cycle: vegetatively growing cells, cells 15 h after the induction of development, peripheral rods, prespores (sonication-sensitive, aggregated cells), fruiting-body spores (sonication-resistant, aggregated cells) 96 h after the induction of development, and glycerol-induced spores 15 h after induction. Seven hundred sixty-one discrete sample spots (SSPs) were identified among the six gels. Comparisons among the samples revealed that each sample had some unique SSPs, ranging from 0.3% of the 15-h developing cell SSPs to 17.9% of 96-h peripheral rod SSPs. Sixty-eight SSPs were ubiquitously distributed, but the relative amounts of these SSPs varied among the samples. Statistical analyses of the distribution and relative quantities of the SSPs indicate that, within a confidence level of greater than 99.99%, peripheral rods are significantly different from vegetatively growing cells, 15-h developing cells, prespores, fruiting-body spores, and glycerol-induced spores. In fact, among the six samples studied, only 15-h developing cells and glycerol-induced spores were similar to each other within a confidence level of P greater than or equal to 0.05. These results are consistent with the description of peripheral rods as a distinct developmental cell type.

Full text

PDF
3334

Images in this article

3336Image
on p.3336
3337Image
on p.3337
3337Image
on p.3337

Selected References

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

  1. Campos J. M., Zusman D. R. Regulation of development in Myxococcus xanthus: effect of 3':5'-cyclic AMP, ADP, and nutrition. Proc Natl Acad Sci U S A. 1975 Feb;72(2):518–522. doi: 10.1073/pnas.72.2.518. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Cumsky M., Zusman D. R. Myxobacterial hemagglutinin: a development-specific lectin of Myxococcus xanthus. Proc Natl Acad Sci U S A. 1979 Nov;76(11):5505–5509. doi: 10.1073/pnas.76.11.5505. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. DWORKIN M., GIBSON S. M. A SYSTEM FOR STUDYING MICROBIAL MORPHOGENESIS: RAPID FORMATION OF MICROCYSTS IN MYXOCOCCUS XANTHUS. Science. 1964 Oct 9;146(3641):243–244. doi: 10.1126/science.146.3641.243. [DOI] [PubMed] [Google Scholar]
  4. DWORKIN M. Nutritional requirements for vegetative growth of Myxococcus xanthus. J Bacteriol. 1962 Aug;84:250–257. doi: 10.1128/jb.84.2.250-257.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Groat R. G., Schultz J. E., Zychlinsky E., Bockman A., Matin A. Starvation proteins in Escherichia coli: kinetics of synthesis and role in starvation survival. J Bacteriol. 1986 Nov;168(2):486–493. doi: 10.1128/jb.168.2.486-493.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hagen D. C., Bretscher A. P., Kaiser D. Synergism between morphogenetic mutants of Myxococcus xanthus. Dev Biol. 1978 Jun;64(2):284–296. doi: 10.1016/0012-1606(78)90079-9. [DOI] [PubMed] [Google Scholar]
  7. Inouye M., Inouye S., Zusman D. R. Biosynthesis and self-assembly of protein S, a development-specific protein of Myxococcus xanthus. Proc Natl Acad Sci U S A. 1979 Jan;76(1):209–213. doi: 10.1073/pnas.76.1.209. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Inouye M., Inouye S., Zusman D. R. Gene expression during development of Myxococcus xanthus: pattern of protein synthesis. Dev Biol. 1979 Feb;68(2):579–591. doi: 10.1016/0012-1606(79)90228-8. [DOI] [PubMed] [Google Scholar]
  9. Jenkins D. E., Chaisson S. A., Matin A. Starvation-induced cross protection against osmotic challenge in Escherichia coli. J Bacteriol. 1990 May;172(5):2779–2781. doi: 10.1128/jb.172.5.2779-2781.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Jenkins D. E., Schultz J. E., Matin A. Starvation-induced cross protection against heat or H2O2 challenge in Escherichia coli. J Bacteriol. 1988 Sep;170(9):3910–3914. doi: 10.1128/jb.170.9.3910-3914.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. 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]
  12. 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]
  13. Losick R., Youngman P., Piggot P. J. Genetics of endospore formation in Bacillus subtilis. Annu Rev Genet. 1986;20:625–669. doi: 10.1146/annurev.ge.20.120186.003205. [DOI] [PubMed] [Google Scholar]
  14. McCleary W. R., Esmon B., Zusman D. R. Myxococcus xanthus protein C is a major spore surface protein. J Bacteriol. 1991 Mar;173(6):2141–2145. doi: 10.1128/jb.173.6.2141-2145.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Milhausen M., Agabian N. Regulation of polypeptide synthesis during Caulobacter development: two-dimensional gel analysis. J Bacteriol. 1981 Oct;148(1):163–173. doi: 10.1128/jb.148.1.163-173.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. O'Connor K. A., Zusman D. R. Behavior of peripheral rods and their role in the life cycle of Myxococcus xanthus. J Bacteriol. 1991 Jun;173(11):3342–3355. doi: 10.1128/jb.173.11.3342-3355.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. O'Connor K. A., Zusman D. R. Development in Myxococcus xanthus involves differentiation into two cell types, peripheral rods and spores. J Bacteriol. 1991 Jun;173(11):3318–3333. doi: 10.1128/jb.173.11.3318-3333.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. O'Connor K. A., Zusman D. R. Reexamination of the role of autolysis in the development of Myxococcus xanthus. J Bacteriol. 1988 Sep;170(9):4103–4112. doi: 10.1128/jb.170.9.4103-4112.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Reeve C. A., Bockman A. T., Matin A. Role of protein degradation in the survival of carbon-starved Escherichia coli and Salmonella typhimurium. J Bacteriol. 1984 Mar;157(3):758–763. doi: 10.1128/jb.157.3.758-763.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Shimkets L. J. Social and developmental biology of the myxobacteria. Microbiol Rev. 1990 Dec;54(4):473–501. doi: 10.1128/mr.54.4.473-501.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Spector M. P., Aliabadi Z., Gonzalez T., Foster J. W. Global control in Salmonella typhimurium: two-dimensional electrophoretic analysis of starvation-, anaerobiosis-, and heat shock-inducible proteins. J Bacteriol. 1986 Oct;168(1):420–424. doi: 10.1128/jb.168.1.420-424.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Spector M. P., Park Y. K., Tirgari S., Gonzalez T., Foster J. W. Identification and characterization of starvation-regulated genetic loci in Salmonella typhimurium by using Mu d-directed lacZ operon fusions. J Bacteriol. 1988 Jan;170(1):345–351. doi: 10.1128/jb.170.1.345-351.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Wireman J. W., Dworkin M. Morphogenesis and developmental interactions in myxobacteria. Science. 1975 Aug 15;189(4202):516–523. doi: 10.1126/science.806967. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES