Skip to main content
Molecular and Cellular Biology logoLink to Molecular and Cellular Biology
. 1984 Sep;4(9):1706–1711. doi: 10.1128/mcb.4.9.1706

Tubulin proteins and RNA during the myxamoeba-flagellate transformation of Physarum polycephalum.

L L Green, W F Dove
PMCID: PMC368976  PMID: 6208478

Abstract

Physarum myxamoebae can be reversibly induced to become flagellates. Physarum flagellates contain a new form of tubulin, alpha 3, that is not found in nonflagellated cells. Evidence is presented that suggests that alpha 3 tubulin arises through posttranslational modification of a preexisting alpha tubulin. Pulse-chase experiments showed that labeled alpha 3 tubulin could be detected when flagellates formed after a chase. RNA was isolated from myxamoebae at different times after induction of flagellum formation. When this RNA was translated in vitro, the resulting products contained no alpha 3 tubulin, also consistent with alpha 3 being made by posttranslational modification. Levels of alpha and beta tubulin RNA increased with the proportion of flagellates in the culture. These elevated tubulin RNA levels declined after the number of flagellates in the population achieved plateau values.

Full text

PDF
1706

Images in this article

Selected References

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

  1. Aldrich H. C. The development of flagella in swarm cells of the myxomycete Physarum flavicomum. J Gen Microbiol. 1968 Feb;50(2):217–222. doi: 10.1099/00221287-50-2-217. [DOI] [PubMed] [Google Scholar]
  2. Burland T. G., Gull K., Schedl T., Boston R. S., Dove W. F. Cell type-dependent expression of tubulins in Physarum. J Cell Biol. 1983 Dec;97(6):1852–1859. doi: 10.1083/jcb.97.6.1852. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cooke D. J., Dee J. Methods for the isolation and analysis of plasmodial mutants in Physarum polycephalum. Genet Res. 1974 Oct;24(2):175–187. doi: 10.1017/s0016672300015202. [DOI] [PubMed] [Google Scholar]
  4. Fyrberg E. A., Kindle K. L., Davidson N., Kindle K. L. The actin genes of Drosophila: a dispersed multigene family. Cell. 1980 Feb;19(2):365–378. doi: 10.1016/0092-8674(80)90511-5. [DOI] [PubMed] [Google Scholar]
  5. Guttman S. D., Gorovsky M. A. Cilia regeneration in starved tetrahymena: an inducible system for studying gene expression and organelle biogenesis. Cell. 1979 Jun;17(2):307–317. doi: 10.1016/0092-8674(79)90156-9. [DOI] [PubMed] [Google Scholar]
  6. L'Hernault S. W., Rosenbaum J. L. Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly. J Cell Biol. 1983 Jul;97(1):258–263. doi: 10.1083/jcb.97.1.258. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Lai E. Y., Walsh C., Wardell D., Fulton C. Programmed appearance of translatable flagellar tubulin mRNA during cell differentiation in Naegleria. Cell. 1979 Aug;17(4):867–878. doi: 10.1016/0092-8674(79)90327-1. [DOI] [PubMed] [Google Scholar]
  8. Marcaud L., Hayes D. RNA synthesis in starved deciliated Tetrahymena pyriformis. Eur J Biochem. 1979 Jul;98(1):267–273. doi: 10.1111/j.1432-1033.1979.tb13185.x. [DOI] [PubMed] [Google Scholar]
  9. McKeithan T. W., Lefebvre P. A., Silflow C. D., Rosenbaum J. L. Multiple forms of tubulin in Polytomella and Chlamydomonas: evidence for a precursor of flagellar alpha-tubulin. J Cell Biol. 1983 Apr;96(4):1056–1063. doi: 10.1083/jcb.96.4.1056. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Merlino G. T., Chamberlain J. P., Kleinsmith L. J. Effects of deciliation of tubulin messenger RNA activity in sea urchin embryos. J Biol Chem. 1978 Oct 10;253(19):7078–7085. [PubMed] [Google Scholar]
  11. Minami S. A., Collis P. S., Young E. E., Weeks D. P. Tubulin induction in C. reinhardii: requirement for tubulin mRNA synthesis. Cell. 1981 Apr;24(1):89–95. doi: 10.1016/0092-8674(81)90504-3. [DOI] [PubMed] [Google Scholar]
  12. Rigby P. W., Dieckmann M., Rhodes C., Berg P. Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I. J Mol Biol. 1977 Jun 15;113(1):237–251. doi: 10.1016/0022-2836(77)90052-3. [DOI] [PubMed] [Google Scholar]
  13. Roberts B. E., Paterson B. M. Efficient translation of tobacco mosaic virus RNA and rabbit globin 9S RNA in a cell-free system from commercial wheat germ. Proc Natl Acad Sci U S A. 1973 Aug;70(8):2330–2334. doi: 10.1073/pnas.70.8.2330. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Rosenbaum J. L., Moulder J. E., Ringo D. L. Flagellar elongation and shortening in Chlamydomonas. The use of cycloheximide and colchicine to study the synthesis and assembly of flagellar proteins. J Cell Biol. 1969 May;41(2):600–619. doi: 10.1083/jcb.41.2.600. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Russell D. G., Miller D., Gull K. Tubulin heterogeneity in the trypanosome Crithidia fasciculata. Mol Cell Biol. 1984 Apr;4(4):779–790. doi: 10.1128/mcb.4.4.779. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Schedl T., Burland T. G., Gull K., Dove W. F. Cell cycle regulation of tubulin RNA level, tubulin protein synthesis, and assembly of microtubules in Physarum. J Cell Biol. 1984 Jul;99(1 Pt 1):155–165. doi: 10.1083/jcb.99.1.155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Schloss J. A., Silflow C. D., Rosenbaum J. L. mRNA abundance changes during flagellar regeneration in Chlamydomonas reinhardtii. Mol Cell Biol. 1984 Mar;4(3):424–434. doi: 10.1128/mcb.4.3.424. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Schmitt J. J., Cohen B. N. Quantitative isolation of DNA restriction fragments from low-melting agarose by Elutip-d affinity chromatography. Anal Biochem. 1983 Sep;133(2):462–464. doi: 10.1016/0003-2697(83)90109-4. [DOI] [PubMed] [Google Scholar]
  19. Sussman D. J., Lai E. Y., Fulton C. Rapid disappearance of translatable actin mRNA during cell differentiation in Naegleria. J Biol Chem. 1984 Jun 10;259(11):7355–7360. [PubMed] [Google Scholar]
  20. Valenzuela P., Quiroga M., Zaldivar J., Rutter W. J., Kirschner M. W., Cleveland D. W. Nucleotide and corresponding amino acid sequences encoded by alpha and beta tubulin mRNAs. Nature. 1981 Feb 19;289(5799):650–655. doi: 10.1038/289650a0. [DOI] [PubMed] [Google Scholar]

Articles from Molecular and Cellular Biology are provided here courtesy of Taylor & Francis

RESOURCES