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. 1978 Oct;75(10):4962–4966. doi: 10.1073/pnas.75.10.4962

Identification of tubulin from the yeast Saccharomyces cerevisiae.

P Baum, J Thorner, L Honig
PMCID: PMC336242  PMID: 368805

Abstract

A tubulin-like protein was identified in the lower eukaryote Saccharomyces cerevisiae. The following criteria were used: (i) copolymerization of the 35S-labeled yeast protein with porcine brain tubulin; (ii) immunoprecipitation of the 35S-labeled yeast protein with antiflagellar tubulin antibody; (iii) the presence of the yeast protein as a constituent of isolated yeast nuclei; and (iv) splitting of the yeast protein in a gel electrophoretic system containing sodium dodecyl sulfate that resolved the alpha- and beta-tubulin chains from other sources. This protein did not appear to have significant affinity for the plant alkaloid, Colcemid.

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Selected References

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  1. Bisson L., Thorner J. Thymidine 5'-monophosphate-requiring mutants of Saccharomyces cerevisiae are deficient in thymidylate synthetase. J Bacteriol. 1977 Oct;132(1):44–50. doi: 10.1128/jb.132.1.44-50.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Burns R. G. 3H-colcicine binding. Failure to detect any binding to soluble proteins from various lower organisms. Exp Cell Res. 1973 Oct;81(2):285–292. doi: 10.1016/0014-4827(73)90517-x. [DOI] [PubMed] [Google Scholar]
  3. Byers B., Goetsch L. Behavior of spindles and spindle plaques in the cell cycle and conjugation of Saccharomyces cerevisiae. J Bacteriol. 1975 Oct;124(1):511–523. doi: 10.1128/jb.124.1.511-523.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Davidse L. C., Flach W. Differential binding of methyl benzimidazol-2-yl carbamate to fungal tubulin as a mechanism of resistance to this antimitotic agent in mutant strains of Aspergillus nidulans. J Cell Biol. 1977 Jan;72(1):174–193. doi: 10.1083/jcb.72.1.174. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Eipper B. A. Rat brain microtubule protein: purification and determination of covalently bound phosphate and carbohydrate. Proc Natl Acad Sci U S A. 1972 Aug;69(8):2283–2287. doi: 10.1073/pnas.69.8.2283. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Flanagan D., Warr J. R. Colchicine binding of a high-speed supernatant of Chlamydomonas reinhardi. FEBS Lett. 1977 Aug 1;80(1):14–18. doi: 10.1016/0014-5793(77)80396-7. [DOI] [PubMed] [Google Scholar]
  7. Haber J. E., Peloquin J. G., Halvorson H. O., Borisy G. G. Colcemid inhibition of cell growth and the characterization of a colcemid-binding activity in Saccharomyces cerevisiae. J Cell Biol. 1972 Nov;55(2):355–367. doi: 10.1083/jcb.55.2.355. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. 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]
  10. Ludueńa R. F., Shooter E. M., Wilson L. Structure of the tubulin dimer. J Biol Chem. 1977 Oct 25;252(20):7006–7014. [PubMed] [Google Scholar]
  11. Mitchison J. M., Carter B. L. Cell cycle analysis. Methods Cell Biol. 1975;11:201–219. [PubMed] [Google Scholar]
  12. Mortimer R. K., Hawthorne D. C. Genetic mapping in yeast. Methods Cell Biol. 1975;11:221–233. doi: 10.1016/s0091-679x(08)60325-8. [DOI] [PubMed] [Google Scholar]
  13. Olmsted J. B., Borisy G. G. Microtubules. Annu Rev Biochem. 1973;42:507–540. doi: 10.1146/annurev.bi.42.070173.002451. [DOI] [PubMed] [Google Scholar]
  14. Peterson J. B., Ris H. Electron-microscopic study of the spindle and chromosome movement in the yeast Saccharomyces cerevisiae. J Cell Sci. 1976 Nov;22(2):219–242. doi: 10.1242/jcs.22.2.219. [DOI] [PubMed] [Google Scholar]
  15. Piperno G., Luck D. J. Microtubular proteins of Chlamydomonas reinhardtii. An immunochemical study based on the use of an antibody specific for the beta-tubulin subunit. J Biol Chem. 1977 Jan 10;252(1):383–391. [PubMed] [Google Scholar]
  16. Sheir-Neiss G., Nardi R. V., Gealt M. A., Morris N. R. Tubulin-like protein from Aspergillus nidulans. Biochem Biophys Res Commun. 1976 Mar 22;69(2):285–290. doi: 10.1016/0006-291x(76)90519-2. [DOI] [PubMed] [Google Scholar]
  17. Snyder J. A., McIntosh J. R. Biochemistry and physiology of microtubules. Annu Rev Biochem. 1976;45:699–720. doi: 10.1146/annurev.bi.45.070176.003411. [DOI] [PubMed] [Google Scholar]
  18. Stadler J., Franke W. W. Characterization of the colchicine binding of membrane fractions from rat and mouse liver. J Cell Biol. 1974 Jan;60(1):297–303. doi: 10.1083/jcb.60.1.297. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Water R. D., Kleinsmith L. J. Identification of alpha and beta tubulin in yeast. Biochem Biophys Res Commun. 1976 Jun 7;70(3):704–708. doi: 10.1016/0006-291x(76)90649-5. [DOI] [PubMed] [Google Scholar]
  20. Weber K., Wehland J., Herzog W. Griseofulvin interacts with microtubules both in vivo and in vitro. J Mol Biol. 1976 Apr 25;102(4):817–829. doi: 10.1016/0022-2836(76)90293-x. [DOI] [PubMed] [Google Scholar]
  21. Weingarten M. D., Suter M. M., Littman D. R., Kirschner M. W. Properties of the depolymerization products of microtubules from mammalian brain. Biochemistry. 1974 Dec 31;13(27):5529–5537. doi: 10.1021/bi00724a012. [DOI] [PubMed] [Google Scholar]
  22. Wiche G., Cole R. D. An improved preparation of highly specific tublin antibodies. Exp Cell Res. 1976 Apr;99(1):15–22. doi: 10.1016/0014-4827(76)90674-1. [DOI] [PubMed] [Google Scholar]
  23. Wilson L., Bamburg J. R., Mizel S. B., Grisham L. M., Creswell K. M. Interaction of drugs with microtubule proteins. Fed Proc. 1974 Feb;33(2):158–166. [PubMed] [Google Scholar]
  24. Wintersberger U., Smith P., Letnansky K. Yeast chromatin. Preparation from isolated nuclei, histone composition and transcription capacity. Eur J Biochem. 1973 Feb 15;33(1):123–130. doi: 10.1111/j.1432-1033.1973.tb02663.x. [DOI] [PubMed] [Google Scholar]

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