Skip to main content
Molecular and Cellular Biology logoLink to Molecular and Cellular Biology
. 1988 Dec;8(12):5108–5115. doi: 10.1128/mcb.8.12.5108

The intron-containing gene for yeast profilin (PFY) encodes a vital function.

V Magdolen 1, U Oechsner 1, G Müller 1, W Bandlow 1
PMCID: PMC365612  PMID: 3072473

Abstract

The gene coding for profilin (PFY), an actin-binding protein, occurs as a single copy in the haploid genome of Saccharomyces cerevisiae and is required for spore germination and cell viability. Displacement of one gene copy in a diploid cell by a nonfunctional allele is recessively lethal: tetrad analysis yields only two viable spores per ascus. The PFY gene maps on chromosome XV and is linked to the ADE2 marker. The primary transcript of about 1,000 bases contains an intron of 209 bases and is spliced into a messenger of about 750 bases. The intron was identified by comparison with a cDNA clone, which also revealed the 3' end of the transcript. The 5' end of the mRNA was mapped by primer elongation. The gene is transcribed constitutively and has a coding capacity for a protein of 126 amino acids. The deduced molecular weight of

Full text

PDF

Images in this article

Selected References

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

  1. Ampe C., Markey F., Lindberg U., Vandekerckhove J. The primary structure of human platelet profilin: reinvestigation of the calf spleen profilin sequence. FEBS Lett. 1988 Feb 8;228(1):17–21. doi: 10.1016/0014-5793(88)80575-1. [DOI] [PubMed] [Google Scholar]
  2. Ampe C., Sato M., Pollard T. D., Vandekerckhove J. The primary structure of the basic isoform of Acanthamoeba profilin. Eur J Biochem. 1988 Jan 4;170(3):597–601. doi: 10.1111/j.1432-1033.1988.tb13739.x. [DOI] [PubMed] [Google Scholar]
  3. Ampe C., Vandekerckhove J., Brenner S. L., Tobacman L., Korn E. D. The amino acid sequence of Acanthamoeba profilin. J Biol Chem. 1985 Jan 25;260(2):834–840. [PubMed] [Google Scholar]
  4. Ampe C., Vandekerckhove J. The F-actin capping proteins of Physarum polycephalum: cap42(a) is very similar, if not identical, to fragmin and is structurally and functionally very homologous to gelsolin; cap42(b) is Physarum actin. EMBO J. 1987 Dec 20;6(13):4149–4157. doi: 10.1002/j.1460-2075.1987.tb02761.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bennetzen J. L., Hall B. D. Codon selection in yeast. J Biol Chem. 1982 Mar 25;257(6):3026–3031. [PubMed] [Google Scholar]
  6. Chen E. Y., Seeburg P. H. Supercoil sequencing: a fast and simple method for sequencing plasmid DNA. DNA. 1985 Apr;4(2):165–170. doi: 10.1089/dna.1985.4.165. [DOI] [PubMed] [Google Scholar]
  7. Freier S. M., Kierzek R., Jaeger J. A., Sugimoto N., Caruthers M. H., Neilson T., Turner D. H. Improved free-energy parameters for predictions of RNA duplex stability. Proc Natl Acad Sci U S A. 1986 Dec;83(24):9373–9377. doi: 10.1073/pnas.83.24.9373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gallwitz D., Sures I. Structure of a split yeast gene: complete nucleotide sequence of the actin gene in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1980 May;77(5):2546–2550. doi: 10.1073/pnas.77.5.2546. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Greer C., Schekman R. Calcium control of Saccharomyces cerevisiae actin assembly. Mol Cell Biol. 1982 Oct;2(10):1279–1286. doi: 10.1128/mcb.2.10.1279. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Henikoff S., Kelly J. D., Cohen E. H. Transcription terminates in yeast distal to a control sequence. Cell. 1983 Jun;33(2):607–614. doi: 10.1016/0092-8674(83)90441-5. [DOI] [PubMed] [Google Scholar]
  11. Huffaker T. C., Hoyt M. A., Botstein D. Genetic analysis of the yeast cytoskeleton. Annu Rev Genet. 1987;21:259–284. doi: 10.1146/annurev.ge.21.120187.001355. [DOI] [PubMed] [Google Scholar]
  12. Isenberg G., Aebi U., Pollard T. D. An actin-binding protein from Acanthamoeba regulates actin filament polymerization and interactions. Nature. 1980 Dec 4;288(5790):455–459. doi: 10.1038/288455a0. [DOI] [PubMed] [Google Scholar]
  13. Kilmartin J. V., Adams A. E. Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces. J Cell Biol. 1984 Mar;98(3):922–933. doi: 10.1083/jcb.98.3.922. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Korn E. D. Actin polymerization and its regulation by proteins from nonmuscle cells. Physiol Rev. 1982 Apr;62(2):672–737. doi: 10.1152/physrev.1982.62.2.672. [DOI] [PubMed] [Google Scholar]
  15. Lassing I., Lindberg U. Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin. Nature. 1985 Apr 4;314(6010):472–474. doi: 10.1038/314472a0. [DOI] [PubMed] [Google Scholar]
  16. Lustig A. J., Lin R. J., Abelson J. The yeast RNA gene products are essential for mRNA splicing in vitro. Cell. 1986 Dec 26;47(6):953–963. doi: 10.1016/0092-8674(86)90810-x. [DOI] [PubMed] [Google Scholar]
  17. Magdolen V., Oechsner U., Bandlow W. The complete nucleotide sequence of the gene coding for yeast adenylate kinase. Curr Genet. 1987;12(6):405–411. doi: 10.1007/BF00434817. [DOI] [PubMed] [Google Scholar]
  18. Malm B. Chemical modification of Cys-374 of actin interferes with the formation of the profilactin complex. FEBS Lett. 1984 Aug 6;173(2):399–402. doi: 10.1016/0014-5793(84)80813-3. [DOI] [PubMed] [Google Scholar]
  19. Müller G., Zimmermann R. Import of honeybee prepromelittin into the endoplasmic reticulum: structural basis for independence of SRP and docking protein. EMBO J. 1987 Jul;6(7):2099–2107. doi: 10.1002/j.1460-2075.1987.tb02476.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Novick P., Botstein D. Phenotypic analysis of temperature-sensitive yeast actin mutants. Cell. 1985 Feb;40(2):405–416. doi: 10.1016/0092-8674(85)90154-0. [DOI] [PubMed] [Google Scholar]
  21. Oechsner U., Magdolen V., Bandlow W. The cDNA and deduced amino acid sequence of profilin from Saccharomyces cerevisiae. Nucleic Acids Res. 1987 Nov 11;15(21):9078–9078. doi: 10.1093/nar/15.21.9078. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Pollard T. D., Cooper J. A. Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Annu Rev Biochem. 1986;55:987–1035. doi: 10.1146/annurev.bi.55.070186.005011. [DOI] [PubMed] [Google Scholar]
  23. Rose M. D., Novick P., Thomas J. H., Botstein D., Fink G. R. A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector. Gene. 1987;60(2-3):237–243. doi: 10.1016/0378-1119(87)90232-0. [DOI] [PubMed] [Google Scholar]
  24. Rothstein R. J. One-step gene disruption in yeast. Methods Enzymol. 1983;101:202–211. doi: 10.1016/0076-6879(83)01015-0. [DOI] [PubMed] [Google Scholar]
  25. Shortle D., Haber J. E., Botstein D. Lethal disruption of the yeast actin gene by integrative DNA transformation. Science. 1982 Jul 23;217(4557):371–373. doi: 10.1126/science.7046050. [DOI] [PubMed] [Google Scholar]
  26. Stossel T. P., Chaponnier C., Ezzell R. M., Hartwig J. H., Janmey P. A., Kwiatkowski D. J., Lind S. E., Smith D. B., Southwick F. S., Yin H. L. Nonmuscle actin-binding proteins. Annu Rev Cell Biol. 1985;1:353–402. doi: 10.1146/annurev.cb.01.110185.002033. [DOI] [PubMed] [Google Scholar]
  27. Tobacman L. S., Korn E. D. The regulation of actin polymerization and the inhibition of monomeric actin ATPase activity by Acanthamoeba profilin. J Biol Chem. 1982 Apr 25;257(8):4166–4170. [PubMed] [Google Scholar]
  28. Vandekerckhove J., Weber K. Actin amino-acid sequences. Comparison of actins from calf thymus, bovine brain, and SV40-transformed mouse 3T3 cells with rabbit skeletal muscle actin. Eur J Biochem. 1978 Oct 16;90(3):451–462. doi: 10.1111/j.1432-1033.1978.tb12624.x. [DOI] [PubMed] [Google Scholar]
  29. Vandekerckhove J., Weber K. Mammalian cytoplasmic actins are the products of at least two genes and differ in primary structure in at least 25 identified positions from skeletal muscle actins. Proc Natl Acad Sci U S A. 1978 Mar;75(3):1106–1110. doi: 10.1073/pnas.75.3.1106. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Zuker M., Stiegler P. Optimal computer folding of large RNA sequences using thermodynamics and auxiliary information. Nucleic Acids Res. 1981 Jan 10;9(1):133–148. doi: 10.1093/nar/9.1.133. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES