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Research Article

Either of the Major H2A Genes but Not an Evolutionarily Conserved H2A.F/Z Variant of Tetrahymena thermophila Can Function as the Sole H2A Gene in the Yeast Saccharomyces cerevisiae

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Pages 2878-2887 | Received 07 Dec 1995, Accepted 17 Mar 1996, Published online: 29 Mar 2023

REFERENCES

  • Alani, E., L. Cao, and N. Kleckner. 1987. A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains. Genetics 116:541–545.
  • Allis, C. D., C. V. C. Glover, J. K. Bowen, and M. A. Gorovsky. 1980. Histone variants specific to the transcriptionally active, amitotically dividing macronucleus of the unicellular eukaryote, Tetrahymena thermophila. Cell 20:609–617.
  • Allis, C. D., C. V. C. Glover, and M. A. Gorovsky. 1979. Micronuclei of Tetrahymena contain two types of histones H3. Proc. Natl. Acad. Sci. USA 76:4857–4861.
  • Allis, C. D., R. Richman, M. A. Gorovsky, Y. S. Ziegler, B. Touchstone, W. A. Bradley, and R. G. Cook. 1986. hv1 is an evolutionarily conserved H2A variant that is preferentially associated with active genes. J. Biol. Chem. 261:1941–1948.
  • Allis, C. D., Y. S. Ziegler, M. A. Gorovsky, and J. B. Olmsted. 1982. A conserved histone variant enriched in nucleoli of mammalian cells. Cell 31:131–136.
  • Andreasen, P., H. D. Dreisig, and K. Kristiansen. 1987. Unusual ciliatespecific codons in Tetrahymena mRNAs are translated correctly in a rabbit reticulocyte lysate supplemented with a subcellular fraction from Tetrahymena. Biochem. J. 244:331–335.
  • Ausubel, F. M., R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). 1988. Current protocols in molecular biology. Wiley Interscience, New York.
  • Ball, D. L. J., C. A. Slaughter, P. Hensley, and W. T. Garrard. 1983. Amino acid sequence of the N-terminal domain of calf thymus histone H2A.Z. FEBS Lett. 154:166–170.
  • Bonner, W. M., and J. D. Stedman. 1979. Histone 1 is proximal to histone 2A and to A24. Proc. Natl. Acad. Sci. USA 76:2190–2194.
  • Bresnick, E. H., M. Bustin, V. Marsaud, H. Richard-Foy, and G. L. Hager. 1992. The transcriptionally-active MMTV promoter is depleted of histone H1. Nucleic Acids Res. 20:273–278.
  • Carr, A. M., S. M. Dorrington, J. Hindley, G. A. Phear, S. J. Aves, and P. Nurse. 1994. Analysis of a histone H2A variant from fission yeast: evidence for a role in chromosome stability. Mol. Gen. Genet. 245:628–635.
  • Choe, J., D. Kolodrubetz, and M. Grunstein. 1982. The two yeast histone H2A genes encode similar protein subtypes. Proc. Natl. Acad. Sci. USA 79:1484–1487.
  • Dedon, P. C., J. A. Soults, C. D. Allis, and M. A. Gorovsky. 1991. Formaldehyde cross-linking and immunoprecipitation demonstrate developmental changes in H1 association with transcriptionally active genes. Mol. Cell. Biol. 11:1729–1733.
  • Elgin, S. C. R., V. Dietrich, E. K. Steiner, J. B. Olmsted, C. D. Allis, and M. A. Gorovsky. Unpublished observations.
  • Ernst, S. G., H. Miller, C. A. Brenner, C. Nocente-McGrath, S. Francis, and R. McIsaac. 1987. Characterization of a cDNA clone coding for a sea urchin histone H2A variant related to the H2A.F/Z histone protein in vertebrates. Nucleic Acids Res. 15:4629–4644.
  • Garrard, W. T. 1991. Histone H1 and the conformation of transcriptionally active chromatin. Bioessays 13:87–88.
  • Glover, C. V. C., and M. A. Gorovsky. 1978. Histone-histone interactions in a lower eukaryote, Tetrahymena thermophila. Biochemistry 17:5705–5713.
  • Grunstein, M. 1990. Nucleosomes: regulators of transcription. Trends Genet. 6:395–400.
  • Grunstein, M. 1990. Histone function in transcription. Annu. Rev. Cell Biol. 6:643–678.
  • Grunstein, M., M. Rykowski, D. Kolodrubetz, J. Choe, and J. Wallis. 1984. A genetic analysis of histone protein subtypes in yeast, p. 35–63. In G. S. Stein, J. L. Stein, and W. F. Marzluff (ed.), Histone genes. John Wiley & Sons, New York.
  • Hanyu, N., Y. Kuchino, and S. Nishimura. 1986. Dramatic events in ciliate evolution: alteration of UAA and UAG termination codons to glutamine codons due to anticodon mutations in two Tetrahymena tRNAsGln. EMBO J. 5:1307–1311.
  • Harvey, R. P., and J. A. Whiting. 1983. H2A.F: an extremely variant histone H2A sequence expressed in the chicken embryo. Proc. Natl. Acad. Sci. USA 80:2819–2823.
  • Hirschhorn, J. N., A. L. Bortvin, S. L. Ricupero-Hovasse, and F. Winston. 1995. A new class of histone H2A mutations in Saccharomyces cerevisiae causes specific transcriptional defects in vivo. Mol. Cell. Biol. 15:1999–2009.
  • Horowitz, S., and M. A. Gorovsky. 1985. An unusual genetic code in nuclear genes of Tetrahymena. Proc. Natl. Acad. Sci. USA 82:2452–2455.
  • Isenberg, I. 1979. Histones. Annu. Rev. Biochem. 48:159–191.
  • Jin, Z. X., K. Inaba, K. Manaka, M. Morisawa, and H. Hayashi. 1994. Monoclonal antibodies against the protein complex that contains the flagellar movement-initiating phosphoprotein of Oncorhynchus keta. J. Biochem. 115:885–890.
  • Kamakaka, R. T., and J. O. Thomas. 1990. Chromatin structure of transcriptionally competent and repressed genes. EMBO J. 9:3997–4006.
  • Kolodrubetz, D., M. O. Rykowski, and M. Grunstein. 1982. Histone H2A subtypes associate interchangeably in vivo with histone H2B subtypes. Proc. Natl. Acad. Sci. USA 79:7814–7818.
  • Kuchino, Y., N. Hanyu, G. Tashiro, and S. Nishimura. 1985. Tetrahymena thermophila glutamine tRNA and its gene that corresponds to UAA termination codon. Proc. Natl. Acad. Sci. USA 82:4758–4762.
  • Lindsey, G. G., S. Orgeig, P. Thompson, N. Davies, and D. L. Maeder. 1991. Extended C-terminal tail of wheat histone H2A interacts with DNA of the "linker" region. J. Mol. Biol. 218:805–813.
  • Lindsey, G. G., and P. Thompson. 1992. S(T)PXX motifs promote the interaction between the extended N-terminal tails of histone H2B with ''linker" DNA. J. Biol. Chem. 267:14622–14628.
  • Liu, X., and M. A. Gorovsky. Cloning and characterization of the major histone H2A genes completes the cloning and sequencing of known histone genes of Tetrahymena thermophila. Submitted for publication.
  • Liu, X., B. Li, and M. A. Gorovsky. Essential and non-essential H2Avariants in Tetrahymena. Submitted for publication.
  • Lohr, D., and L. Hereford. 1979. Yeast chromatin is uniformly digested by DNase I. Proc. Natl. Acad. Sci. USA 76:4285–4288.
  • Lundblad, V. 1989. Segregation of plasmids from yeast cells, p. 13.10.1–13.10.6. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology. Greene Publishing Associates, Brooklyn, N.Y.
  • Mardian, J. K., and I. Isenberg. 1978. Yeast inner histones and the evolutionary conservation of histone-histone interactions. Biochemistry 17:3825–3833.
  • Martindale, D. W. 1989. Codon usage in Tetrahymena and other ciliates. J. Protozool. 36:29–34.
  • Moehs, C. P., A. D. Baxevanis, E. N. Moudrianakis, and S. Spiker. 1992. Enhanced stability of histone octamers from plant nucleosomes: role of H2A and H2B histones. Biochemistry 31:10844–10851.
  • Phizicky, E. M., R. C. Schwartz, and J. Abelson. 1986. Saccharomyces cerevisiae tRNA ligase: purification of the protein and isolation of the structural gene. J. Biol. Chem. 261:2978–2986.
  • Rothstein, R. J. 1983. One-step gene disruption in yeast. Methods Enzymol. 101:202–211.
  • Rykowski, M. C., J. W. Wallis, J. Choe, and M. Grunstein. 1981. Histone H2B subtypes are dispensable during the yeast cell cycle. Cell 25:477–487.
  • Schiestl, R. H., and R. D. Gietz. 1989. High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr. Genet. 16:339–346.
  • Schuster, T., M. Han, and M. Grunstein. 1986. Yeast histone H2A and H2B amino termini have interchangeable functions. Cell 45:445–451.
  • Shwed, P. S., J. M. Neelin, and V. L. Seligy. 1992. Expression of Xenopus laevis histone H5 gene in yeast. Biochim. Biophys. Acta 1131:152–160.
  • Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19–27.
  • Sobel, R., and C. D. Allis. Unpublished observations.
  • Stargell, L. A., J. Bowen, C. A. Dadd, P. C. Dedon, M. Davis, R. G. Cook, C. D. Allis, and M. A. Gorovsky. 1993. Temporal and spatial association of histone H2A variant hv1 with transcriptionally competent chromatin during nuclear development in Tetrahymena thermophila. Genes Dev. 7:2641–2651.
  • Thatcher, T. H., and M. A. Gorovsky. 1994. Phylogenetic analysis of the core histones H2A, H2B, H3, and H4. Nucleic Acids Res. 22:174–179.
  • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350–4354.
  • Van Daal, A., and S. C. R. Elgin. 1992. A histone variant, H2AvD, is essential in Drosophila melanogaster. Mol. Biol. Cell 3:593–602.
  • Van Daal, A., E. M. White, S. C. R. Elgin, and M. A. Gorovsky. 1990. Conservation of intron position indicates separation of major and variant H2As is an early event in the evolution of eukaryotes. J. Mol. Evol. 30:449–455.
  • Van Daal, A., E. M. White, M. A. Gorovsky, and S. C. R. Elgin. 1988. Drosophila has a single copy of the gene encoding a highly conserved histone H2A variant of the H2A.F/Z type. Nucleic Acids Res. 16:7487–7498.
  • Van Holde, K. E. 1989. Chromatin. Springer-Verlag, New York.
  • Wenkert, D., and C. D. Allis. 1984. Timing of the appearance of macronuclear-specific histone variant hv1 and gene expression in developing new macronuclei of Tetrahymena thermophila. J. Cell Biol. 98:2107–2117.
  • White, E. M., D. L. Shapiro, C. D. Allis, and M. A. Gorovsky. 1988. Sequence and properties of the message encoding Tetrahymena hv1, a highly evolutionarily conserved histone H2A variant that is associated with active genes. Nucleic Acids Res. 16:179–198.
  • Wu, R. S., H. T. Panusz, C. L. Hatch, and W. M. Bonner. 1986. Histones and their modifications. Crit. Rev. Biochem. 20:201–263.

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