Skip to main content
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1993 Feb 1;120(3):613–624. doi: 10.1083/jcb.120.3.613

Mitotic repression of transcription in vitro

PMCID: PMC2119533  PMID: 8381119

Abstract

A normal consequence of mitosis in eukaryotes is the repression of transcription. Using Xenopus egg extracts shifted to a mitotic state by the addition of purified cyclin, we have for the first time been able to reproduce a mitotic repression of transcription in vitro. Active RNA polymerase III transcription is observed in interphase extracts, but strongly repressed in extracts converted to mitosis. With the topoisomerase II inhibitor VM-26, we demonstrate that this mitotic repression of RNA polymerase III transcription does not require normal chromatin condensation. Similarly; in vitro mitotic repression of transcription does not require the presence of nucleosome structure or involve a general repressive chromatin-binding protein, as inhibition of chromatin formation with saturating amounts of non-specific DNA has no effect on repression. Instead, the mitotic repression of transcription appears to be due to phosphorylation of a component of the transcription machinery by a mitotic protein kinase, either cdc2 kinase and/or a kinase activated by it. Mitotic repression of RNA polymerase III transcription is observed both in complete mitotic cytosol and when a kinase-enriched mitotic fraction is added to a highly simplified 5S RNA transcription reaction. We present evidence that, upon depletion of cdc2 kinase, a secondary protein kinase activity remains and can mediate this in vitro mitotic repression of transcription.

Full Text

The Full Text of this article is available as a PDF (1.9 MB).

Selected References

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

  1. Adachi Y., Luke M., Laemmli U. K. Chromosome assembly in vitro: topoisomerase II is required for condensation. Cell. 1991 Jan 11;64(1):137–148. doi: 10.1016/0092-8674(91)90215-k. [DOI] [PubMed] [Google Scholar]
  2. Almouzni G., Méchali M., Wolffe A. P. Competition between transcription complex assembly and chromatin assembly on replicating DNA. EMBO J. 1990 Feb;9(2):573–582. doi: 10.1002/j.1460-2075.1990.tb08145.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Almouzni G., Méchali M., Wolffe A. P. Transcription complex disruption caused by a transition in chromatin structure. Mol Cell Biol. 1991 Feb;11(2):655–665. doi: 10.1128/mcb.11.2.655. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Binétruy B., Smeal T., Karin M. Ha-Ras augments c-Jun activity and stimulates phosphorylation of its activation domain. Nature. 1991 May 9;351(6322):122–127. doi: 10.1038/351122a0. [DOI] [PubMed] [Google Scholar]
  5. Boyle W. J., Smeal T., Defize L. H., Angel P., Woodgett J. R., Karin M., Hunter T. Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity. Cell. 1991 Feb 8;64(3):573–584. doi: 10.1016/0092-8674(91)90241-p. [DOI] [PubMed] [Google Scholar]
  6. Bradbury E. M., Inglis R. J., Matthews H. R. Control of cell division by very lysine rich histone (F1) phosphorylation. Nature. 1974 Feb 1;247(5439):257–261. doi: 10.1038/247257a0. [DOI] [PubMed] [Google Scholar]
  7. Bradbury E. M. Reversible histone modifications and the chromosome cell cycle. Bioessays. 1992 Jan;14(1):9–16. doi: 10.1002/bies.950140103. [DOI] [PubMed] [Google Scholar]
  8. Brizuela L., Draetta G., Beach D. p13suc1 acts in the fission yeast cell division cycle as a component of the p34cdc2 protein kinase. EMBO J. 1987 Nov;6(11):3507–3514. doi: 10.1002/j.1460-2075.1987.tb02676.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Brown D. D. The role of stable complexes that repress and activate eucaryotic genes. Cell. 1984 Jun;37(2):359–365. doi: 10.1016/0092-8674(84)90366-0. [DOI] [PubMed] [Google Scholar]
  10. Carrara G., Di Segni G., Otsuka A., Tocchini-Valentini G. P. Deletion of the 3' half of the yeast tRNA-Leu3 gene does not abolish promotor function in vitro. Cell. 1981 Dec;27(2 Pt 1):371–379. doi: 10.1016/0092-8674(81)90420-7. [DOI] [PubMed] [Google Scholar]
  11. Chen G. L., Yang L., Rowe T. C., Halligan B. D., Tewey K. M., Liu L. F. Nonintercalative antitumor drugs interfere with the breakage-reunion reaction of mammalian DNA topoisomerase II. J Biol Chem. 1984 Nov 10;259(21):13560–13566. [PubMed] [Google Scholar]
  12. Cisek L. J., Corden J. L. Phosphorylation of RNA polymerase by the murine homologue of the cell-cycle control protein cdc2. Nature. 1989 Jun 29;339(6227):679–684. doi: 10.1038/339679a0. [DOI] [PubMed] [Google Scholar]
  13. Cohen P. The structure and regulation of protein phosphatases. Annu Rev Biochem. 1989;58:453–508. doi: 10.1146/annurev.bi.58.070189.002321. [DOI] [PubMed] [Google Scholar]
  14. Comai L., Tanese N., Tjian R. The TATA-binding protein and associated factors are integral components of the RNA polymerase I transcription factor, SL1. Cell. 1992 Mar 6;68(5):965–976. doi: 10.1016/0092-8674(92)90039-f. [DOI] [PubMed] [Google Scholar]
  15. Corden J. L. Tails of RNA polymerase II. Trends Biochem Sci. 1990 Oct;15(10):383–387. doi: 10.1016/0968-0004(90)90236-5. [DOI] [PubMed] [Google Scholar]
  16. Cormack B. P., Struhl K. The TATA-binding protein is required for transcription by all three nuclear RNA polymerases in yeast cells. Cell. 1992 May 15;69(4):685–696. doi: 10.1016/0092-8674(92)90232-2. [DOI] [PubMed] [Google Scholar]
  17. Dilworth S. M., Black S. J., Laskey R. A. Two complexes that contain histones are required for nucleosome assembly in vitro: role of nucleoplasmin and N1 in Xenopus egg extracts. Cell. 1987 Dec 24;51(6):1009–1018. doi: 10.1016/0092-8674(87)90587-3. [DOI] [PubMed] [Google Scholar]
  18. Draetta G., Luca F., Westendorf J., Brizuela L., Ruderman J., Beach D. Cdc2 protein kinase is complexed with both cyclin A and B: evidence for proteolytic inactivation of MPF. Cell. 1989 Mar 10;56(5):829–838. doi: 10.1016/0092-8674(89)90687-9. [DOI] [PubMed] [Google Scholar]
  19. Dunphy W. G., Brizuela L., Beach D., Newport J. The Xenopus cdc2 protein is a component of MPF, a cytoplasmic regulator of mitosis. Cell. 1988 Jul 29;54(3):423–431. doi: 10.1016/0092-8674(88)90205-x. [DOI] [PubMed] [Google Scholar]
  20. Dunphy W. G., Newport J. W. Mitosis-inducing factors are present in a latent form during interphase in the Xenopus embryo. J Cell Biol. 1988 Jun;106(6):2047–2056. doi: 10.1083/jcb.106.6.2047. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Edgar B. A., Kiehle C. P., Schubiger G. Cell cycle control by the nucleo-cytoplasmic ratio in early Drosophila development. Cell. 1986 Jan 31;44(2):365–372. doi: 10.1016/0092-8674(86)90771-3. [DOI] [PubMed] [Google Scholar]
  22. Edgar B. A., Schubiger G. Parameters controlling transcriptional activation during early Drosophila development. Cell. 1986 Mar 28;44(6):871–877. doi: 10.1016/0092-8674(86)90009-7. [DOI] [PubMed] [Google Scholar]
  23. Fang F., Newport J. W. Evidence that the G1-S and G2-M transitions are controlled by different cdc2 proteins in higher eukaryotes. Cell. 1991 Aug 23;66(4):731–742. doi: 10.1016/0092-8674(91)90117-h. [DOI] [PubMed] [Google Scholar]
  24. Felsenfeld G. Chromatin as an essential part of the transcriptional mechanism. Nature. 1992 Jan 16;355(6357):219–224. doi: 10.1038/355219a0. [DOI] [PubMed] [Google Scholar]
  25. Felsenfeld G., McGhee J. D. Structure of the 30 nm chromatin fiber. Cell. 1986 Feb 14;44(3):375–377. doi: 10.1016/0092-8674(86)90456-3. [DOI] [PubMed] [Google Scholar]
  26. Felts S. J., Weil P. A., Chalkley R. Transcription factor requirements for in vitro formation of transcriptionally competent 5S rRNA gene chromatin. Mol Cell Biol. 1990 May;10(5):2390–2401. doi: 10.1128/mcb.10.5.2390. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Fink K., Turnock G. Synthesis of transfer RNA during the synchronous nuclear division cycle in Physarum polycephalum. Eur J Biochem. 1977 Oct 17;80(1):93–96. doi: 10.1111/j.1432-1033.1977.tb11860.x. [DOI] [PubMed] [Google Scholar]
  28. Fletcher C., Heintz N., Roeder R. G. Purification and characterization of OTF-1, a transcription factor regulating cell cycle expression of a human histone H2b gene. Cell. 1987 Dec 4;51(5):773–781. doi: 10.1016/0092-8674(87)90100-0. [DOI] [PubMed] [Google Scholar]
  29. Forbes D. J., Kirschner M. W., Newport J. W. Spontaneous formation of nucleus-like structures around bacteriophage DNA microinjected into Xenopus eggs. Cell. 1983 Aug;34(1):13–23. doi: 10.1016/0092-8674(83)90132-0. [DOI] [PubMed] [Google Scholar]
  30. Fotedar R., Roberts J. M. Association of p34cdc2 with replicating DNA. Cold Spring Harb Symp Quant Biol. 1991;56:325–333. doi: 10.1101/sqb.1991.056.01.039. [DOI] [PubMed] [Google Scholar]
  31. Gautier J., Norbury C., Lohka M., Nurse P., Maller J. Purified maturation-promoting factor contains the product of a Xenopus homolog of the fission yeast cell cycle control gene cdc2+. Cell. 1988 Jul 29;54(3):433–439. doi: 10.1016/0092-8674(88)90206-1. [DOI] [PubMed] [Google Scholar]
  32. Gazit B., Cedar H., Lerer I., Voss R. Active genes are sensitive to deoxyribonuclease I during metaphase. Science. 1982 Aug 13;217(4560):648–650. doi: 10.1126/science.6283640. [DOI] [PubMed] [Google Scholar]
  33. Geiduschek E. P., Tocchini-Valentini G. P. Transcription by RNA polymerase III. Annu Rev Biochem. 1988;57:873–914. doi: 10.1146/annurev.bi.57.070188.004301. [DOI] [PubMed] [Google Scholar]
  34. Glotzer M., Murray A. W., Kirschner M. W. Cyclin is degraded by the ubiquitin pathway. Nature. 1991 Jan 10;349(6305):132–138. doi: 10.1038/349132a0. [DOI] [PubMed] [Google Scholar]
  35. Gottesfeld J. M. Novobiocin inhibits RNA polymerase III transcription in vitro by a mechanism distinct from DNA topoisomerase II. Nucleic Acids Res. 1986 Mar 11;14(5):2075–2088. doi: 10.1093/nar/14.5.2075. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Gottesfeld J., Bloomer L. S. Assembly of transcriptionally active 5S RNA gene chromatin in vitro. Cell. 1982 Apr;28(4):781–791. doi: 10.1016/0092-8674(82)90057-5. [DOI] [PubMed] [Google Scholar]
  37. Heck M. M., Hittelman W. N., Earnshaw W. C. In vivo phosphorylation of the 170-kDa form of eukaryotic DNA topoisomerase II. Cell cycle analysis. J Biol Chem. 1989 Sep 15;264(26):15161–15164. [PubMed] [Google Scholar]
  38. Hirano T., Mitchison T. J. Cell cycle control of higher-order chromatin assembly around naked DNA in vitro. J Cell Biol. 1991 Dec;115(6):1479–1489. doi: 10.1083/jcb.115.6.1479. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Johnson T. C., Holland J. J. Ribonucleic acid and protein synthesis in mitotic HeLa cells. J Cell Biol. 1965 Dec;27(3):565–574. doi: 10.1083/jcb.27.3.565. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Johnston L. H., White J. H., Johnson A. L., Lucchini G., Plevani P. The yeast DNA polymerase I transcript is regulated in both the mitotic cell cycle and in meiosis and is also induced after DNA damage. Nucleic Acids Res. 1987 Jul 10;15(13):5017–5030. doi: 10.1093/nar/15.13.5017. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Kassavetis G. A., Riggs D. L., Negri R., Nguyen L. H., Geiduschek E. P. Transcription factor IIIB generates extended DNA interactions in RNA polymerase III transcription complexes on tRNA genes. Mol Cell Biol. 1989 Jun;9(6):2551–2566. doi: 10.1128/mcb.9.6.2551. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Keller H. J., You Q. M., Romaniuk P. J., Gottesfeld J. M. Additional intragenic promoter elements of the Xenopus 5S RNA genes upstream from the TFIIIA-binding site. Mol Cell Biol. 1990 Oct;10(10):5166–5176. doi: 10.1128/mcb.10.10.5166. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Kerem B. S., Goitein R., Diamond G., Cedar H., Marcus M. Mapping of DNAase I sensitive regions on mitotic chromosomes. Cell. 1984 Sep;38(2):493–499. doi: 10.1016/0092-8674(84)90504-x. [DOI] [PubMed] [Google Scholar]
  44. Kimelman D., Kirschner M., Scherson T. The events of the midblastula transition in Xenopus are regulated by changes in the cell cycle. Cell. 1987 Feb 13;48(3):399–407. doi: 10.1016/0092-8674(87)90191-7. [DOI] [PubMed] [Google Scholar]
  45. Kornberg R. D., Lorch Y. Irresistible force meets immovable object: transcription and the nucleosome. Cell. 1991 Nov 29;67(5):833–836. doi: 10.1016/0092-8674(91)90354-2. [DOI] [PubMed] [Google Scholar]
  46. Labbe J. C., Picard A., Peaucellier G., Cavadore J. C., Nurse P., Doree M. Purification of MPF from starfish: identification as the H1 histone kinase p34cdc2 and a possible mechanism for its periodic activation. Cell. 1989 Apr 21;57(2):253–263. doi: 10.1016/0092-8674(89)90963-x. [DOI] [PubMed] [Google Scholar]
  47. Laskey R. A., Leno G. H. Assembly of the cell nucleus. Trends Genet. 1990 Dec;6(12):406–410. doi: 10.1016/0168-9525(90)90301-l. [DOI] [PubMed] [Google Scholar]
  48. Laskey R. A., Mills A. D., Morris N. R. Assembly of SV40 chromatin in a cell-free system from Xenopus eggs. Cell. 1977 Feb;10(2):237–243. doi: 10.1016/0092-8674(77)90217-3. [DOI] [PubMed] [Google Scholar]
  49. Laybourn P. J., Kadonaga J. T. Role of nucleosomal cores and histone H1 in regulation of transcription by RNA polymerase II. Science. 1991 Oct 11;254(5029):238–245. doi: 10.1126/science.254.5029.238. [DOI] [PubMed] [Google Scholar]
  50. Lewin B. Driving the cell cycle: M phase kinase, its partners, and substrates. Cell. 1990 Jun 1;61(5):743–752. doi: 10.1016/0092-8674(90)90181-d. [DOI] [PubMed] [Google Scholar]
  51. Lewis C. D., Lebkowski J. S., Daly A. K., Laemmli U. K. Interphase nuclear matrix and metaphase scaffolding structures. J Cell Sci Suppl. 1984;1:103–122. doi: 10.1242/jcs.1984.supplement_1.8. [DOI] [PubMed] [Google Scholar]
  52. Liu L. F. DNA topoisomerase poisons as antitumor drugs. Annu Rev Biochem. 1989;58:351–375. doi: 10.1146/annurev.bi.58.070189.002031. [DOI] [PubMed] [Google Scholar]
  53. Lohka M. J., Maller J. L. Induction of nuclear envelope breakdown, chromosome condensation, and spindle formation in cell-free extracts. J Cell Biol. 1985 Aug;101(2):518–523. doi: 10.1083/jcb.101.2.518. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Lohka M. J., Masui Y. Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components. Science. 1983 May 13;220(4598):719–721. doi: 10.1126/science.6601299. [DOI] [PubMed] [Google Scholar]
  55. Mattoccia E., Baldi I. M., Gandini-Attardi D., Ciafrè S., Tocchini-Valentini G. P. Site selection by the tRNA splicing endonuclease of Xenopus laevis. Cell. 1988 Nov 18;55(4):731–738. doi: 10.1016/0092-8674(88)90231-0. [DOI] [PubMed] [Google Scholar]
  56. Miake-Lye R., Kirschner M. W. Induction of early mitotic events in a cell-free system. Cell. 1985 May;41(1):165–175. doi: 10.1016/0092-8674(85)90071-6. [DOI] [PubMed] [Google Scholar]
  57. Millstein L. S., Gottesfeld J. M. Control of gene expression in eukaryotic cells: lessons from class III genes. Curr Opin Cell Biol. 1989 Jun;1(3):497–502. doi: 10.1016/0955-0674(89)90011-2. [DOI] [PubMed] [Google Scholar]
  58. Minshull J., Blow J. J., Hunt T. Translation of cyclin mRNA is necessary for extracts of activated xenopus eggs to enter mitosis. Cell. 1989 Mar 24;56(6):947–956. doi: 10.1016/0092-8674(89)90628-4. [DOI] [PubMed] [Google Scholar]
  59. Moreno S., Nurse P. Substrates for p34cdc2: in vivo veritas? Cell. 1990 May 18;61(4):549–551. doi: 10.1016/0092-8674(90)90463-o. [DOI] [PubMed] [Google Scholar]
  60. Murray A. W., Solomon M. J., Kirschner M. W. The role of cyclin synthesis and degradation in the control of maturation promoting factor activity. Nature. 1989 May 25;339(6222):280–286. doi: 10.1038/339280a0. [DOI] [PubMed] [Google Scholar]
  61. Newport J. W., Kirschner M. W. Regulation of the cell cycle during early Xenopus development. Cell. 1984 Jul;37(3):731–742. doi: 10.1016/0092-8674(84)90409-4. [DOI] [PubMed] [Google Scholar]
  62. Newport J. Nuclear reconstitution in vitro: stages of assembly around protein-free DNA. Cell. 1987 Jan 30;48(2):205–217. doi: 10.1016/0092-8674(87)90424-7. [DOI] [PubMed] [Google Scholar]
  63. Newport J., Spann T. Disassembly of the nucleus in mitotic extracts: membrane vesicularization, lamin disassembly, and chromosome condensation are independent processes. Cell. 1987 Jan 30;48(2):219–230. doi: 10.1016/0092-8674(87)90425-9. [DOI] [PubMed] [Google Scholar]
  64. Newport J., Spann T., Kanki J., Forbes D. The role of mitotic factors in regulating the timing of the midblastula transition in Xenopus. Cold Spring Harb Symp Quant Biol. 1985;50:651–656. doi: 10.1101/sqb.1985.050.01.079. [DOI] [PubMed] [Google Scholar]
  65. Otsuka A., de Paolis A., Tocchini-Valentini G. P. Ribonuclease "XlaI," an activity from Xenopus laevis oocytes that excises intervening sequences from yeast transfer ribonucleic acid precursors. Mol Cell Biol. 1981 Mar;1(3):269–280. doi: 10.1128/mcb.1.3.269. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. PRESCOTT D. M., BENDER M. A. Synthesis of RNA and protein during mitosis in mammalian tissue culture cells. Exp Cell Res. 1962 Mar;26:260–268. doi: 10.1016/0014-4827(62)90176-3. [DOI] [PubMed] [Google Scholar]
  67. Peterson R. C., Doering J. L., Brown D. D. Characterization of two xenopus somatic 5S DNAs and one minor oocyte-specific 5S DNA. Cell. 1980 May;20(1):131–141. doi: 10.1016/0092-8674(80)90241-x. [DOI] [PubMed] [Google Scholar]
  68. Pfaller R., Smythe C., Newport J. W. Assembly/disassembly of the nuclear envelope membrane: cell cycle-dependent binding of nuclear membrane vesicles to chromatin in vitro. Cell. 1991 Apr 19;65(2):209–217. doi: 10.1016/0092-8674(91)90155-r. [DOI] [PubMed] [Google Scholar]
  69. Pines J., Hunter T. p34cdc2: the S and M kinase? New Biol. 1990 May;2(5):389–401. [PubMed] [Google Scholar]
  70. Razik M. A., Blanco J., Gottesfeld J. M. Pathways of nucleoprotein assembly on 5S RNA genes in a Xenopus oocyte S-150 extract. Nucleic Acids Res. 1989 Jun 12;17(11):4117–4130. doi: 10.1093/nar/17.11.4117. [DOI] [PMC free article] [PubMed] [Google Scholar]
  71. Roberge M., Th'ng J., Hamaguchi J., Bradbury E. M. The topoisomerase II inhibitor VM-26 induces marked changes in histone H1 kinase activity, histones H1 and H3 phosphorylation, and chromosome condensation in G2 phase and mitotic BHK cells. J Cell Biol. 1990 Nov;111(5 Pt 1):1753–1762. doi: 10.1083/jcb.111.5.1753. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Roberts S. B., Segil N., Heintz N. Differential phosphorylation of the transcription factor Oct1 during the cell cycle. Science. 1991 Aug 30;253(5023):1022–1026. doi: 10.1126/science.1887216. [DOI] [PubMed] [Google Scholar]
  73. Schlissel M. S., Brown D. D. The transcriptional regulation of Xenopus 5s RNA genes in chromatin: the roles of active stable transcription complexes and histone H1. Cell. 1984 Jul;37(3):903–913. doi: 10.1016/0092-8674(84)90425-2. [DOI] [PubMed] [Google Scholar]
  74. Schultz M. C., Reeder R. H., Hahn S. Variants of the TATA-binding protein can distinguish subsets of RNA polymerase I, II, and III promoters. Cell. 1992 May 15;69(4):697–702. doi: 10.1016/0092-8674(92)90233-3. [DOI] [PubMed] [Google Scholar]
  75. Segil N., Roberts S. B., Heintz N. Mitotic phosphorylation of the Oct-1 homeodomain and regulation of Oct-1 DNA binding activity. Science. 1991 Dec 20;254(5039):1814–1816. doi: 10.1126/science.1684878. [DOI] [PubMed] [Google Scholar]
  76. Shermoen A. W., O'Farrell P. H. Progression of the cell cycle through mitosis leads to abortion of nascent transcripts. Cell. 1991 Oct 18;67(2):303–310. doi: 10.1016/0092-8674(91)90182-x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  77. Shimamura A., Sapp M., Rodriguez-Campos A., Worcel A. Histone H1 represses transcription from minichromosomes assembled in vitro. Mol Cell Biol. 1989 Dec;9(12):5573–5584. doi: 10.1128/mcb.9.12.5573. [DOI] [PMC free article] [PubMed] [Google Scholar]
  78. Simanis V., Nurse P. The cell cycle control gene cdc2+ of fission yeast encodes a protein kinase potentially regulated by phosphorylation. Cell. 1986 Apr 25;45(2):261–268. doi: 10.1016/0092-8674(86)90390-9. [DOI] [PubMed] [Google Scholar]
  79. Simpson R. T., Thoma F., Brubaker J. M. Chromatin reconstituted from tandemly repeated cloned DNA fragments and core histones: a model system for study of higher order structure. Cell. 1985 Oct;42(3):799–808. doi: 10.1016/0092-8674(85)90276-4. [DOI] [PubMed] [Google Scholar]
  80. Smythe C., Newport J. W. Coupling of mitosis to the completion of S phase in Xenopus occurs via modulation of the tyrosine kinase that phosphorylates p34cdc2. Cell. 1992 Feb 21;68(4):787–797. doi: 10.1016/0092-8674(92)90153-4. [DOI] [PubMed] [Google Scholar]
  81. Smythe C., Newport J. W. Systems for the study of nuclear assembly, DNA replication, and nuclear breakdown in Xenopus laevis egg extracts. Methods Cell Biol. 1991;35:449–468. doi: 10.1016/s0091-679x(08)60583-x. [DOI] [PubMed] [Google Scholar]
  82. Solomon M. J., Glotzer M., Lee T. H., Philippe M., Kirschner M. W. Cyclin activation of p34cdc2. Cell. 1990 Nov 30;63(5):1013–1024. doi: 10.1016/0092-8674(90)90504-8. [DOI] [PubMed] [Google Scholar]
  83. Toyoda T., Wolffe A. P. In vitro transcription by RNA polymerase II in extracts of Xenopus oocytes, eggs, and somatic cells. Anal Biochem. 1992 Jun;203(2):340–347. doi: 10.1016/0003-2697(92)90322-x. [DOI] [PubMed] [Google Scholar]
  84. Uemura T., Ohkura H., Adachi Y., Morino K., Shiozaki K., Yanagida M. DNA topoisomerase II is required for condensation and separation of mitotic chromosomes in S. pombe. Cell. 1987 Sep 11;50(6):917–925. doi: 10.1016/0092-8674(87)90518-6. [DOI] [PubMed] [Google Scholar]
  85. Weintraub H. Assembly and propagation of repressed and depressed chromosomal states. Cell. 1985 Oct;42(3):705–711. doi: 10.1016/0092-8674(85)90267-3. [DOI] [PubMed] [Google Scholar]
  86. White J. H., Green S. R., Barker D. G., Dumas L. B., Johnston L. H. The CDC8 transcript is cell cycle regulated in yeast and is expressed coordinately with CDC9 and CDC21 at a point preceding histone transcription. Exp Cell Res. 1987 Jul;171(1):223–231. doi: 10.1016/0014-4827(87)90265-5. [DOI] [PubMed] [Google Scholar]
  87. White R. J., Jackson S. P., Rigby P. W. A role for the TATA-box-binding protein component of the transcription factor IID complex as a general RNA polymerase III transcription factor. Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1949–1953. doi: 10.1073/pnas.89.5.1949. [DOI] [PMC free article] [PubMed] [Google Scholar]
  88. Wilson K. L., Newport J. A trypsin-sensitive receptor on membrane vesicles is required for nuclear envelope formation in vitro. J Cell Biol. 1988 Jul;107(1):57–68. doi: 10.1083/jcb.107.1.57. [DOI] [PMC free article] [PubMed] [Google Scholar]
  89. Wolffe A. P., Andrews M. T., Crawford E., Losa R., Brown D. D. Negative supercoiling is not required for 5S RNA transcription in vitro. Cell. 1987 May 8;49(3):301–303. doi: 10.1016/0092-8674(87)90279-0. [DOI] [PubMed] [Google Scholar]
  90. Wolffe A. P., Brown D. D. Differential 5S RNA gene expression in vitro. Cell. 1987 Dec 4;51(5):733–740. doi: 10.1016/0092-8674(87)90096-1. [DOI] [PubMed] [Google Scholar]
  91. Wolffe A. P. Developmental regulation of chromatin structure and function. Trends Cell Biol. 1991 Aug;1(2-3):61–66. doi: 10.1016/0962-8924(91)90091-m. [DOI] [PubMed] [Google Scholar]
  92. Wolffe A. P. Dominant and specific repression of Xenopus oocyte 5S RNA genes and satellite I DNA by histone H1. EMBO J. 1989 Feb;8(2):527–537. doi: 10.1002/j.1460-2075.1989.tb03407.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  93. Wood E. R., Earnshaw W. C. Mitotic chromatin condensation in vitro using somatic cell extracts and nuclei with variable levels of endogenous topoisomerase II. J Cell Biol. 1990 Dec;111(6 Pt 2):2839–2850. doi: 10.1083/jcb.111.6.2839. [DOI] [PMC free article] [PubMed] [Google Scholar]
  94. Wu M., Gerhart J. C. Partial purification and characterization of the maturation-promoting factor from eggs of Xenopus laevis. Dev Biol. 1980 Oct;79(2):465–477. doi: 10.1016/0012-1606(80)90131-1. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES