Dexamethasone stimulates ribosomal protein L32 gene transcription in rat myoblasts

Molecular and Cellular Endocrinology

Volumn 167, Issue 1-2, 2000, Pages 127-137

  Sienna, Nancy ^a   Larson, Dawn E ^a   Sells, Bruce H ^a  

^a UNIVERSITY OF GUELPH   (Canada)

Author keywords

Dexamethasone; Myoblasts; Ribosomal protein gene expression; RU38486

Indexed keywords

DEXAMETHASONE; GLUCOCORTICOID; MIFEPRISTONE; PROTEIN RPL32; PROTEIN SUBUNIT; RIBOSOME PROTEIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DRUG MECHANISM; GENE ACTIVATION; HORMONE RESPONSIVE ELEMENT; MYOBLAST; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN DNA BINDING; RAT; TRANSCRIPTION REGULATION;

ANIMAL; BLOTTING, WESTERN; CELL EXTRACTS; CELL LINE; CYCLOHEXIMIDE; DACTINOMYCIN; DEXAMETHASONE; DNA-BINDING PROTEINS; ELECTROPHORESIS; GLUCOCORTICOIDS, SYNTHETIC; HORMONE ANTAGONISTS; MIFEPRISTONE; MUSCLE DEVELOPMENT; MUSCLES; NUCLEIC ACID SYNTHESIS INHIBITORS; PLASMIDS; PROMOTER REGIONS (GENETICS); RATS; RIBOSOMAL PROTEINS; RNA; SUPPORT, NON-U.S. GOV'T; TRANS-ACTIVATION (GENETICS); TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC;

EID: 0034715064     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(00)00282-3     Document Type: Article

References (60)

1. Agrawal M.G., Bowman L.H. Transcriptional and translational regulation of ribosomal protein formation during mouse myoblast differentiation. J. Biol. Chem. 262:1987;4868-4875.
2. Atchison M.L., Meyuhas O., Perry R.P. Localization of transcriptional regulatory elements and nuclear factor binding sites in mouse ribosomal protein gene rpL32. Mol. Cell. Biol. 9:1989;2067-2074.
3. Campagnoni A.T., Verdi J.M., Verity A.N., Amur-Umarjee S., Byravan S. Posttranscriptional regulation of myelin protein gene expression. Ann. N. Y. Acad. Sci. 633:1991;178-188.
4. Cavanaugh A.H., Thompson E.A. Hormonal regulation of transcription of rDNA. J. Biol. Chem. 258:1983;9768-9773.
5. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. Biophys. 172:1987;627-633.
6. Chung S., Perry R.P. Importance of introns in for the expression of mouse ribosomal protein gene rpL32. Mol. Cell. Biol. 9:1989;2075-2082.
7. Collingwood T.N., Urnov F.D., Wolffe A.P. Nuclear receptors: coactivators, corepressors and chromatin remodeling in the control of transcription. J. Mol. Endocrin. 23:1999;255-275.
8. Dabeva M.D., Ikonomova R.N. Acceleration of ribosome formation in rat liver in response to hydrocortisone. Mol. Cell. Endocrinol. 28:1982;263-273.
9. Diamond D.J., Goodman H.M. Regulation of growth hormone messenger RNA synthesis by dexamethasone and triiodothyronine. J. Mol. Biol. 181:1985;41-62.
10. Dignam J.D., Lebovitz R.M., Roeder R.G. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1983;1475-1489.
11. Donovan D.M., Pearson N.J. Transcriptional regulation of ribosomal proteins during a nutritional upshift in Saccharomyces cerevisiae. Mol. Cell. Biol. 6:1986;2429-2435.
12. Dudov K.P., Perry R.P. The gene family encoding the mouse ribosomal protein L32 contains a uniquely expressed intron-containing gene and an unmutated processed gene. Cell. 37:1984;457-468.
13. Fang Y., Sheffield L.G. Regulation of epidermal growth factor expression in mammary epithelial cells by a Yin-Yang-1-like element. J. Mol. Endocrinol. 20:1998;337-344.
14. Flanagan J.R., Becker K.G., Ennist D.L., Gleason S.L., Driggers P.H., Levi B.-Z., Apella E., Ozato K. Cloning of a negative transcription factor that binds to the upstream conserved region of Moloney murine leukemia virus. Mol. Cell. Biol. 12:1992;38-44.
15. Flusser G., Ginzburg V., Meyuhas O. Glucocorticoids induce transcription of ribosomal protein genes in rat liver. Mol. Cell. Endocrinol. 64:1989;213-222.
16. Frey A., Seifart K.H. Glucorticoids directly affect the synthesis of ribosomal RNA in rat liver cells. Mol. Cell. Endocrinol. 28:1982;161-172.
17. Fulton R., Birnie G.D., Knowler J.T. Post-transcriptional regulation of rat liver gene expression by glucocorticoids. Nucleic Acids Res. 13:1985;6467-6482.
18. Genuario R.R., Kelley D.E., Perry R.P. Comparative utilization of transcription factor GABP by the promoters of ribosomal protein genes rpL30 and rpL32. Gene Expression. 3:1993;279-288.
19. Glibetic M., Larson D.E., Rothblum L.I., Sells B.H. Dexamethasone stimulates rRNA gene transcription in rat myoblasts. Mol. Cell. Endocrinol. 94:1993;243-252.
20. Grange T., Martins de Sa C., Oddos J., Pictet R. Human mRNA polyadenylate binding protein: evolutionary conservation of a nucleic acid binding motif. Nucleic Acids Res. 15:1987;4771-4787.
21. Guo B., Odgren P.R., Van Wijnen A.J., Last T.J., Nickerson J., Penman S., Lian J.B., Stein J.L., Stein G.S. The nuclear matrix protein NMP-1 is the transcription factor YY1. Proc. Natl. Acad. Sci. USA. 92:1995;10526-10530.
22. Hariharan N., Kelley D.E., Perry R.P. Equipotent mouse ribosomal protein promoters have a similar architecture that includes internal sequence elements. Genes Dev. 3:1989;1789-1800.
23. Hariharan N., Kelley D.E., Perry R.P. δ a transcription factor that binds to downstream elements in several polymerase II promoters, is a functionally versatile zinc finger protein. Proc. Natl. Acad. Sci. USA. 88:1991;9799-9803.
24. Herruer M.H., Mager W.H., Woudt L.P., Nieuwint R.T.M., Wassenaar G.M., Groeneveld P., Planta R.J. Transcriptional control of yeast ribosomal protein synthesis during carbon-source upshift. Nucleic Acids Res. 15:1987;10133-10144.
25. Herruer M.H., Mager W.H., Raue H.A., Vreken P., Wilms E., Planta R.J. Mild temperature shock affects transcription of yeast ribosomal protein genes as well as the stability of their mRNAs. Nucleic Acids Res. 16:1988;7917-7929.
26. Huang S., Hershey J.W.B. Translational initiation factor expression and ribosomal protein gene expression are repressed coordinately but by different mechanisms in murine lymphosarcoma cells treated with glucocorticoids. Mol. Cell. Biol. 9:1989;3679-3684.
27. Jacobs F.A., Bird R.C., Sells B.H. Differentiation of rat myoblasts. Regulation of turnover of ribosomal proteins and their mRNAs. Eur. J. Biochem. 150:1985;255-263.
28. Jonat C., Rahmsdorf H.J., Park K.K., Cato A.C.B., Gebel S., Ponta H., Herrlich P. Antitumor promotion and antiinflammation: down-modulation of AP-1 (Fos/Jun) activity by glucocorticoid hormone. Cell. 62:1990;1189-1204.
29. Kamei Y., Xu L., Heinzel T., Torchia J., Kurokawa R., Gloss B., Lin S.C., Heyman R.A., Rose D.W., Glass C.K., Rosenfeld M.G. A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell. 85:1996;403-414.
30. Kim C.H., Warner J.R. Mild temperature shock alters the transcription of a discrete class of Saccharomyces cerevisiae genes. Mol. Cell. Biol. 3:1983;457-465.
31. Konagaya M., Konagaya Y., Friedman J.A., Max S.R. Nuclear glucocorticoid receptor binding in L6 skeletal muscle cells in culture. J. Steroid Biochem. 29:1988;685-689.
32. Lucibello F.C., Slater E.P., Jooss K.U., Beato M., Mueller R. Mutual transrepression of Fos and the glucocorticoid receptor: involvement of a functional domain in Fos which is absent in FosB. EMBO J. 9:1990;2827-2834.
33. Macleod K., Leprince D., Stehelin D. The ets gene family. Trends Biochem. Sci. 17:1992;251-256.
34. Mahajan P.B., Thompson E.A. Hormonal regulation of transcription of rDNA. Purification and characterization of the hormone-regulated transcription factor IC. J. Biol. Chem. 265:1990;16225-16233.
35. Mahajan P.B., Thompson E.A. Copurification of RNA polymerase I and the glucocorticoid-regulated transcription factor IC. Protein Exp. Purif. 3:1992;410-416.
36. McEwan I.J., Dahlman-Wright K., Amlof T., Ford J., Wright A.P.H., Gustafsson J.-A. Mechanisms of transcription activation by nuclear receptors: studies on the human glucocorticoid receptor tau 1 transactivation domain. Mutat. Res. 333:1995;15-22.
37. McEwan I.J., Wright A.P.H., Dahlman-Wright K., Carlstedt-Duke J., Gustafsson J.-A. Direct interaction of the (1 transactivation domain of the human glucocorticoid receptor with the basal transcriptional machinery. Mol. Cell. Biol. 13:1993;399-407.
38. Meyuhas O., Thompson E.A.J.r., Perry R.P. Glucocorticoids selectively inhibit translation of ribosomal protein mRNAs in P1798 lymphosarcoma cells. Mol. Cell. Biol. 7:1987;2691-2699.
39. Meyuhas O., Baldin V., Bouche G., Amaldi F. Glucocorticoids repress ribosome biosynthesis in lymphosarcoma cells by affecting gene expression at the level of transcription, posttranscription and translation. Biochim. Biophys. Acta. 1049:1990;38-44.
40. Misseyanni A., Scheidereit C., Kalff M., Beato M. Neither the endogenous nor a functional steroid hormone receptor binding site transactivate the ribosomal RNA gene promoter in vitro. J. Steroid Biochem. Mol. Biol. 39:1991;409-418.
41. Moura-Neto R., Dudov K.P., Perry R.P. An element downstream of the cap site is required for transcription of the gene encoding mouse ribosomal protein L32. Proc. Natl. Acad. Sci. USA. 86:1989;3997-4001.
42. Paek I., Axel R. Glucocorticoids enhance stability of human growth hormone mRNA. Mol. Cell. Biol. 7:1987;1496-1507.
43. Park K., Atchison M.L. Isolation of a candidate repressor/activator, NF-E1 (YY1/δ), that binds to the immunoglobulin κ 3′ enhancer and the immunoglobulin heavy-chain μE1 site. Proc. Natl. Acad. Sci. USA. 88:1991;9804-9808.
44. Raghow R., Gossage D., Kang A.H. Pretranslational regulation of type I collagen, fibronectin, and a 50-kilodalton noncollagenous extracellular protein by dexamethasone in rat fibroblasts. J. Biol. Chem. 261:1986;4677-4684.
45. Renkawitz R., Kaltschmidt C., Leers J., Martin B., Muller M., Eggert M. Enhancement of nuclear receptor transcriptional signalling. J. Steroid. Biochem. Mol. Biol. 56:1996;39-45.
46. Riggs K.J., Merrell K.T., Wilson G., Calame K. Common factor 1 is a transcriptional activator which binds in the c-myc promoter, the skeletal α-actin promoter, and the immunoglobulin heavy chain enhancer. Mol. Cell. Biol. 11:1991;1765-1769.
47. Safrany G., Perry R.P. Characterization of the mouse gene that encodes the (δYY1/NF-E1/UCRBP transcription factor. Proc. Natl. Acad. Sci. USA. 90:1993;5559-5563.
48. Seto E., Shi Y., Shenk T. YY1 is an initiator sequence-binding protein that directs and activates transcription in vitro. Nature. 354:1991;241-245.
49. Shemshedini L., Knauthe R., Sassone-Corsi P., Pornon A., Gronemeyer H. Cell-specific inhibitory and stimulatory effects of Fos and Jun on transcription activation by nuclear receptors. EMBO J. 10:1991;3839-3849.
50. Shi Y., Seto E., Chang L.-S., Shenk T. Transcriptional repression by YY1, a human GLI-Kruppel-related protein, and relief of repression by adenovirus E1A protein. Cell. 67:1991;377-388.
51. Thompson C.C., Brown T.A., McKnight S.L. Convergence of Ets- and Notch-related structural motifs in a heteromeric DNA binding complex. Science. 253:1991;762-768.
52. Wagner M., Perry R.P. Characterization of the multigene family encoding the mouse S16 ribosomal protein: strategy for distinguishing an expressed gene from its processed pseudogene counterparts by an analysis of total genomic DNA. Mol. Cell. Biol. 5:1985;3560-3576.
53. Webb M.L., Mealey-Cavender J.F., Jacob S.T. Glucocorticoid induced stimulation of ribosomal gene transcription in rat hepatoma cells is mediated by modification of RNA polymerase I or an associated factor. Mol. Endocrinol. 3:1989;1861-1868.
54. Wiedemann L.M., Perry R.P. Characterization of the expressed gene and several processed pseudogenes for the mouse ribosomal protein L30 gene family. Mol. Cell. Biol. 4:1984;2518-2528.
55. Yang-Yen H.F., Chambard J.C., Sun Y.L., Smeal T., Schmidt T.J., Drouin J., Karin M. Transcriptional interference between c-Jun and the glucocorticoid receptor: mutual inhibition of DNA binding due to direct protein-protein interaction. Cell. 62:1990;1205-1215.
56. Yoganathan T., Sells B.H. A downstream sequence of the rpL32 promoter competes with the glucocorticoid responsive element for a protein factor. Biochem. Cell Biol. 70:1992;787-791.
57. Yoganathan T., Bhat N.K., Sells B.H. A positive regulator of the ribosomal protein gene, β factor, belongs to the Ets oncoprotein family. Biochem. J. 287:1992;349-353.
58. Yoganathan T., Horikoshi M., Hasegawa S., Roeder R.G., Sells B.H. Yeast transcription factor IID participates in cell-free transcription of a mammalian ribosomal protein TATA-less promoter. Biochem. J. 285:1992;721-723.
59. Zahradka P., Larson D.E., Sells B.H. Post-transcriptional regulation of 5S rRNA synthesis following myoblast differentiation. Eur. J. Biochem. 184:1989;261-266.
60. Zeiner M., Gehring U. A protein that interacts with members of the nuclear hormone receptor family: identification and cDNA cloning. Proc. Natl. Acad. Sci. USA. 92:1995;11465-11469.