Nonexpression of a Major Heat Shock Gene in Mouse Plasmacytoma MPC-11

LITERATURE CITED

• Abrams, H. D., Rohrschneider L. R., and Eisenman R. N.. 1982. Nuclear location of the putative transforming protein of avian myelocytomatosis virus. Cell 29:427–439.
   PubMed Web of Science ®Google Scholar
• Atkinson, B. G., Cunningham T., Dean R. L., and SomerviUe M.. 1982. Comparison of the effects of heat-shock and metal ion stress on gene expression in cells undergoing myogenesis. Can. J. Biochem. Cell Biol. 61:404–413.
   Google Scholar
• Benoit, C, and Chambon P.. 1980. Deletions covering the putative promoter region of early mRNAs of simian virus 40 do not abolish T-antigen expression. Proc. Natl. Acad. Sci. U.S.A. 77:3865–3869.
   PubMedGoogle Scholar
• Bensaude, O., Babinet C., Morange M., and Jacob F.. 1983. Heat-shock proteins, first major products of zygotic gene activity in mouse embryo. Nature (London) 305:331–333.
   PubMed Web of Science ®Google Scholar
• Bensaude, O., and Morange M.. 1983. Spontaneous high expression of heat shock proteins in embryonal carcinoma cells and ectoderm from day 8 mouse embryo. EMBO J. 2:173–177.
   PubMedGoogle Scholar
• Berk, A. J., and Sharp P. A.. 1977. Sizing and mapping of early adenovirus mRNAs by gel electrophoresis of SI endonuclease-digested hybrids. Cell 12:721–732.
   PubMed Web of Science ®Google Scholar
• Chamberlain, J. P. 1979. Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate. Anal. Biochem. 98:132–135.
   PubMed Web of Science ®Google Scholar
• Corces, V. A., PeUicer A., Axel R., and Meselson M.. 1981. Integration, transcription and control of a Drosophila heat-shock gene in mouse cells. Proc. Natl. Acad. Sci. U.S.A. 78:7038–7042.
   PubMed Web of Science ®Google Scholar
• Donner, P., Greiser-Wilke I., and Moelling K.. 1982. Nuclear localization and DNA binding of the transforming gene product of avian myelocytomatosis virus. Nature (London) 296:262–266.
   PubMed Web of Science ®Google Scholar
• Duesberg, P. H. 1983. Retroviral transforming genes in normal cells. Nature (London) 304:219–226.
   PubMed Web of Science ®Google Scholar
• Gross-BeUard, M., Oudet P., and Chambon P.. 1973. Isolation of high-molecular-weight DNA from mammalian cells. Eur. J. Biochem. 36:32–38.
   PubMedGoogle Scholar
• Feldman, L. T., and Nevins J. R.. 1983. Localization of the adenovirus ElAa protein, a positive-acting transcriptional factor, in infected cells infected cells [sic]. Mol. Cell. Biol. 3:829–838.
   PubMedGoogle Scholar
• Imperiale, M. J., Kao H.-T., Feldman L. T., Nevins J. R., and Strickland S.. 1984. Common control of the heat shock gene and early adenovirus genes: evidence for a cellular ElA-like activity. Mol. Cell. Biol. 4:867–374.
   PubMed Web of Science ®Google Scholar
• Jeffrey, J. S., Roberts B. F., and Paterson B. M.. 1982. Determination of the organization and identity of eukaryotic genes utilizing cell-free translation systems, p. 103–117. In Setlow J. K., and Hollaender A. (ed.), Genetic Engineering, vol. 4. Plenum Publishing Corp., New York.
   Google Scholar
• Kelley, P. M., and Schlesinger M. J.. 1978. The effect of amino acid analogues and heat-shock on gene expression in chicken embryo fibroblasts. Cell 15:1277–1286.
   PubMed Web of Science ®Google Scholar
• Kelley, P. M., and Schlesinger M. J.. 1982. Antibodies to two major chicken heat shock proteins cross-react with similar proteins in widely divergent species. Mol. Cell. Biol. 2:267–274.
   PubMed Web of Science ®Google Scholar
• Kingston, R. E., Baldwin A. S., Jr., and Sharp P. A.. 1984. Regulation of heat-shock protein 70 gene expression by c-myc. Nature (London) 312:280–282.
   PubMed Web of Science ®Google Scholar
• Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680–685.
   PubMed Web of Science ®Google Scholar
• Land, H., Parada L. F., and Weinberg R. A.. 1983. Tumorigenic conversion of primary embryo fibroblasts requires at least two cooperating oncogenes. Nature (London) 304:596–602.
   PubMed Web of Science ®Google Scholar
• Leff, T., Elkaim R., Goding C. R., Jalinot P., Sassone-Corsi P., Perricaudet M., Kedinger C., and Chambon P.. 1984. Individual products of the adenovirus 12S and 13S Ela mRNAs stimulate viral EIHa and EHI expression at the transcriptional level. Proc. Natl. Acad. Sci. U.S.A. 81:4381–4385.
   PubMedGoogle Scholar
• Loomis, W. F., and Wheeler S. A.. 1982. Chromatin-associated heat-shock proteins of Dictyostelium. Dev. Biol. 90:412–418.
   PubMed Web of Science ®Google Scholar
• Lowe, D. G., and Moran L. A.. 1984. Proteins related to the mouse L cell major heat shock protein are synthesized in the absence of heat-shock gene expression. Proc. Natl. Acad. Sci. U.S.A. 81:2317–2321.
   PubMed Web of Science ®Google Scholar
• Marcu, K. B., Harris L. J., Stanton L. W., Erikson J., Watt R., and Croce C. M.. 1983. Transcriptionally active c-myc oncogene is contained within NIARD, a DNA sequence associated with chromosome translocations in B cell neoplasia. Proc. Natl. Acad. Sci. U.S.A. 80:519–523.
   PubMed Web of Science ®Google Scholar
• Moran, L. A., Chauvin M., Kennedy M. E., Kari M., Lowe D. G., Nicholson R. C., and Perry M. D.. 1983. The major heat-shock protein (hsp 70) gene family: related sequences in mouse, Drosophila and yeast. Can. J. Biochem. Cell Biol. 61:488–499.
   PubMedGoogle Scholar
• Morange, M., Diu A., Bensaude O., and Babinet C.. 1984. Altered expression of heat shock proteins in embryonal carcinoma and mouse early embryonic cells. Mol. Cell. Biol. 4:730–735.
   PubMedGoogle Scholar
• Morimoto, R., and Fodor E.. 1984. Cell-specific expression of heat shock proteins in chicken reticulocytes and lymphocytes. J. Cell Biol. 99:1316–1323.
   PubMed Web of Science ®Google Scholar
• Nevins, J. R. 1981. Mechanism of activation of early viral transcription by the adenovirus El A gene product. Cell 26:213–219.
   PubMed Web of Science ®Google Scholar
• Nevins, J. R. 1982. Induction of the synthesis of a 70,000 dalton mammalian heat-shock protein by the adenovirus E1A gene product. Cell 29:913–919.
   PubMed Web of Science ®Google Scholar
• Parker, C. S., and Topol J.. 1984. A Drosophila RNA polymerase II transcription factor binds to the regulatory site of an hsp 70 gene. Cell 37:273–283.
   PubMed Web of Science ®Google Scholar
• Pelham, H. R. B. 1982. A regulatory upstream promoter element in the Drosophila hsp 70 heat shock gene. Cell 30:517–528.
   PubMed Web of Science ®Google Scholar
• Ralston, R., and Bishop J. M.. 1983. The protein products of the myc and myb oncogenes and adenovirus E1A are structurally related. Nature (London) 306:803–805.
   PubMedGoogle Scholar
• Rigby, P. W. J., Dieckmann M., Rhodes C., and Berg P.. 1977. Labelling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I. J. Mol. Biol. 113:237–251.
   PubMed Web of Science ®Google Scholar
• Singh, M. K., and Yu J.. 1984. Accumulation of a heat-shocklike protein during differentiation of human erythroid cell line K 562. Nature (London) 309:631–633.
   PubMedGoogle Scholar
• Stanton, C. W., Young J. Q., Eckhardt C. A., Harrison L. J., Birshtein B. K., and Marcu K. B.. 1983. Transcriptionally active c-myc oncogene is contained within NIARD, a DNA sequence associated with chromosome translocations in B-cell neoplasia. Proc. Natl. Acad. Sci. U.S.A. 80:519–523.
   PubMedGoogle Scholar
• Voellmy, R., and Bromley P. A.. 1982. Massive heat-shock polypeptide synthesis in late chicken embryos: convenient system for study of protein synthesis in highly differentiated organisms. Mol. Cell. Biol. 2:479–483.
   PubMedGoogle Scholar
• Wahl, G. M., Stern M., and Stark G. R.. 1979. Efficient transfer of large DNA fragment from agarose gels to diazobenzyloxy-methyl-paper and rapid hybridization using dextran sulfate. Proc. Natl. Acad. Sci. U.S.A. 76:3683–3687.
   PubMed Web of Science ®Google Scholar
• Wang, C, Gower R. H., and Lazarides E.. 1981. Heat-shock proteins are methylated in avian and mammalian cells. Proc. Natl. Acad. Sci. U.S.A. 78:3531–3535.
   PubMed Web of Science ®Google Scholar
• Wu, C. 1984. Two protein binding sites in chromatin implicated in activation of heat-shock gene. Nature (London) 309:229–234.
   PubMed Web of Science ®Google Scholar
• Wu, C. 1984. Activating protein factor binds in vitro to upstream control sequences in heat-shock gene chromatin. Nature (London) 311:81–84.
   PubMed Web of Science ®Google Scholar