Glucose-Regulated Protein (GRP94 and GRP78) Genes Share Common Regulatory Domains and Are Coordinately Regulated by Common trans-Acting Factors

LITERATURE CITED

• Baez, M., D. R. Sargan, A. Elbrecht, M. S. Kulomaa, T. Zarucki-Schulz, M.-J. Tsai, and B. W. O'Malley. 1987. Steroid hormone regulation of the gene encoding the chicken heat shock protein HSP108. J. Biol. Chem. 262:6582–6588.
   PubMedGoogle Scholar
• Bergsma, D. J., K. S. Chang, and R. J. Schwartz. 1985. Novel chicken actin gene: third cytoplasmic isoform. Mol. Cell. Biol. 5:1151–1162.
   PubMedGoogle Scholar
• Bole, D. G., L. M. Hendershot, and J. F. Kearney. 1986. Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in non-secreting and secreting hybridomas. J. Cell Biol. 102:1558–1566.
   PubMed Web of Science ®Google Scholar
• Catelli, M. G., N. Binart, I. Jung-Testas, J. M. Renoir, E. E. Baulieu, J. R. Feramisco, and W. J. Welch. 1985. The common 90-kd protein component of non-transformed ‘8S’ steroid receptors is a heat shock protein. EMBO J. 4:3131–3135.
   PubMed Web of Science ®Google Scholar
• Chang, S. C., S. K. Wooden, T. Nakaki, Y. K. Kim, A. Y. Lin, L. Kung, J. W. Attenello, and A. S. Lee. 1987. Rat gene encoding the 78-kDa glucose-regulated protein GRP78: its regulatory sequences and the effect of protein glycosylation on its expression. Proc. Natl. Acad. Sci. USA 84:680–684.
   PubMed Web of Science ®Google Scholar
• Day, L., A. J. Hirst, E. C. Lai, M. L. Mace, and S. L. Woo. 1981. 5′ domain and nucleotide sequence of an adult chicken chromosomal β-globin gene. Biochemistry 20:2091–2098.
   PubMedGoogle Scholar
• Dierks, P., A. V. Ooyen, M. D. Cochran, C. Dobkin, J. Reiser, and C. Weissmann. 1983. Three regions upstream from the cap site are required for efficient and accurate transcription of the rabbit β-globin gene in mouse 3T6 cells. Cell 32:695–706.
   PubMed Web of Science ®Google Scholar
• Drummond, I. A. S., A. S. Lee, E. Resendez, Jr., and R. A. Steinhardt. 1987. Depletion of intracellular calcium stores by calcium ionophore A23187 induces the genes for the glucose-regulated proteins in hamster fibroblasts. J. Biol. Chem. 262:12801–12805.
   PubMedGoogle Scholar
• Feinberg, A. P., and B. Vogelstein. 1983. A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132:6–13.
   PubMed Web of Science ®Google Scholar
• Fried, M., and D. Crothers. 1981. Equilibrium and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis. Nucleic Acids Res. 9:6505–6525.
   PubMed Web of Science ®Google Scholar
• Gorman, C. M., L. F. Moffat, and B. H. Howard. 1982. Recombinant genomes which express chloramphenicol acetyl-transferase in mammalian cells. Mol. Cell. Biol. 2:1044–1051.
   PubMed Web of Science ®Google Scholar
• Hendershot, L. M., J. Ting, and A. S. Lee. 1988. Identity of the immunoglobulin heavy-chain-binding protein with the 78,000-dalton glucose-regulated protein and the role of posttranslational modifications in its binding function. Mol. Cell. Biol. 8:4250–4256.
   PubMed Web of Science ®Google Scholar
• Kim, Y. K., and A. S. Lee. 1987. Transcriptional activation of the glucose-regulated protein genes and their heterologous fusion genes by β-mercaptoethanol. Mol. Cell. Biol. 7:2974–2976.
   PubMedGoogle Scholar
• Kleinsek, D. A., W. G. Beattie, M.-J. Tsai, and B. W. O'Malley. 1986. Molecular cloning of a steroid-regulated 108 k heat shock protein gene from hen oviduct. Nucleic Acids Res. 14:10053–10069.
   PubMedGoogle Scholar
• Koch, G., M. Smith, D. Macer, P. Webster, and R. Mortara. 1986. Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin. J. Cell Sci. 86:217–232.
   PubMed Web of Science ®Google Scholar
• Koch, G. L. E.. 1987. Reticuloplasmins: a novel group of proteins in the endoplasmic reticulum. J. Cell Sci. 87:491–492.
   PubMedGoogle Scholar
• Koch, G. L. E., D. R. J. Macer, and F. B. P. Wooding. 1988. Endoplasmin is a reticuloplasmin. J. Cell Sci. 90:485–491.
   PubMedGoogle Scholar
• Koch, G. L. E., M. J. Smith, and R. A. Mortara. 1985. An abundant, ubiquitous glycoprotein (GP100) in nucleated mammalian cells. FEBS Lett. 179:294–298.
   PubMedGoogle Scholar
• Kozutsumi, Y., M. Segal, K. Normington, M.-J. Gething, and J. Sambrook. 1988. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature (London) 332:462–464.
   PubMed Web of Science ®Google Scholar
• Kulomaa, M. S., N. L. Weigel, D. A. Kleinsek, W. G. Beattie, O. M. Conneely, C. March, T. Zarucki-Schulz, W. T. Schrader, and B. W. O'Malley. 1986. Amino acid sequence of a chicken heat shock protein derived from the complementary DNA nucleotide sequence. Biochemistry 25:6244–6251.
   PubMedGoogle Scholar
• Lawn, R. M., E. F. Fritsch, R. C. Parker, G. Blake, and T. Maniatis. 1978. The isolation and characterization of linked δ-and β-globin genes from a cloned library of human DNA. Cell 15:1157–1174.
   PubMed Web of Science ®Google Scholar
• Lee, A. S.. 1981. The accumulation of three specific proteins related to glucose-regulated proteins in a temperature-sensitive hamster mutant cell line K12. J. Cell Physiol. 106:119–125.
   PubMed Web of Science ®Google Scholar
• Lee, A. S.. 1987. Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells. Trends Biochem. Sci. 12:20–23.
   Web of Science ®Google Scholar
• Lee, A. S., J. Bell, and J. Ting. 1984. Biochemical characterization of the 94- and 78-kilodalton glucose-regulated proteins in hamster fibroblasts. J. Biol. Chem. 259:4616–4621.
   PubMed Web of Science ®Google Scholar
• Lee, A. S., A. M. Delegeane, V. Baker, and P. C. Chow. 1983. Transcriptional regulation of two genes specifically induced by glucose starvation in a hamster mutant fibroblast cell line. J. Biol. Chem. 258:597–603.
   PubMedGoogle Scholar
• Lewis, M. J., S. J. Turco, and M. Green. 1985. Structure and assembly of the endoplasmic reticulum: biosynthetic sorting of endoplasmic reticulum proteins. J. Biol. Chem. 260:6926–6931.
   PubMedGoogle Scholar
• Lin, A. Y., S. C. Chang, and A. S. Lee. 1986. A calcium ionophore-inducible cellular promoter is highly active and has enhancerlike properties. Mol. Cell. Biol. 6:1235–1243.
   PubMedGoogle Scholar
• Lin, A. Y., and A. S. Lee. 1984. Induction of two genes by glucose starvation in hamster fibroblasts. Proc. Natl. Acad. Sci. USA 81:988–992.
   PubMed Web of Science ®Google Scholar
• Maxam, A. M., and W. Gilbert. 1980. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 65:499–560.
   PubMedGoogle Scholar
• Mazzarella, R. A., and M. Green. 1987. ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90 kDa heat shock protein (hsp90) and the 94 kDa glucose regulated protein (GRP94). J. Biol. Chem. 262:8875–8883.
   PubMed Web of Science ®Google Scholar
• Munro, S., and H. R. B. Pelham. 1986. An HSP70-like protein in the ER: identity with the 78 kD glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46:291–300.
   PubMed Web of Science ®Google Scholar
• Nakaki, T., R. J. Deans, and A. S. Lee. 1989. Enhanced transcription of the 78,000-dalton glucose-regulated protein (GRP78) gene and association of GRP78 with immunoglobulin light chains in a nonsecreting B-cell myeloma line (NS-1). Mol. Cell. Biol. 9:2233–2238.
   PubMed Web of Science ®Google Scholar
• Reinberg, D., and R. G. Roeder. 1987. Factors involved in specific transcription by mammalian RNA polymerase II: purification and functional analysis of initiation factors IIB and IIE. J. Biol. Chem. 262:3310–3321.
   PubMed Web of Science ®Google Scholar
• Resendez, E., Jr., J. W. Attenello, A. Grafsky, C. S. Chang, and A. S. Lee. 1985. Calcium ionophore A23187 induces expression of glucose-regulated genes and their heterologous fusion genes. Mol. Cell. Biol. 5:1212–1219.
   PubMed Web of Science ®Google Scholar
• Resendez, E., Jr., S. K. Wooden, and A. S. Lee. 1988. Identification of highly conserved regulatory domains and protein-binding sites in the promoters of the rat and human genes encoding the stress-inducible 78-kilodalton glucose-regulated protein. Mol. Cell. Biol. 8:4579–4584.
   PubMedGoogle Scholar
• Sanchez, E. R., D. O. Toft, M. J. Schlesinger, and W. B. Pratt. 1985. Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein. J. Biol. Chem. 260:12398–12401.
   PubMed Web of Science ®Google Scholar
• Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463–5467.
   PubMed Web of Science ®Google Scholar
• Shapiro, D. J., P. A. Sharp, W. W. Wahli, and M. J. Keller. 1988. A high efficiency HeLa cell nuclear transcription extract. DNA 7:47–55.
   PubMedGoogle Scholar
• Shiu, R. P. C., J. Pouyssegur, and I. Pastan. 1977. Glucose depletion accounts for the induction of two transformationsensitive membrane proteins in Rous sarcoma virus-transformed chick embryo fibroblasts. Proc. Natl. Acad. Sci. USA 74:3840–3844.
   PubMed Web of Science ®Google Scholar
• Smith, M. J., and G. L. E. Koch. 1987. Isolation and identification of partial cDNA clones for endoplasmin, the major glycoprotein of mammalian endoplasmic reticulum. J. Mol. Biol. 194:345–347.
   PubMedGoogle Scholar
• Sorger, P. K., and H. R. B. Pelham. 1987. The glucose-regulated protein grp94 is related to heat shock protein hsp90. J. Mol. Biol. 194:341–344.
   PubMedGoogle Scholar
• Ting, J., and A. S. Lee. 1988. Human gene encoding the 78,000 dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation. DNA 7:275–286.
   PubMedGoogle Scholar
• Ting, J., S. K. Wooden, R. Kriz, K. Kelleher, R. J. Kaufman, and A. S. Lee. 1987. The nucleotide sequence encoding the hamster 78 kDa glucose-regulated protein (GRP78) and its conservation between hamster and rat. Gene 55:147–152.
   PubMed Web of Science ®Google Scholar
• Wasylyk, B., and P. Chambon. 1981. A T to A base substitution and small deletions in the conalbumin TATA box drastically decrease specific in vitro transcription. Nucleic Acids Res. 9:1813–1824.
   PubMed Web of Science ®Google Scholar
• Yamamoto, K. K., G. A. Gonzalez, W. H. Biggs III, and M. R. Montminy. 1988. Phosphorylation-induced binding and transcriptional efficacy of nuclear factor CREB. Nature (London) 334:494–498.
   PubMedGoogle Scholar
• Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectors. Gene 33:103–119.
   PubMed Web of Science ®Google Scholar
• Zarucki-Schulz, T., S. Y. Tsai, K. Itakura, X. Soberon, R. B. Wallace, M.-J. Tsai, S. L. C. Woo, and B. W. O'Malley. 1982. Point mutagenesis of the ovalbumin gene promoter sequence and its effect on in vitro transcription. J. Biol. Chem. 257:11070–11077.
   PubMedGoogle Scholar