Purification and Characterization of an Erythroid Cell-Specific Factor That Binds the Murine α- and β-Globin Genes

LITERATURE CITED

• Baeuerle, P. A., and D. Baltimore. 1988. IkB: a specific inhibitor of the NF-kB transcription factor. Science 242:540–546.
   PubMed Web of Science ®Google Scholar
• Barnhart, K. M., C. G. Kim, S. S. Banerji, and M. Sheffery. 1988. Identification and characterization of multiple erythroid cell proteins that interact with the promoter of the murine α-globin gene. Mol. Cell. Biol. 8:3215–3226.
   PubMed Web of Science ®Google Scholar
• Bradford, M. M.. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal. Biochem. 72:248–254.
   PubMed Web of Science ®Google Scholar
• Chambers, L., J. Frampton, P. Goldfarb, N. Affara, W. McBain, and P. R. Harrison. 1986. The structure of the mouse glutathione peroxidase gene: the selenocycteine in the active site is encoded by the “termination” codon TGA. EMBO J. 5:1221–1227.
   PubMed Web of Science ®Google Scholar
• Chodosh, L. A., R. W. Carthew, and P. A. Sharp. 1986. A single polypeptide possesses the binding and transcription activities of the adenovirus major late transcription factor. Mol. Cell. Biol. 6:4723–4733.
   PubMed Web of Science ®Google Scholar
• Chretien, S., A. Dubart, D. Beaupain, N. Raich, B. Grandchamp, J. Rosa, M. Goossens, and P.-H. Romeo. 1988. Alternative transcription and slicing of the human porphobilinogen deaminase gene result either in tissue-specific or in housekeeping expression. Proc. Natl. Acad. Sci. USA 85:6–10.
   PubMed Web of Science ®Google Scholar
• Cohen, R. B., M. Sheffery, and C. G. Kim. 1986. Partial purification of a nuclear protein that binds to the CCAAT box of the mouse α1globin gene. Mol. Cell. Biol. 6:821–832.
   PubMed Web of Science ®Google Scholar
• deBoer, E., M. Antoniou, V. Mignotte, L. Wall, and F. Grosveld. 1988. The human β-globin promoter; nuclear protein factors and erythroid-specific induction of transcription. EMBO J. 7:4203–4212.
   PubMedGoogle Scholar
• Dignam, J. D., P. L. Martin, B. S. Shastry, and R. G. Roeder. 1983. Eukaryotic gene transcription with purified components. Methods Enzymol. 101:582–598.
   PubMed Web of Science ®Google Scholar
• Evans, T., M. Reitman, and G. Felsenfeld. 1988. An erythrocytespecific DNA binding factor recognizes a regulatory sequence common to all chicken globin genes. Proc. Natl. Acad. Sci. USA 85:5976–5980.
   PubMed Web of Science ®Google Scholar
• Galson, D. L., and D. E. Housman. 1988. Detection of two tissue-specific DNA-binding proteins with affinity for sites in the mouse β-globin intervening sequence 2. Mol. Cell. Biol. 8:381–392.
   PubMedGoogle Scholar
• Gumucio, D. L., K. L. Rood, T. A. Gray, M. F. Riordan, C. I. Sartor, and F. S. Collins. 1988. Nuclear proteins that bind the human gamma γ-globin gene promoter: alterations in binding produced by point mutations associated with hereditary persistence of fetal hemoglobin. Mol. Cell. Biol. 8:5310–5322.
   PubMed Web of Science ®Google Scholar
• Hatamochi, A., P. T. Golumbek, E. van Schaftingen, and B. de Crombrugghe. 1988. A CCAAT DNA binding factor consisting of two different components that are both required for DNA binding. J. Biol. Chem. 263:5940–5947.
   PubMedGoogle Scholar
• Kadonaga, J. T., and R. Tjian. 1986. Affinity purification of sequence-specific DNA binding proteins. Proc. Natl. Acad. Sci. USA 83:5889–5893.
   PubMed Web of Science ®Google Scholar
• Kemper, B., P. D. Jackson, and G. Felsenfeld. 1987. Proteinbinding sites within the 5′ DNase I-hypersensitive region of the chicken αD-globin gene. Mol. Cell. Biol. 7:2059–2069.
   PubMedGoogle Scholar
• Kim, C. G., K. M. Barnhart, and M. Sheffery. 1988. Purification of multiple erythroid cell proteins that bind the promoter of the α-globin gene. Mol. Cell. Biol. 8:4270–4281.
   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
• Mantovani, R., N. Malgaretti, S. Nicolis, B. Giglioni, P. Comi, N. Cappedini, M. T. Bertero, F. Caligaris-Cappio, and S. Ottolenghi. 1988. An erythroid-specific nuclear factor binding to the proximal CACCC box of the β-globin gene promoter. Nucleic Acids Res. 16:4299–4313.
   PubMed Web of Science ®Google Scholar
• Nishioka, Y., and P. Leder. 1979. The complete sequence of a chromosomal mouse α-globin gene reveals elements conserved throughout vertebrate evolution. Cell 18:875–882.
   PubMed Web of Science ®Google Scholar
• Perkins, N. D., R. H. Nicolas, M. A. Plumb, and G. H. Goodwin. 1989. The purification of an erythroid protein which binds to enhancer and promoter elements of haemoglobin genes. Nucleic Acids Res. 17:1299–1314.
   PubMedGoogle Scholar
• Plumb, M., J. Frampton, H. Wainwright, M. Walker, K. Macleod, G. Goodwin, and P. Harrison. 1989. GATAAG; a ciscontrol region binding an erythroid-specific nuclear factor with a role in globin and non-globin gene expression. Nucleic Acids Res. 17:73–92.
   PubMedGoogle Scholar
• Reitman, M., and G. Felsenfeld. 1988. Mutational analysis of the chicken β-globin enhancer reveals two positive-acting domains. Proc. Natl. Acad. Sci. USA 85:6267–6271.
   PubMedGoogle Scholar
• Sheffery, M., P. A. Marks, and R. A. Rifkind. 1984. Gene expression in murine erythroleukemia cells: transcriptional control and chromatin structure of the α1-globin gene. J. Mol. Biol. 172:417–436.
   PubMedGoogle Scholar
• Super-Furga, G., A. Barberis, G. Schaffner, and M. Busslinger. 1988. The ‒117 mutation in Greek HPFH affects the binding of three nuclear factors to the CCAAT region of the gamma-globin gene. EMBO J. 7:3099–3107.
   PubMedGoogle Scholar
• Wall, L., E. deBoer, and F. Grosveld. 1988. The human β-globin gene 3′ enhancer contains multiple binding sites for an erythroid-specific protein. Genes Dev. 2:1089–1100.
   PubMed Web of Science ®Google Scholar