Promoter-selective properties of the TBP-related factor TRF1

Science

Volumn 288, Issue 5467, 2000, Pages 867-870

  Holmes, Michael C ^a   Tjian, Robert ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYRIBONUCLEASE I; TATA BINDING PROTEIN;

ARTICLE; DROSOPHILA; EMBRYO DEVELOPMENT; IMMUNOPRECIPITATION; NONHUMAN; POLYTENE CHROMOSOME; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN BINDING; PROTEIN EXPRESSION; RNA ANALYSIS; TRANSCRIPTION REGULATION;

ANIMALS; CELL LINE; DNA; DNA FOOTPRINTING; DNA-BINDING PROTEINS; DROSOPHILA; DROSOPHILA PROTEINS; GENE EXPRESSION REGULATION; GENES, INSECT; GENES, REPORTER; INSECT PROTEINS; MEMBRANE TRANSPORT PROTEINS; PROMOTER REGIONS (GENETICS); RECOMBINANT PROTEINS; TATA BOX BINDING PROTEIN-LIKE PROTEINS; TATA-BOX BINDING PROTEIN; TRANSCRIPTION FACTOR TFIIA; TRANSCRIPTION FACTOR TFIIB; TRANSCRIPTION FACTOR TFIID; TRANSCRIPTION FACTORS; TRANSCRIPTION FACTORS, TFII; TRANSCRIPTION, GENETIC; TRANSFECTION;

METAZOA;

EID: 0034608084     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.288.5467.867     Document Type: Article

References (26)

1. C. S. Hill and R. Treisman, Cell 80, 199 (1995); M. Mannervik et al., Science 284, 606 (1999); K. Struhl, Cell 98, 1 (1999).
2. C. S. Hill and R. Treisman, Cell 80, 199 (1995); M. Mannervik et al., Science 284, 606 (1999); K. Struhl, Cell 98, 1 (1999).
3. C. S. Hill and R. Treisman, Cell 80, 199 (1995); M. Mannervik et al., Science 284, 606 (1999); K. Struhl, Cell 98, 1 (1999).
4. T. E. Crowley et al., Nature 361, 557 (1993).
5. S. K. Hansen et al., Cell 91, 71 (1997).
6. 32P]deoxycytidine triphosphate and then used to probe DNA hybridization blots containing restriction fragments of the tudor and AntP1 promoters.
7. B. P. England, U. Heberlein, R. Tjian, J. Biol. Chem. 265, 5086 (1990).
8. T. A. Bunch, Y. Grinblat, L. S. Goldstein, Nucleic Acids Res. 16, 1043 (1988).
9. M. C. Holmes and R. Tjian, unpublished data.
10. Y. Sadovsky et al., Mol. Cell. Biol. 15, 1554 (1995); J. Colgan and J. L. Manley, Genes Dev. 6, 304 (1992).
11. Y. Sadovsky et al., Mol. Cell. Biol. 15, 1554 (1995); J. Colgan and J. L. Manley, Genes Dev. 6, 304 (1992).
12. S. Takada and R. Tjian, unpublished data.
13. M. C. Holmes, P. Hurban, K. P. White, R. Tjian, unpublished data.
14. M. D. Rabenstein et al., Proc. Natl. Acad. Sci. U.S.A. 96, 4791 (1999); E. Maldonado, J. Biol. Chem. 274, 12963 (1999); T. Ohbayashi, Y. Makino, T. Tamura, Nucleic Acids Res. 27, 750 (1999); E. Wieczorek et al., Nature 393, 187 (1998).
15. M. D. Rabenstein et al., Proc. Natl. Acad. Sci. U.S.A. 96, 4791 (1999); E. Maldonado, J. Biol. Chem. 274, 12963 (1999); T. Ohbayashi, Y. Makino, T. Tamura, Nucleic Acids Res. 27, 750 (1999); E. Wieczorek et al., Nature 393, 187 (1998).
16. M. D. Rabenstein et al., Proc. Natl. Acad. Sci. U.S.A. 96, 4791 (1999); E. Maldonado, J. Biol. Chem. 274, 12963 (1999); T. Ohbayashi, Y. Makino, T. Tamura, Nucleic Acids Res. 27, 750 (1999); E. Wieczorek et al., Nature 393, 187 (1998).
17. M. D. Rabenstein et al., Proc. Natl. Acad. Sci. U.S.A. 96, 4791 (1999); E. Maldonado, J. Biol. Chem. 274, 12963 (1999); T. Ohbayashi, Y. Makino, T. Tamura, Nucleic Acids Res. 27, 750 (1999); E. Wieczorek et al., Nature 393, 187 (1998).
18. R. Dikstein, S. Zhou, R. Tjian, Cell 87, 137 (1996); M. Hiller, T.-Y. Lin, M. Fuller, unpublished data.
19. P. Margolis, A. Driks, R. Losick, Curr. Opin. Genet. Dev. 1, 330 (1991).
20. 6) were transfected with 300 ng of the luciferase reporter construct, 50 ng of a CMV-renilla construct as an internal standard, and 100 ng, 500 ng, or 1 μg of the pPAC vector expressing either TRF1 or TBP. An empty pPAC vector was added to each transfection experiment to bring the total amount of pPAC in each experiment up to 1 μg, and salmon sperm was added to bring the total amount of DNA in each transfection to 5 μg.
21. 2, 0.1 mM EDTA, 10% glycerol, 1 mM dithiothreitol, 1 mM PMSF, and 1 mM sodium metabisulfite], and loaded onto a 40-ml Poros 20 HE1 column. The basal factors were stepped off with 0.4 M NaCl HEMG buffer and loaded onto a 520-ml Sephacryl-300 column (S300, Pharmacia) equilibrated in 0.1 M NaCl HEMG buffer. The proteins were resolved isocraticatty and the fractions assayed for transcriptional activity. TFIID activity was isolated from fractions corresponding to the void volume of the S300 column. Several fractions eluting after the void volume and TFIID were tested and found to contain the TFIIE, TFIIF, TFIIH, and RNA Pol II activities used in the experiments for this study. TFIID was further purified by directly loading the S300 fractions containing TFIID activity onto an 8-ml Mono-Q HR 10/10 column (Pharmacia). TFIID was eluted from the column with a 25-column volume gradient from 0.1 to 0.5 M NaCl in HEMG buffer. TFIID activity eluted between 0.25 and 0.3 M NaCl.
22. 2, 0.1 mM EDTA, 10% glycerol, 1 mM dithiothreitol, 1 mM PMSF, and 1 mM sodium metabisulfite], and loaded onto a 40-ml Poros 20 HE1 column. The basal factors were stepped off with 0.4 M NaCl HEMG buffer and loaded onto a 520-ml Sephacryl-300 column (S300, Pharmacia) equilibrated in 0.1 M NaCl HEMG buffer. The proteins were resolved isocraticatty and the fractions assayed for transcriptional activity. TFIID activity was isolated from fractions corresponding to the void volume of the S300 column. Several fractions eluting after the void volume and TFIID were tested and found to contain the TFIIE, TFIIF, TFIIH, and RNA Pol II activities used in the experiments for this study. TFIID was further purified by directly loading the S300 fractions containing TFIID activity onto an 8-ml Mono-Q HR 10/10 column (Pharmacia). TFIID was eluted from the column with a 25-column volume gradient from 0.1 to 0.5 M NaCl in HEMG buffer. TFIID activity eluted between 0.25 and 0.3 M NaCl.
23. 2, 0.1 mM EDTA, 10% glycerol, 1 mM dithiothreitol, 1 mM PMSF, and 1 mM sodium metabisulfite], and loaded onto a 40-ml Poros 20 HE1 column. The basal factors were stepped off with 0.4 M NaCl HEMG buffer and loaded onto a 520-ml Sephacryl-300 column (S300, Pharmacia) equilibrated in 0.1 M NaCl HEMG buffer. The proteins were resolved isocraticatty and the fractions assayed for transcriptional activity. TFIID activity was isolated from fractions corresponding to the void volume of the S300 column. Several fractions eluting after the void volume and TFIID were tested and found to contain the TFIIE, TFIIF, TFIIH, and RNA Pol II activities used in the experiments for this study. TFIID was further purified by directly loading the S300 fractions containing TFIID activity onto an 8-ml Mono-Q HR 10/10 column (Pharmacia). TFIID was eluted from the column with a 25-column volume gradient from 0.1 to 0.5 M NaCl in HEMG buffer. TFIID activity eluted between 0.25 and 0.3 M NaCl.
24. K. Yokomori et al., Genes Dev. 8, 2313 (1994).
25. A. M. Maxam and W. Gilbert, Proc. Natl. Acad. Sci. U.S.A. 74, 560 (1977).
26. We thank R. Freiman, C. Inouye, A. Ladurner, A. Hochheimer, J. Ziegelbauer, and D. Rio for critical reading and comments on the manuscript; J. Zwicker for collaborating in setting up a reconstituted in vitro transcription system; S. Takada for stably transformed SL2 cell lines and affinity-purified antibodies to TRF1; R. Jacobson and S. Ryu for reagents; and T. O'Brien for helpful scientific discussions and advice. Supported in part by NIH grant CA25417 (R.T.).