Transcription factor-specific requirements for coactivators and their acetyltransferase functions

Science

Volumn 279, Issue 5351, 1998, Pages 703-707

  Korzus, Edward ^a   Torchia, Joseph ^a   Rose, David W ^a   Xu, Lan ^a   Kurokawa, Riki ^a   McInerney, Eileen M ^a   Mullen, Tina Marie ^a   Glass, Christopher K ^a   Rosenfeld, Michael G ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; HISTONE ACETYLTRANSFERASE; RETINOIC ACID RECEPTOR; STAT1 PROTEIN; TRANSCRIPTION FACTOR;

ARTICLE; HELA CELL; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN PROTEIN INTERACTION; TRANSACTIVATION;

ACETYLTRANSFERASES; CELL CYCLE PROTEINS; CREB-BINDING PROTEIN; CYCLIC AMP; CYCLIC AMP RESPONSE ELEMENT-BINDING PROTEIN; DNA-BINDING PROTEINS; GENE EXPRESSION REGULATION; HELA CELLS; HISTONE ACETYLTRANSFERASES; HUMANS; LIGANDS; MUTATION; NUCLEAR PROTEINS; PROMOTER REGIONS (GENETICS); RECEPTORS, RETINOIC ACID; REPRESSOR PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; STAT1 TRANSCRIPTION FACTOR; TRANS-ACTIVATION (GENETICS); TRANS-ACTIVATORS; TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC;

MAMMALIA;

EID: 0032579292     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.279.5351.703     Document Type: Article

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50. Whole-cell extracts were prepared by lysing the cells in-NET-N buffer containing 50 mM tris (pH 7.6), 5 mM EDTA, 0.3 M NaCl, 1 mM dithiothreitol, 0.1 % NP-40, and protease inhibitors (2 mM phenylmethylsulfonyl fluoride and 10 μg/ml each of leupeptin, pepstatin, and aprotinin). The mixture was then centrifuged at 30,000g for 1 hour at 4°C, and the supernatant was stored at -80°C until use. For coimmunoprecipitation assays, 1 mg of cell extract was incubated in the presence of 2 μg of anti-p/CIP, anti-Flag, or anti-RAR IgG for 2 hours at 4°C. The immune complexes were then precipitated with protein A-Sepharose. Protein complexes were resolved by SDS-polyacrylamide gel electrophoresis (PAGE) [U. K. Laemmli, Nature 227, 680 (1970)], protein immunoblotted, and probed using 1 μg/ml of anti-Flag, anti-p/CIP, or an anti-hemagglutinin (anti-HA).
51. - medium containing 2% galactose. Isolated yeast colonies were then allowed to grow in the same liquid medium and were subsequently assayed for β-galactosidase, as previously described [F. M. Ausubel et al., Current Protocols in Molecular Biology (Wiley, New York, 1995)]. All constructs were sequenced and functionally tested in yeast two-hybrid assays, showing interaction with other proteins as previously described (2, 7). In the case of p/CAF constructs, each fragment interacted positively with at least one other coactivator except the fragment with amino acids 86 through 518.
52. - medium containing 2% galactose. Isolated yeast colonies were then allowed to grow in the same liquid medium and were subsequently assayed for β-galactosidase, as previously described [F. M. Ausubel et al., Current Protocols in Molecular Biology (Wiley, New York, 1995)]. All constructs were sequenced and functionally tested in yeast two-hybrid assays, showing interaction with other proteins as previously described (2, 7). In the case of p/CAF constructs, each fragment interacted positively with at least one other coactivator except the fragment with amino acids 86 through 518.
53. Insulin-responsive Rat-1 fibroblasts were seeded on acid-washed glass cover slips at subconfluent density and grown in D-MEM/F-12 (Life Technologies) medium supplemented with 10% fetal bovine serum, gentamicin, and methotrexate. Before the injection, the cells were rendered quiescent by incubation in serum-free medium for 24 to 36 hours. Plasmids were injected into the nuclei of cells at a final concentration of 100 μg/ml. Immunoglobulin G specific for p/CAF was prepared from guinea pig serum raised against a bacterially expressed fragment (amino acids 466 to 832) of p/CAF; this IgG recognized the single band of p/CAF in protein immunoblot analysis. Either preimmune IgG or the appropriate specific antibodies directed against p/CAF, p/CIP, SRC-1, or CBP were coinjected and allowed the unambiguous identification of the injected cells (7). Preimmune controls were included in all experiments. Microinjections were carried out using an Eppendorf semiautomated microinjection system mounted on an inverted Zeiss microscope. Approximately 1 hour after injection, the cells were stimulated, where indicated, with the appropriate ligand. In the case of rescue experiments, the cells were stimulated with ligand 6 hours after injection to allow protein expression. After overnight incubation, the cells were fixed and then stained to detect injected IgG and β-galactosidase expression (D.W. Rose et al., J. Cell Biol. 119, 1405 (1992); (2)]. Injected cells were identified by staining with tetramethylrhodamine-conjugated donkey antirabbit IgG. All experimental results are expressed as the mean ± SEM of at least three experiments in which at least 1000 cells were injected.
54. 35S-labeled p/CAF proteins generated by in vitro transcription and translation for 2 hours at 4°C. The complexes were washed five times with NET-N buffer, resolved by SDS-PAGE, and fluorographed.
55. HAT-). A similar strategy was used to obtain mutants of CBP. Mutants of p/CAF and CBP were expressed in bacteria and baculovirus, respectively, and tested for HAT activity in solution using histones as substrates [J. E. Brownell and C. D. Allis, Proc. Natl. Acad. Sci. U.S.A. 92, 6364 (1995)].
56. We thank R. Heyman for use of TTNPB and LG629, S. L. Berger for discussion and providing hGCN5 expression vector, and Y. Nakatani and X. J. Yang for providing a tagged p/CAF expression vector. We also thank C. Nelson for experimental assistance, L.-M. Phillips for excellent technical assistance, and P. Myer for expertise in figure preparation. E.K. is supported by a U.S. Army Medical Research Program Award, J.T. by the National Cancer Institute of Canada, E.M.M. by an NIH Postdoctoral Fellowship, D.W.R. by an American Diabetes Association Career Development Award, and L.X. by an American Heart Association Predoctoral Fellowship. Supported by grants from NIH to C.K.G. and M.G.R.