TAF1 Activates Transcription by Phosphorylation of Serine 33 in Histone H2B

Science

Volumn 304, Issue 5673, 2004, Pages 1010-1014

  Maile, Tobias ^a   Kwoczynski, Simona ^b   Katzenberger, Rebeccah J ^c   Wassarman, David A ^c   Sauer, Frank ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF HEIDELBERG   (Germany)

^c UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; CYTOLOGY; ENZYMES; GENETIC ENGINEERING; REACTION KINETICS;

CELL CYCLE; PHOSPHORYLATION; TRANSCRIPTION; TRANSCRIPTIONAL ACTIVATION;

AMINO ACIDS;

CARBOXYL TERMINAL KINASE; HISTONE H2B; PHOSPHOTRANSFERASE; PROTEIN SUBUNIT; SERINE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR TAF1; UNCLASSIFIED DRUG; CAUDAL PROTEIN, DROSOPHILA; DNA BINDING PROTEIN; DROSOPHILA PROTEIN; GIANT PROTEIN, DROSOPHILA; HISTONE; HISTONE ACETYLTRANSFERASE; HOMEODOMAIN PROTEIN; PHOSPHOSERINE; PROTEIN TYROSINE PHOSPHATASE; RECOMBINANT PROTEIN; REPRESSOR PROTEIN; STG PROTEIN, DROSOPHILA; TAF1 PROTEIN, DROSOPHILA; TRANSCRIPTION FACTOR IID;

BIOLOGY;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL CYCLE; CELL MATURATION; CHROMATIN STRUCTURE; CONTROLLED STUDY; DROSOPHILA; ENZYME ACTIVITY; ENZYME SUBSTRATE; GENETIC CONSERVATION; INSECT CELL; MOLECULAR DYNAMICS; MOLECULAR EVOLUTION; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; REGULATOR GENE; TRANSCRIPTION INITIATION; TRANSCRIPTION REGULATION; ACETYLATION; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL; ANIMAL EMBRYO; CHEMISTRY; GENE; GENETIC TRANSCRIPTION; GENETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; PHOSPHORYLATION; PHYSIOLOGY; PRENATAL DEVELOPMENT; PROTEIN MOTIF; PROTEIN TERTIARY STRUCTURE; RNA INTERFERENCE; TRANSACTIVATION;

ANIMALIA; ARACHNIDA; EUKARYOTA; HEXAPODA; INSECTA;

ACETYLATION; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; CELL CYCLE; DNA-BINDING PROTEINS; DROSOPHILA; DROSOPHILA PROTEINS; EMBRYO, NONMAMMALIAN; GENES, INSECT; HISTONE ACETYLTRANSFERASES; HISTONES; HOMEODOMAIN PROTEINS; MOLECULAR SEQUENCE DATA; MUTATION; PHOSPHORYLATION; PHOSPHOSERINE; PROMOTER REGIONS (GENETICS); PROTEIN STRUCTURE, TERTIARY; PROTEIN-TYROSINE-PHOSPHATASE; RECOMBINANT PROTEINS; REPRESSOR PROTEINS; RNA INTERFERENCE; TRANS-ACTIVATION (GENETICS); TRANSCRIPTION FACTOR TFIID; TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC;

EID: 2342506598     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1095001     Document Type: Article

References (31)

1. B. Lemon, R. Tjian, Genes Dev. 14, 2551 (2000).
2. G. Orphanides, D. Reinberg, Cell 108, 439 (2002).
3. K. Luger, A. W. Mader, R. Richmond, D. F. Sargent, T. J. Richmond, Nature 389, 251 (1997).
4. M. G. Goll T. H. Bestor, Genes Dev. 16, 1739 (2002).
5. W. Fischle, Y. Wang, C. D. Allis, Nature 425, 475 (2003).
6. W. L. Cheung et al., Cell 113, 507 (2003).
7. I. Isenberg, Annu. Rev. Biochem. 48, 159 (1979).
8. Materials and methods are available as supporting material on Science Online.
9. B. S. Chen, M. Hampsey, Curr. Biol. 12, R620 (2002).
10. R. Dikstein, S. Ruppert, R. Tjian, Cell 84, 781 (1996).
11. D. A. Wassarman, F. Sauer, J. Cell Sci. 114, 2895 (2001).
12. A.-D. Pham, F. Sauer, Science 289, 2357 (2000).
13. S. C. Elgin, J. Schilling, L. E. Hood, Biochemistry 18, 5679 (1979).
14. R. H. Jacobson, A. G. Ladumer, D. S. King, R. Tjian, Science 288, 1422 (2000).
15. C. Beisel, A. Imhof, J. Greene, E. Kremmer, F. Sauer, Nature 419, 857 (2002).
16. P. T. Georgel, T. Tsukiyama, C. Wu, EMBO J. 16, 4717 (1997).
17. M. S. Lee et al., Mol. Biol. Cell 3, 73 (1992).
18. L. A. Pile, E. M. Schlag, D. A. Wassarman, Mol. Cell. Biol. 22, 4965 (2002).
19. C. A. Mizzen et al., Cell 87, 1261 (1996).
20. R. Rivera-Pomar, H. Jäckle, Trends Genet. 12, 478 (1996).
21. K. Luger, T. J. Richmond, Curr. Opin. Struct. Biol. 8, 33 (1998).
22. J. Recht, M. A. Osley, EMBO J. 18, 229 (1999).
23. A. Hamiche, J.-G. Kang, C. Dennis, H. Xiao, C. Wu, Proc. Natl. Acad. Sci. U.S.A. 98, 14316 (2001).
24. L. Zheng, M. M. Zhou, FEBS Lett. 513, 124 (2002).
25. B. Florence, D. V. Faller, Front. Biosci. 6, D1008 (2001).
26. L. M. Apone, C. M. Verasius, J. C. Reese, M. R. Green, Genes Dev. 10, 2368 (1996).
27. J. Martin, R. Halenbeck, J. Kaufmann, Mol. Cell. Biol. 19, 5548 (1999).
28. M. Um, J. Yamauchi, S. Kato, J. L. Manley, Mol. Cell. Biol. 21, 2435 (2002).
29. E. L. Dunphy, T. Johnson, S. S. Auerbach, E. H. Wang, Mol. Cell. Biol. 20, 1134 (2001).
30. Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G. Gly; H, His; I, lle; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
31. We thank S. Hansen and R. Tjian for the RAP74 expression plasmid, K. Schell and J. Batchelder at the UW-Madison Comprehensive Cancer Flow Cytometry Facility for their assistance, and C. Metcalf and T. Sanchez-Elsner for comments that improved the manuscript. This work was supported by an NIH grant (GM066204-02) to D.A.W. and a Volkswagen Stiftung grant (I/77 996) to F.S.