A conserved domain in the transcription factor ITF-2B attenuates its activity

Biochemical and Biophysical Research Communications

Volumn 370, Issue 2, 2008, Pages 327-331

  Herbst, A ^a   Kolligs, F T ^a  

^a UNIVERSITY OF MUNICH   (Germany)

Author keywords

bHLH; Conserved; Domain; ITF 2; Lysine; Repression; Transcription

Indexed keywords

BASIC HELIX LOOP HELIX TRANSCRIPTION FACTOR; IMMUNOGLOBULIN TRANSCRIPTION FACTOR 2B; TRANSCRIPTION FACTOR E2A; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CELL DIFFERENTIATION; CELL STRAIN HEK293; E BOX ELEMENT; GENE REPRESSION; HELA CELL; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN DOMAIN; SEQUENCE ALIGNMENT; TRANSCRIPTION REGULATION;

AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CONSERVED SEQUENCE; CRICETINAE; DOGS; GENES, REPORTER; HUMANS; LUCIFERASES; MICE; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; RATS; REPRESSOR PROTEINS; TCF TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC;

EID: 42249111873     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.03.081     Document Type: Article

References (15)

1. Atchley W.R., and Fitch W.M. A natural classification of the basic helix-loop-helix class of transcription factors. Proc. Natl. Acad. Sci. USA 94 (1997) 5172-5176
2. Murre C., Bain G., van Dijk M.A., Engel I., Furnari B.A., Massari M.E., Matthews J.R., Quong M.W., Rivera R.R., and Stuiver M.H. Structure and function of helix-loop-helix proteins. Biochim. Biophys. Acta 1218 (1994) 129-135
3. Henthorn P., Kiledjian M., and Kadesch T. Two distinct transcription factors that bind the immunoglobulin enhancer microE5/kappa 2 motif. Science 247 (1990) 467-470
4. Corneliussen B., Thornell A., Hallberg B., and Grundstrom T. Helix-loop-helix transcriptional activators bind to a sequence in glucocorticoid response elements of retrovirus enhancers. J. Virol. 65 (1991) 6084-6093
5. Massari M.E., Jennings P.A., and Murre C. The AD1 transactivation domain of E2A contains a highly conserved helix which is required for its activity in both Saccharomyces cerevisiae and mammalian cells. Mol. Cell. Biol. 16 (1996) 121-129
6. Quong M.W., Massari M.E., Zwart R., and Murre C. A new transcriptional-activation motif restricted to a class of helix-loop-helix proteins is functionally conserved in both yeast and mammalian cells. Mol. Cell. Biol. 13 (1993) 792-800
7. Feil R., Wagner J., Metzger D., and Chambon P. Regulation of Cre recombinase activity by mutated estrogen receptor ligand-binding domains. Biochem Biophys Res Commun 237 (1997) 752-757
8. Freiman R.N., and Tjian R. Regulating the regulators: lysine modifications make their mark. Cell 112 (2003) 11-17
9. Pawson T., and Scott J.D. Protein phosphorylation in signaling--50 years and counting. Trends Biochem. Sci. 30 (2005) 286-290
10. Lu K.P., Liou Y.C., and Zhou X.Z. Pinning down proline-directed phosphorylation signaling. Trends Cell. Biol. 12 (2002) 164-172
11. Frankel A.D., and Kim P.S. Modular structure of transcription factors: implications for gene regulation. Cell 65 (1991) 717-719
12. Massari M.E., Grant P.A., Pray-Grant M.G., Berger S.L., Workman J.L., and Murre C. A conserved motif present in a class of helix-loop-helix proteins activates transcription by direct recruitment of the SAGA complex. Mol. Cell. 4 (1999) 63-73
13. Morgunkova A., and Barlev N.A. Lysine methylation goes global. Cell Cycle 5 (2006) 1308-1312
14. Grunstein M. Histone acetylation in chromatin structure and transcription. Nature 389 (1997) 349-352
15. Martin M.L., Lieberman P.M., and Curran T. Fos-Jun dimerization promotes interaction of the basic region with TFIIE-34 and TFIIF. Mol. Cell. Biol. 16 (1996) 2110-2118