Arginine (348) is a major determinant of the DNA binding specificity of transcription factor E12

Biological Chemistry

Volumn 379, Issue 6, 1998, Pages 731-735

  Sieber, Martin ^a   Allemann, Rudolf K ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

BHLH proteins; Conformation; DNA binding selectivity; DNA recognition; Indirect effects; Transcription factors

Indexed keywords

ARGININE; DNA; DNA BINDING PROTEIN; GLUTAMIC ACID; HELIX LOOP HELIX PROTEIN; MUTANT PROTEIN; TRANSCRIPTION FACTOR;

ARTICLE; CONTROLLED STUDY; DISSOCIATION CONSTANT; DNA PROTEIN COMPLEX; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DNA BINDING; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ARGININE; DNA PRIMERS; DNA-BINDING PROTEINS; HELIX-LOOP-HELIX MOTIFS; HUMANS; MOLECULAR SEQUENCE DATA; POLYMERASE CHAIN REACTION; TRANSCRIPTION FACTORS;

EID: 0031868294     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (19)

1. Buonanno, A., Apone, L., Morasso, M.I., Beers, R., Brenner, H.R., and Eftimie, R. (1992). The MyoD family of myogenic factors is regulated by electrical activity: isolation and characterization of a mouse Myf-5 cDNA. Nucleic Acids Res. 20, 539-544.
2. Davis, R.L., Weintraub, H., and Lassar, A.B. (1987). Expression of a single transfected cDNA converts fibroblasts to myoblasts. Cell 51, 987-1000.
3. Dobler, M. (1992). MoMo (color version 1.4) ETH-Zurich.
4. Edmondson, D.G., and Olson E.N. (1989). A gene with homology to the myc similarity region of MyoD1 is expressed during myogenesis and is sufficient to activate the muscle differentiation program. Genes and Development 3, 628-640.
5. Ellenberger, T., Fass, D., Arnaud, M., and Harrison, S.C. (1994). Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer. Genes and Development 8, 970-980.
6. Fairman, R., Beran-Steed, R.K., Anthony-Cahill, S.J., Lear, J.D., Stafford III, W.F., DeGrado, W.F., Benfield, P.A., and Brenner, S.L (1993). Multiple oligomeric states regulate the DNA binding of helix-loop-helix petides. Proc. Natl. Acad. Sci. USA 90, 10429-10433.
7. Jen-Jacobsen, L. (1997). Protein-DNA recognition complexes: Conservation of structure and binding energy in the transition state. Biopoly. 44, 153-180.
8. Johnson, J.E., Birren, S.J., and Anderson, D.J. (1990). Two rat homologues of Drosophila achaete-scute specifically expressed in neuronal precursors. Nature 346, 858-861.
9. Künne, A.G.E., Meierhans, D., and Allemann, R.K. (1996). Basic helix-loop-helix protein MyoD displays modest DNA binding specificity. FEBS Lett. 391, 79-83.
10. Ma, P.C.M., Rould, M.A., Weintraub, H., and Pabo, C.O. (1994). Crystal structure of MyoD bHLH domain-DNA complex: Perspectives on DNA recognition and implications for transcriptional activation. Cell 77, 451-459.
11. Meierhans, D., el Ariss, C., Neuenschwander, M., Sieber, M., Stackhouse, J.F., and Allemann, R.K. (1995). DNA binding specificity of the basic-helix-loop-helix protein MASH-1. Biochemistry 34, 11026-11036.
12. Metz, R., and Ziff, E. (1991). The helix-loop-helix protein rE12 and the C/EBP-related factor rNFIL-6 bind to neighboring sites within the c-fos serum response element. Oncogene 6, 2165-2178.
13. Miner, J.H., and Wold, B. (1990). Herculin, a fourth member of the MyoD family of myogenic regulatory genes. Proc. Natl. Acad. Sci. USA 87, 1089-1093.
14. Murre, C., Schonleber McCaw, P., Vaessin, H., Jan, L.Y., Cabrera, C.V., Buskin, J.N., Hauschka, S.D., Lassar, A.B., Weintraub, H., and Baltimore, D. (1989a). Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNAsequence. Cell 58, 537-544.
15. Murre, C., Schonleber McCaw, P., and Baltimore, D. (1989b). A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins. Cell 56, 777-783.
16. Rosenberg, J.M., and Greene, P. (1982). Eco RI* specificity and hydrogen bonding. DNA 1, 117-124.
17. Sanger, F., Nicklen, S., and Coulson, A.R. (1977). DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463-5467.
18. Seeman, N.C., Rosenberg, J.M., and Rich, A. (1976). Sequence-specific recognition of double helical nucleic acids by proteins. Proc. Natl. Acad. Sci. USA 73, 804-808.
19. Winter, B., Braun, T., and Arnold, H.-H. (1992). Co-operativity of functional domains in the muscle-specific transcription factor Myf-5. EMBO J. 11, 1843-1855.