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Science 8 March 1991:
Vol. 251. no. 4998, pp. 1211 - 1217
DOI: 10.1126/science.2006410
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Articles

Science, Vol 251, Issue 4998, 1211-1217
Copyright © 1991 by American Association for the Advancement of Science

articles

Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc

EM Blackwood and RN Eisenman

Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104.

The myc protooncogene family has been implicated in cell proliferation, differentiation, and neoplasia, but its mechanism of function at the molecular level is unknown. The carboxyl terminus of Myc family proteins contains a basic region helix-loop-helix leucine zipper motif (bHLH-Zip), which has DNA-binding activity and has been predicted to mediate protein-protein interactions. The bHLH-Zip region of c-Myc was used to screen a complementary DNA (cDNA) expression library, and a bHLH-Zip protein, termed Max, was identified. Max specifically associated with c-Myc, N-Myc, and L-Myc proteins, but not with a number of other bHLH, bZip, or bHLH-Zip proteins. The interaction between Max and c-Myc was dependent on the integrity of the c-Myc HLH-Zip domain, but not on the basic region or other sequences outside the domain. Furthermore, the Myc-Max complex bound to DNA in a sequence-specific manner under conditions where neither Max nor Myc exhibited appreciable binding. The DNA-binding activity of the complex was dependent on both the dimerization domain and the basic region of c-Myc. These results suggest that Myc family proteins undergo a restricted set of interactions in the cell and may belong to the more general class of eukaryotic DNA-binding transcription factors.


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Deconstructing Myc.
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c-Myc Is a Critical Target for C/EBP{alpha} in Granulopoiesis.
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Mol. Cell. Biol. 21, 3789-3806
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T. Veldman, I. Horikawa, J. C. Barrett, and R. Schlegel (2001)
J. Virol. 75, 4467-4472
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Mol. Cell. Biol. 21, 703-712
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Role of 14-3-3{epsilon}, c-Myc/Max, and Akt phosphorylation in HIV-1 gp 120-induced mesangial cell proliferation.
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   Abstract »    Full Text »    PDF »
Induction of Cell Cycle Progression and Acceleration of Apoptosis Are Two Separable Functions of c-Myc: Transrepression Correlates with Acceleration of Apoptosis.
S. D. Conzen, K. Gottlob, E. S. Kandel, P. Khanduri, A. J. Wagner, M. O'Leary, and N. Hay (2000)
Mol. Cell. Biol. 20, 6008-6018
   Abstract »    Full Text »
HMG-I/Y, a New c-Myc Target Gene and Potential Oncogene.
L. J. Wood, M. Mukherjee, C. E. Dolde, Y. Xu, J. F. Maher, T. E. Bunton, J. B. Williams, and L. M. S. Resar (2000)
Mol. Cell. Biol. 20, 5490-5502
   Abstract »    Full Text »
Assembly of a Functional Beta Interferon Enhanceosome Is Dependent on ATF-2-c-jun Heterodimer Orientation.
J. V. Falvo, B. S. Parekh, C. H. Lin, E. Fraenkel, and T. Maniatis (2000)
Mol. Cell. Biol. 20, 4814-4825
   Abstract »    Full Text »
Mad1 Function Is Regulated through Elements within the Carboxy Terminus.
G. Barrera-Hernandez, C. M. Cultraro, S. Pianetti, and S. Segal (2000)
Mol. Cell. Biol. 20, 4253-4264
   Abstract »    Full Text »
Molecular Cloning, Expression, and Characterization of Rat Homolog of Human AP-2{alpha} That Stimulates Neuropeptide Y Transcription Activity in Response to Nerve Growth Factor.
B.-S. Li, P. R. Kramer, W. Zhao, W. Ma, D. A. Stenger, and L. Zhang (2000)
Mol. Endocrinol. 14, 837-847
   Abstract »    Full Text »
An in Vivo Function for the Transforming Myc Protein: Elicitation of the Angiogenic Phenotype.
C. V. Ngo, M. Gee, N. Akhtar, D. Yu, O. Volpert, R. Auerbach, and A. Thomas-Tikhonenko (2000)
Cell Growth Differ. 11, 201-210
   Abstract »    Full Text »
Effect of Trichloroethylene and Its Metabolites, Dichloroacetic Acid and Trichloroacetic Acid, on the Methylation and Expression of c-Jun and c-Myc Protooncogenes in Mouse Liver: Prevention by Methionine.
L. Tao, S. Yang, M. Xie, P. M. Kramer, and M. A. Pereira (2000)
Toxicol. Sci. 54, 399-407
   Abstract »    Full Text »    PDF »
Inhibition of Proliferation and Apoptosis by the Transcriptional Repressor Mad1. REPRESSION OF Fas-INDUCED CASPASE-8 ACTIVATION.
S. Gehring, S. Rottmann, A. R. Menkel, J. Mertsching, A. Krippner-Heidenreich, and B. Luscher (2000)
J. Biol. Chem. 275, 10413-10420
   Abstract »    Full Text »    PDF »
Reciprocal Regulation via Protein-Protein Interaction between c-Myc and p21cip1/waf1/sdi1 in DNA Replication and Transcription.
H. Kitaura, M. Shinshi, Y. Uchikoshi, T. Ono, T. Tsurimoto, H. Yoshikawa, S. M. M. Iguchi-Ariga, and H. Ariga (2000)
J. Biol. Chem. 275, 10477-10483
   Abstract »    Full Text »    PDF »
Expression of Fas Ligand in Activated T Cells Is Regulated by c-Myc.
T. Brunner, S. Kasibhatla, M. J. Pinkoski, C. Frutschi, N. J. Yoo, F. Echeverri, A. Mahboubi, and D. R. Green (2000)
J. Biol. Chem. 275, 9767-9772
   Abstract »    Full Text »    PDF »
TFE3, a Transcription Factor Homologous to Microphthalmia, Is a Potential Transcriptional Activator of Tyrosinase and TyrpI Genes.
C. Verastegui, C. Bertolotto, K. Bille, P. Abbe, J. P. Ortonne, and R. Ballotti (2000)
Mol. Endocrinol. 14, 449-456
   Abstract »    Full Text »
Expression of Steroidogenic Factor 1 in the Testis Requires an E Box and CCAAT Box in its Promoter Proximal Region.
M. A.F. Daggett, D. A. Rice, and L. L. Heckert (2000)
Biol Reprod 62, 670-679
   Abstract »    Full Text »
c-Myc Protein Synthesis Is Initiated from the Internal Ribosome Entry Segment during Apoptosis.
M. Stoneley, S. A. Chappell, C. L. Jopling, M. Dickens, M. MacFarlane, and A. E. Willis (2000)
Mol. Cell. Biol. 20, 1162-1169
   Abstract »    Full Text »
Sp1 cooperates with c-Myc to activate transcription of the human telomerase reverse transcriptase gene (hTERT).
S. Kyo, M. Takakura, T. Taira, T. Kanaya, H. Itoh, M. Yutsudo, H. Ariga, and M. Inoue (2000)
Nucleic Acids Res. 28, 669-677
   Abstract »    Full Text »    PDF »


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