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J. Molkentin, E. Olson (1996)
Combinatorial control of muscle development by basic helix-loop-helix and MADS-box transcription factors.Proceedings of the National Academy of Sciences of the United States of America, 93 18
Davis (1992)
256Science, 12
J. Molkentin, B. Black, James Martin, E. Olson (1995)
Cooperative activation of muscle gene expression by MEF2 and myogenic bHLH proteinsCell, 83
Jane Johnson, S. Birren, T. Saito, David Anderson (1992)
DNA binding and transcriptional regulatory activity of mammalian achaete-scute homologous (MASH) proteins revealed by interaction with a muscle-specific enhancer.Proceedings of the National Academy of Sciences of the United States of America, 89
D. Edmondson, E. Olson (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 & development, 3 5
P. Puri, P. Puri, Vittorio Sartorelli, Vittorio Sartorelli, Xiang-Jiao Yang, Yasuo Hamamori, Vasily Ogryzko, Bruce Howard, L. Kedes, Jean Wang, Adolf Graessmann, Yoshihiro Nakatani, Massimo Levrero, Massimo Levrero (1997)
Differential roles of p300 and PCAF acetyltransferases in muscle differentiation.Molecular cell, 1 1
Jane Johnson, S. Birren, D. Anderson (1990)
Two rat homologues of Drosophila achaete-scute specifically expressed in neuronal precursorsNature, 346
Molkentin (1996)
93Proc Natl Acad Sci USA
(1998)
Basic-Helix-Loop-Helix und MADS-Box Transkriptionsfaktoren: zwei Strategien zur spezifischen DNS Erkennung
P. Ma, M. Rould, H. Weintraub, C. Pabo (1994)
Crystal structure of MyoD bHLH domain-DNA complex: Perspectives on DNA recognition and implications for transcriptional activationCell, 77
H. Weintraub (1993)
The MyoD family and myogenesis: Redundancy, networks, and thresholdsCell, 75
M. Sieber, R. Allemann (1998)
Arginine (348) is a major determinant of the DNA binding specificity of transcription factor E12.Biological chemistry, 379 6
V. Sartorelli, Jing Huang, Y. Hamamori, L. Kedes (1997)
Molecular mechanisms of myogenic coactivation by p300: direct interaction with the activation domain of MyoD and with the MADS box of MEF2CMolecular and Cellular Biology, 17
Sartorelli (1997)
300Mol Cell Biol
D. Meierhan, C. el-Ariss, M. Neuenschwander, M. Sieber, J. Stackhouse, R. Allemann (1995)
DNA binding specificity of the basic-helix-loop-helix protein MASH-1.Biochemistry, 34 35
E. Olson (1989)
A new myocyte-specific enhancer-binding factor that recognizes a conserved element associated with multiple muscle-specific genes.Molecular and cellular biology, 9 11
(1997)
Covalently linking MASH-1 BHLH subunits enhances specificity of DNA binding
F. Sanger, S. Nicklen, A. Coulson (1977)
DNA sequencing with chain-terminating inhibitors.Proceedings of the National Academy of Sciences of the United States of America, 74 12
Thomas Ellenberger, Deborah Fass, Martha Arnaud, Stephen Harrison, Stephen Harrison (1994)
Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer.Genes & development, 8 8
L. Sommer, N. Shah, M. Rao, D. Anderson (1995)
The cellular function of MASH1 in autonomic neurogenesisNeuron, 15
J. Molkentin, E. Olson (1996)
Defining the regulatory networks for muscle development.Current opinion in genetics & development, 6 4
Sieber (1998)
348Biol Chem, 12
Kuenne (1997)
36Biochemistry, 1
R. Davis, H. Weintraub (1992)
Acquisition of myogenic specificity by replacement of three amino acid residues from MyoD into E12.Science, 256 5059
Johnson (1992)
DNA binding and transcriptional regulatory activity of mammalian achaete - scute homologous ( MASH ) proteins re - vealed by interaction with a muscle - specific enhancer NatlProc Acad Sci USA
A. Baranger, C. Palmer, Mary Hamm, H. Giebler, A. Brauweiler, J. Nyborg, A. Schepartz (1995)
Mechanism of DNA-binding enhancement by the human T-cell leukaemia virus transactivator TaxNature, 376
Johnson (1992)
89Proc Acad Sci USA
Puri (1997)
Differential roles of and PCAF acetyltransferases in muscle differentiation CellMol Biol
R. Davis, H. Weintraub, A. Lassar (1987)
Expression of a single transfected cDNA converts fibroblasts to myoblastsCell, 51
Baranger (1995)
376Nature
Kuenne (1996)
391FEBS Lett
R. Eckner, T. Yao, Elizabeth Oldread, David Livingston (1996)
Interaction and functional collaboration of p300/CBP and bHLH proteins in muscle and B-cell differentiation.Genes & development, 10 19
Ma (1994)
77Cell
A. Künne, D. Meierhans, R. Allemann (1996)
Basic helix‐loop‐helix protein MyoD displays modest DNA binding specificityFEBS Letters, 391
Johnson (1990)
346Nature
Sanger (1977)
74Proc Natl Acad Sci USA
G. Perini, S. Wagner, M. Green (1995)
Recognition of bZIP proteins by the human T-cell leukaemia virus transactivator TaxNature, 376
Davis (1987)
51Cell
Tapscott (1988)
1Science
S. Tapscott, R. Davis, M. Thayer, P. Cheng, H. Weintraub, A. Lassar (1988)
MyoD1: a nuclear phosphoprotein requiring a Myc homology region to convert fibroblasts to myoblasts.Science, 242 4877
Abstract The homologous transcription factors Myf-5, MyoD, myogenin, MRF-4, and MASH-1 bind with high affinity and modest sequence specificity to DNA containing an E-box (CANNTG). This similarity of the in vitro DNA binding specificity is in sharp contrast to the high physiological specificity displayed by these proteins. Myf-5, MyoD, myogenin, and MRF-4 induce cells to differentiate along a myogenic pathway, while MASH-1 promotes the differentiation of neuronal precursor cells. We show here that MASH-1 can be converted into a protein capable of inducing myogenesis in fibroblasts by replacing leucine (130) of MASH-1 with lysine and introducing an additional turn into its basic recognition helix. These changes do not significantly alter the DNA binding properties of the proteins in cell free conditions. Crystallographic data for the DNA complexes of MyoD and E12 suggest that Leu (130) points away from the DNA into the solvent. We postulate that the identity of the amino acid in position 130 is important for protein-protein interactions that might affect the DNA binding specificities displayed by BHLH-proteins in vivo and form the molecular basis of the different physiological properties of the myogenic and neurogenic BHLH-proteins.
Biological Chemistry – de Gruyter
Published: Jun 1, 1999
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