The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
The MyoD DNA binding domain contains a recognition code for muscle-specific gene activation
Abstract
A 60 amino acid domain of the myogenic determination gene MyoD is necessary and sufficient for sequence-specific DNA binding in vitro and myogenic conversion of transfected C3H10T1/2 cells. We show that a highly basic region, immediately upstream of the helix-loop-helix (HLH) oligomerization motif, is required for MyoD DNA binding in vitro. Replacing helix1, helix2, or the loop of MyoD with the analogous sequence of the Drosophila T4 achaete-scute protein (required for peripheral neurogenesis) has no substantial effect on DNA binding in vitro or muscle-specific gene activation in transfected C3H10T1/2 cells. However, replacing the basic region of MyoD with the analogous sequence of other HLH proteins (the immunoglobulin enhancer binding E12 protein or T4 achaete scute protein) allows DNA binding in vitro, yet abolishes muscle-specific gene activation. These findings suggest that a recognition code that determines muscle-specific gene activation lies within the MyoD basic region and that the capacity for specific DNA binding is insufficient to activate the muscle program.
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In the citing paper
“Mutation analysis has shown that the amino acids A114, T115, and K124 of mouse MyoD1 are crucial for myogenic activity.”
From Evolutionary aspects of developmentally regulated helix-loop-helix transcription factors in striated muscle of jellyfish (2003) · cites this paper as Davis et al., 1990
In the citing paper
“Remarkably, placing the corresponding amino acid residues from MyoD1 into its dimerization partner E-12 produces a protein that functions as myogenic activator”
From Evolutionary aspects of developmentally regulated helix-loop-helix transcription factors in striated muscle of jellyfish (2003) · cites this paper as Davis et al., 1990
In the citing paper
“JellyD1 contains two of the crucial amino acids needed for myogenic activity”
From Evolutionary aspects of developmentally regulated helix-loop-helix transcription factors in striated muscle of jellyfish (2003) · cites this paper as Davis et al., 1990
Citations
Cites
Recombinant Genomes Which Express Chloramphenicol Acetyltransferase in Mammalian Cells
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The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins
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Expression of a single transfected cDNA converts fibroblasts to myoblasts
Davis, R. L., Weintraub, H. M., & Lassar, A. B. (1987) · Cell · doi:10.1016/0092-8674(87)90585-x · Cited by 3,388
Self-citationPrediction of protein conformation
Chou, P. Y., & Fasman, G. D. (1974) · Biochemistry · doi:10.1021/bi00699a002 · Cited by 3,309
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How eukaryotic transcriptional activators work
Ptashne, M. (1988) · Nature · doi:10.1038/335683a0 · Cited by 1,828
Murre, C., Page-McCaw, P., Vaessin, H., Caudy, M. A., Jan, L. Y., Jan, Y. N., Cabrera, C. V., Buskin, J. N., Hauschka, S. D., Lassar, A. B., et al. (1989) · Cell · doi:10.1016/0092-8674(89)90434-0 · Cited by 1,815
Self-citationAmino Acid Preferences for Specific Locations at the Ends of α Helices
Richardson, J. S., & Richardson, D. C. (1988) · Science · doi:10.1126/science.3381086 · Cited by 1,364
DNA-mediated transfer of the adenine phosphoribosyltransferase locus into mammalian cells.
Wigler, M. H., Pellicer, À., Silverstein, S. J., Axel, R., Urlaub, G., & Chasin, L. A. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.3.1373 · Cited by 1,278
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NeuN, a neuronal specific nuclear protein in vertebratesxs
Mullen, R. J., Buck, C. R., & Smith, A. M. (1992) · Development · doi:10.1242/dev.116.1.201 · Cited by 2,351
The protein Id: A negative regulator of helix-loop-helix DNA binding proteins
Benezra, R., Davis, R. L., Lockshon, D., Turner, D. L., & Weintraub, H. M. (1990) · Cell · doi:10.1016/0092-8674(90)90214-y · Cited by 2,202
Self-citationMax: A Helix-Loop-Helix Zipper Protein That Forms a Sequence-Specific DNA-Binding Complex with Myc
Blackwood, E. M., & Eisenman, R. N. (1991) · Science · doi:10.1126/science.2006410 · Cited by 1,681
The myoD Gene Family: Nodal Point During Specification of the Muscle Cell Lineage
Weintraub, H. M., Davis, R. L., Tapscott, S. J., Thayer, M., Krause, M., Benezra, R., Blackwell, T. K., Turner, D. L., Rupp, R. A. W., Hollenberg, S. M., et al. (1991) · Science · doi:10.1126/science.1846704 · Cited by 1,581
Self-citationKatagiri, T. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.127.6.1755 · Cited by 1,452
Metadata
- Authors
- Davis, R. L., Cheng, P.-F., Lassar, A. B., & Weintraub, H.
- Affiliations
- University of Washington (US)
- Fred Hutch Cancer Center (US)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1990-03
- Volume
- 60
- Issue
- 5
- Pages
- 733-746
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2078709292
- Cited by
- 765
- References
- 52
- Citations by year
- 2026: 2 · 2024: 3 · 2023: 1 · 2022: 4 · 2021: 4 · 2020: 4 · 2019: 3 · 2018: 3 · 2017: 7 · 2016: 9 · 2015: 5 · 2014: 5 · 2013: 8 · 2012: 12
- FWCI
- 45.35
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Keywords
- MyoD, DNA-binding domain, helix-loop-helix proteins, basic region, E12, C3H10T1/2 cells, sequence-specific DNA binding, transcriptional activation
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Cell Differentiation, Cells, Cultured, Chromosome Deletion, DNA, Enhancer Elements, Genetic, Gene Expression Regulation, Genes, Models, Molecular, Molecular Sequence Data, Muscle Proteins, Muscles, Protein Conformation, Transfection, Oligonucleotide Probes, Transcriptional Activation, MyoD Protein, Mice
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