Differential Interactions of Id Proteins with Basic-Helix-Loop-Helix Transcription Factors

Dimerization of three Id proteins (Id1, Id2, and Id3) with the four class A E proteins (E12, E47, E2-2, and HEB) and two groups of class B proteins, the myogenic regulatory factors (MRFs: MyoD, myogenin, Myf-5 and MRF4/Myf-6), and the hematopoietic factors (Scl/Tal-1, Tal-2, and Lyl-1) were tested i...

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Bibliographic Details
Published in:The Journal of biological chemistry 1997-08, Vol.272 (32), p.19785-19793
Main Authors: Langlands, Kenneth, Yin, Xiaoying, Anand, Geetha, Prochownik, Edward V.
Format: Article
Language:English
Subjects:
Animals
Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
Basic Helix-Loop-Helix Transcription Factors
Binding Sites - genetics
Dimerization
DNA-Binding Proteins - metabolism
Helix-Loop-Helix Motifs
Inhibitor of Differentiation Protein 1
Mice
Muscle Proteins - metabolism
Mutagenesis, Site-Directed
MyoD Protein - metabolism
Myogenic Regulatory Factor 5
Myogenic Regulatory Factors - metabolism
Myogenin - metabolism
Nerve Tissue Proteins
Protein Binding
Repressor Proteins
Saccharomyces cerevisiae
TCF Transcription Factors
Trans-Activators - metabolism
Transcription Factor 4
Transcription Factor 7-Like 1 Protein
Transcription Factors - metabolism
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Summary:Dimerization of three Id proteins (Id1, Id2, and Id3) with the four class A E proteins (E12, E47, E2-2, and HEB) and two groups of class B proteins, the myogenic regulatory factors (MRFs: MyoD, myogenin, Myf-5 and MRF4/Myf-6), and the hematopoietic factors (Scl/Tal-1, Tal-2, and Lyl-1) were tested in a quantitative yeast 2-hybrid assay. All three Ids bound with high affinity to E proteins, but a much broader range of interactions was observed between Ids and the class B factors. Id1 and Id2 interacted strongly with MyoD and Myf-5 and weakly with myogenin and MRF4/Myf-6, whereas Id3 interacted weakly with all four MRFs. Similar specificities were observed in co-immunoprecipitation and mammalian 2-hybrid analyses. No interactions were found between the Ids and any of the hematopoietic factors. Each Id was able to disrupt the ability of E protein-MyoD complexes to transactivate from a muscle creatine kinase reporter construct in vivo. Finally, mutagenesis experiments showed that the differences between Id1 and Id3 binding map to three amino acids in the first helix and to a small cluster of upstream residues. The Id proteins thus display a signature range of interactions with all of their potential dimerization partners and may play a role in myogenesis which is distinct from that in hematopoiesis.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.272.32.19785