Differential interactions of Id proteins with basic-helix-loop-helix transcription factors
Differential interactions of Id proteins with basic-helix-loop-helix transcription factors
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DOI:
10.1074/jbc.272.32.19785
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发表时间:
1997-08-08
影响因子:
4.8
通讯作者:
Prochownik, EV
中科院分区:
文献类型:
--
作者:
Langlands, K;Yin, XY;Prochownik, EV
Dimerization of three Id proteins (Idl, 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, Idl 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 a-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 Idl 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.