TY - JOUR
T1 - MIDA1, an Id-associating protein, has two distinct DNA binding activities that are converted by the association with Id1
T2 - A novel function of Id protein
AU - Inoue, Toshiaki
AU - Shoji, Wataru
AU - Obinata, Masuo
N1 - Funding Information:
We thank Drs. T. C. Schulz and M. Oshimura (Tottori University) for critical reading of the manuscript. This work was supported in part by a Grant-in-Aid from the Ministry of Education, Science, Sports, and Culture of Japan.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 1999/12/9
Y1 - 1999/12/9
N2 - Id proteins not only regulate cell differentiation negatively, but they also promote growth, immortalization, and apoptosis. To know the mechanism of how Id regulates cell fate, we previously isolated an Id-associating protein, MIDA1, which positively regulates cell growth. Its predicted amino acid sequence consists of a Zuotin (a Z-DNA binding protein in yeast) homology region and tryptophan-mediated repeats (Tryp-med repeats). MIDA1 exhibits a sequence-specific DNA binding activity through the Tryp-med repeats. In this study, we revealed that, like Zuotin, MIDA1 can specifically bind to Z-DNA. This suggested that MIDA is a novel DNA binding protein that has two different DNA binding activities. Furthermore, association of Id1 with MIDA1 stimulated the sequence-specific DNA binding activity, while it inhibited the Z-DNA binding activity. Therefore, we concluded that MIDA1 may act as a mediator of the growth-promoting function of Id, by switching the two DNA binding activities of MIDA1.
AB - Id proteins not only regulate cell differentiation negatively, but they also promote growth, immortalization, and apoptosis. To know the mechanism of how Id regulates cell fate, we previously isolated an Id-associating protein, MIDA1, which positively regulates cell growth. Its predicted amino acid sequence consists of a Zuotin (a Z-DNA binding protein in yeast) homology region and tryptophan-mediated repeats (Tryp-med repeats). MIDA1 exhibits a sequence-specific DNA binding activity through the Tryp-med repeats. In this study, we revealed that, like Zuotin, MIDA1 can specifically bind to Z-DNA. This suggested that MIDA is a novel DNA binding protein that has two different DNA binding activities. Furthermore, association of Id1 with MIDA1 stimulated the sequence-specific DNA binding activity, while it inhibited the Z-DNA binding activity. Therefore, we concluded that MIDA1 may act as a mediator of the growth-promoting function of Id, by switching the two DNA binding activities of MIDA1.
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U2 - 10.1006/bbrc.1999.1779
DO - 10.1006/bbrc.1999.1779
M3 - Article
C2 - 10581180
AN - SCOPUS:0033539917
VL - 266
SP - 147
EP - 151
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -