TY - JOUR
T1 - Solution structure of the DNA-binding domain of MafG
AU - Kusunoki, Hideki
AU - Motohashi, Hozumi
AU - Katsuoka, Fumiki
AU - Morohashi, Akio
AU - Yamamoto, Masayuki
AU - Tanaka, Toshiyuki
N1 - Funding Information:
We thank E. Arai and F. Arisaka for ultracentrifuge analysis, T. Maeda for useful discussion, K. Yap for providing a program to calculate interhelical angles and T. O’Connor for critical reading of the manuscript. This work was supported by grants from JSPS and TARA (T.T.); the Ministry of Education, Science, Sports and Culture of Japan (H.M. and M.Y.); JSPS and CREST (M.Y.); and PROBRAIN (H.M.).
PY - 2002
Y1 - 2002
N2 - The Maf family proteins, which constitute a subgroup of basic region-leucine zipper (bZIP) proteins, function as transcriptional regulators of cellular differentiation. Together with the basic region, the Maf extended homology region (EHR), conserved only within the Maf family, defines the DNA binding specific to Mafs. Here we present the first NMR-derived structure of the DNA-binding domain (residues 1-76) of MafG, which contains the EHR and the basic region. The structure consists of three α-helices and resembles the fold of the DNA-binding domain of Skn-1, a developmental transcription factor of Caenorhabditis elegans. The structural similarity between MafG and Skn-1 enables us to propose a possible mechanism by which Maf family proteins recognize their consensus DNA sequences.
AB - The Maf family proteins, which constitute a subgroup of basic region-leucine zipper (bZIP) proteins, function as transcriptional regulators of cellular differentiation. Together with the basic region, the Maf extended homology region (EHR), conserved only within the Maf family, defines the DNA binding specific to Mafs. Here we present the first NMR-derived structure of the DNA-binding domain (residues 1-76) of MafG, which contains the EHR and the basic region. The structure consists of three α-helices and resembles the fold of the DNA-binding domain of Skn-1, a developmental transcription factor of Caenorhabditis elegans. The structural similarity between MafG and Skn-1 enables us to propose a possible mechanism by which Maf family proteins recognize their consensus DNA sequences.
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U2 - 10.1038/nsb771
DO - 10.1038/nsb771
M3 - Article
C2 - 11875518
AN - SCOPUS:0036213691
SN - 1072-8368
VL - 9
SP - 252
EP - 256
JO - Nature Structural Biology
JF - Nature Structural Biology
IS - 4
ER -