Dimerization and DNA Binding Facilitate .ALPHA.-Helix Formation of Max in Solution.
-
- Horiuchi Masataka
- Department of Bioengineering, Faculty of Engineering, Yokohama National University
-
- Kurihara Yasuyuki
- Department of Bioengineering, Faculty of Engineering, Yokohama National University
-
- Katahira Masato
- Department of Bioengineering, Faculty of Engineering, Yokohama National University
-
- Maeda Tadakazu
- Department of Physics, Kitasato University
-
- Saito Toshiyuki
- Division of Genetics, National Institute of Radiological Sciences
-
- Uesugi Seiichi
- Department of Bioengineering, Faculty of Engineering, Yokohama National University
抄録
Max is a basic region/helix-loop-helix/leucine zipper (b/HLH/Z) protein that forms a hetero-complex with the Myc family proteins Myc, Mad, and Mxil, and a homo-complex with itself. These complexes specifically bind to double-stranded DNA containing CACGTG sequences. Here, we report on the structural properties in aqueous solution of a 109-aminoacid protein, Max110, corresponding to the N-terminal domain of Max containing the b/ HLH/Z motif (residues 2-110), as characterized by combined use of circular dichroism (CD) and sedimentation equilibrium experiments. The results showed that the α-helical content of Max 110 increases with increasing protein concentration. The sedimentation equilibrium data indicated that Max110 exists as a monomer at low protein concentration, and forms a dimer at high protein concentration. Further increases in the α-helical content of Max110 occur upon addition of DNA with the CACGTG recognition sequence. Thus, dimerization and binding to DNA of Max both favor an increase of the α-helical content.
収録刊行物
-
- The Journal of Biochemistry
-
The Journal of Biochemistry 122 (4), 711-716, 1997
The Japanese Biochemical Society
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1570291228186077824
-
- NII論文ID
- 130003417737
-
- ISSN
- 0021924X
-
- 本文言語コード
- en
-
- データソース種別
-
- CiNii Articles