| Autor: |
Uno T; Laboratory of Biological Chemistry, Department of Biofunctional Chemistry, Faculty of Agriculture, Kobe University, Nada-ku, Kobe, Hyogo, 657-8501, Japan. uno_tom@yahoo.co.jp, Nomura Y, Nakamura M, Nakao A, Tajima S, Kanamaru K, Yamagata H, Iwanaga Y |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of insect science (Online) [J Insect Sci] 2005; Vol. 5, pp. 8. |
| DOI: |
10.1093/jis/5.1.8 |
| Abstrakt: |
A cDNA clone encoding methyl DNA binding domain-containing protein (bMBD2/3) was obtained by homology searches using a Bombyx mori fat body cDNA library. The cDNA encoded a polypeptide with 249 amino acids sharing 54% similarity with the methyl DNA binding protein from Drosophila melanogaster. To characterize the biochemical properties of bMBD2/3, the clone was expressed in Escherichia coli as His-tagged protein. The recombinant protein was purified to homogeneity using Ni-NTA superflow resin and heparin agarose. The protein showed specific methyl DNA binding activity and was phosphorylated by protein kinase in vitro. Immunoblotting using the purified antibody indicated that bMBD2/3 was expressed in almost all tissues. Using west-western blotting analysis, some proteins that interact with bMBD2/3 were identified in the brain. This is the first report that insect MBD is phosphorylated and is present in adult tissues. These results suggest that bMBD2/3 plays important roles in the DNA methylation-specific transcription of Bombyx mori. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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