Published online 1 February 2005
Article |
Fibroin-modulator-binding protein-1 (FMBP-1) contains a novel DNA-binding domain, repeats of the score and three amino acid peptide (STP), conserved from Caenorhabditis elegans to humans
1 Center for Advanced Science and Technology and Hokkaido University North 10, West 8, Kita-ku, Sapporo 060-0810, Japan 2 Graduate School of Environmental Earth Science, Hokkaido University North 10, West 8, Kita-ku, Sapporo 060-0810, Japan 3 National Institute for Basic Biology Nishigo-naka 38, Okazaki 444-8585, Japan
*To whom correspondence should be addressed. Tel: +81 11 706 3590; Fax: +81 11 737 0536; Email: takiya{at}rmg.hokudai.ac.jp
Received October 14, 2004. Revised January 18, 2004. Accepted January 18, 2004.
The predicted transcriptional regulatory factor for the fibroin gene of the silkworm Bombyx mori, fibroin-modulator-binding protein-1 (FMBP-1), was purified by sequential DNA affinity column chromatography, and cDNA clones corresponding to FMBP-1 were isolated from a library. The N-terminal half of FMBP-1 has a weak similarity to the DNA-binding domain of several transcriptional regulatory factors in higher plants. The C-terminal half contains four tandem repeats of a novel 23 amino acid motif, which we named the score and three amino acid peptide (STP). Other genes containing STP repeats were found in Drosophila, Caenorhabditis elegans, mouse and human. Mutational analysis of FMBP-1 showed that the STP repeats form a novel DNA-binding domain. Sequences flanking STP repeats modulated DNA-binding activity. The FMBP-1 gene was expressed during the fourth to fifth instar. FMBP-1 activity appeared to be regulated at the transcriptional level and by the post-transcriptional modification.
Present address: Yoshiaki Suzuki, 5651-451 Matsukawa Village, North Azumi County, Nagano Prefecture 399-8501, Japan
DDBJ/EMBL/GenBank accession no. AB163434
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