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Sequence‐specific DNA binding activity in the RAE28 protein, a mouse homologue of the Drosophila polyhomeotic protein
Author(s) -
Nomura Midori,
Takihara Yoshihiro,
Motaleb Abdul,
Horie Kyoji,
Higashinakagawa Toru,
Shimada Kazunori
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800204452
Subject(s) - fusion protein , biology , microbiology and biotechnology , gene , oligonucleotide , consensus sequence , dna , nuclear protein , ddb1 , binding protein , hmg box , dna binding protein , peptide sequence , genetics , recombinant dna , transcription factor
The rae28 gene, a mouse homologue of the Drosophila polyhomeotic gene, is involved in the maintenance of the transcriptional repression states of Hox genes. In this study we synthesized the glutathione S transferase‐RAE28 (GST‐RAE28) fusion protein and examined sequence‐specific DNA binding activity in the RAE28 protein by using the selected and amplified binding site method. After five rounds of enrichment, the eluted DNAs were amplified, cloned and sequenced. The sequences of individual oligonucleotides included the following consensus sequences; 5′‐ACCA‐3′, 5′‐ACCCA‐3′, 5′‐CTATCA‐3′ and 5′‐TGCC‐3′. The oligonucleotides including these consensus sequences were show to have significant affinity with the GST‐RAE28 fusion protein. The RAE28 protein was recently shown to form multimeric protein complexes with other members of mouse Pc‐G proteins in the nucleus. These findings strongly suggest that the RAE28 protein constitutes a sequence‐specific DNA binding domain in multimeric Pc‐G protein complexes.