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. 1994 Dec 25;22(25):5679–5685. doi: 10.1093/nar/22.25.5679

Cloning and characterization of a c-myc intron binding protein (MIBP1).

R Makino 1, K Akiyama 1, J Yasuda 1, S Mashiyama 1, S Honda 1, T Sekiya 1, K Hayashi 1
PMCID: PMC310133  PMID: 7838722

Abstract

The cDNA for a c-myc intron 1 binding protein 1 (MIBP1) in the rat was isolated from lambda gt11 and lambda ZAPII cDNA libraries. Sequencing of the cDNA clones revealed a long ORF which encoded a putative protein of 2437 amino acid residues. This protein has two widely separated zinc finger regions, each of which carries C2H2 motifs. When expressed in E. coli as a fusion protein, part of the MIBP1 showed sequence-specific binding to the target sequence, i.e., a 9-bp sequence in the rat c-myc intron 1. MIBP1 is most likely the rat counterpart of human MHC binding protein-2 (MBP-2/HIV-EP2), based on the 86% similarity in nucleotide sequence and 93% similarity in amno acid sequence. Northern blotting revealed a high level of MIBP1 mRNA in the brain.

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