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Nucleic Acids Research, 1994, Vol. 22, No. 25 5679-5685
© 1994

Articles

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

Reiko Makino, Kosuke Akiyama, Jun Yasuda, Shoji Mashiyama, Soichi Honda, Takao Sekiya and Kenshi Hayashi1,*

Oncogene Division, National Cancer Center Research Institute Tsukiji 5-1-1, Chuo-ku, Tokyo 104 1Division of Genome Analysis, Institute of Genetic Information, Kyushu University Maidashi 3-1-1, Higashi-ku, Fukuoka 812, Japan

*To whom correspondence should be addressed

Received August 19, 1994. Accepted November 14, 1994.

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 amlno acid residues. This protein has two widely separated zinc finger regions, each of which carries C2H2 motifs. When expressed in E.coll 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 proteln-2 (MBP-2/HIV-EP2), based on the 86% similarity in nucleotlde sequence and 93% similarity in amino acid sequence. Northern blotting revealed a high level of MIBP1 mRNA in the brain.


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