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

Reiko Makino; Kosuke Akiyama; Jun Yasuda; Shoji Mashiyama; Soichi Honda; Takao Sekiya; Kenshi Hayashi

doi:10.1093/nar/22.25.5679

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

Reiko Makino, Kosuke Akiyama, Jun Yasuda, Shoji Mashiyama, Soichi Honda, Takao Sekiya, Kenshi Hayashi

Tohoku Medical Megabank Organization (ToMMo)

Research output: Contribution to journal › Article › peer-review

26 Citations (Scopus)

Abstract

The cDNA for a c-myc intron 1 binding protein 1 (MIBP1) in the rat was Isolated from λgt11 and λZAPII 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.

Original language	English
Pages (from-to)	5679-5685
Number of pages	7
Journal	Nucleic acids research
Volume	22
Issue number	25
DOIs	https://doi.org/10.1093/nar/22.25.5679
Publication status	Published - 1994

ASJC Scopus subject areas

Genetics

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title = "Cloning and characterization of a c-myc intron binding protein (MIBP1)",

abstract = "The cDNA for a c-myc intron 1 binding protein 1 (MIBP1) in the rat was Isolated from λgt11 and λZAPII 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.",

author = "Reiko Makino and Kosuke Akiyama and Jun Yasuda and Shoji Mashiyama and Soichi Honda and Takao Sekiya and Kenshi Hayashi",

note = "Funding Information: We thank the Human Genome Center, Institute of Medical Science, The University of Tokyo for computer analyses of sequences. This work was supported in part by Grants-in-Aid from the Ministry of Health and Welfare of Japan for the Comprehensive 10-Year Strategy for Cancer Control and from the Ministry of Science, Education and Culture of Japan. Copyright: Copyright 2010 Elsevier B.V., All rights reserved.",

year = "1994",

doi = "10.1093/nar/22.25.5679",

language = "English",

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T1 - Cloning and characterization of a c-myc intron binding protein (MIBP1)

AU - Makino, Reiko

AU - Akiyama, Kosuke

AU - Yasuda, Jun

AU - Mashiyama, Shoji

AU - Honda, Soichi

AU - Sekiya, Takao

AU - Hayashi, Kenshi

N1 - Funding Information: We thank the Human Genome Center, Institute of Medical Science, The University of Tokyo for computer analyses of sequences. This work was supported in part by Grants-in-Aid from the Ministry of Health and Welfare of Japan for the Comprehensive 10-Year Strategy for Cancer Control and from the Ministry of Science, Education and Culture of Japan. Copyright: Copyright 2010 Elsevier B.V., All rights reserved.

PY - 1994

Y1 - 1994

N2 - The cDNA for a c-myc intron 1 binding protein 1 (MIBP1) in the rat was Isolated from λgt11 and λZAPII 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.

AB - The cDNA for a c-myc intron 1 binding protein 1 (MIBP1) in the rat was Isolated from λgt11 and λZAPII 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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