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fos/jun and octamer-binding protein interact with a common site in a negative element of the human c-myc gene

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/72477

Title: fos/jun and octamer-binding protein interact with a common site in a negative element of the human c-myc gene
Authors: Takimoto, Masato Browse this author →KAKEN DB
Quinn, John P. Browse this author
Farina, A. Rosella Browse this author
Staudt, Louis M. Browse this author
Levens, David Browse this author
Issue Date: 25-May-1989
Publisher: American Society for Biochemistry and Molecular Biology
Journal Title: The Journal of biological chemistry
Volume: 264
Issue: 15
Start Page: 8992
End Page: 8999
PMID: 02498322
Abstract: A negative element has previously been localized to a 57-base pair segment approximately 300 base pairs upstream of the human c-myc promoter P1. Within this element, a 26-base pair region was protected in vitro from DNase I digestion with a HeLa cell nuclear factor(s). Two specific DNA-protein complexes were identified in gel retardation assays using HeLa cell nuclear extracts and an oligonucleotide probe spanning the footprinted region. Exonuclease and chemical footprint analyses suggested that the binding sites for both complexes are almost entirely overlapping. One of the complexes was eliminated by oligonucleotide competitors possessing known AP-1 binding sites. This same complex reacted strongly with anti-fos immunoglobulin suggesting a role for c-fos in governing c-myc expression. Precipitation of fos protein bound to c-myc DNA that was immobilized on beads confirmed the involvement of c-fos in a specific complex with the c-myc upstream sequence. In contrast, the other complex seen by the c-myc probe could not be competitively inhibited by AP-1 binding sites and was not affected by anti-fos antibody. Instead, this complex was efficiently eliminated by unlabeled oligonucleotides containing the octamer DNA motif found in immunoglobulin gene promoters. Purified octamer-binding proteins formed stable complexes with the 26-base pair c-myc sequences. These results demonstrate that degeneracy in the consensus recognition sequences of these distinct factors allows each of them to bind the c-myc negative element. The interaction of known transcriptional activators with a negative element suggests that the same factors can mediate both transcriptional activation and repression.
Rights: This research was originally published in the Journal of Biological Chemistry. M Takimoto, J P Quinn, A R Farina, L M Staudt and D Levens. fos/jun and octamer-binding protein interact with a common site in a negative element of the human c-myc gene. J. Biol. Chem. 1989; 264:8992-8999. © the American Society for Biochemistry and Molecular Biology
Relation: http://www.jbc.org/content/264/15/8992.abstract
Type: article
URI: http://hdl.handle.net/2115/72477
Appears in Collections:遺伝子病制御研究所 (Institute for Genetic Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 瀧本 将人

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