Blackwell, T K and Kretzner, L and Blackwood, E M and Eisenman, R N and Weintraub, H (1990) Sequence-specific DNA binding by the c-Myc protein. Science (New York, N.Y.), 250 (4984). pp. 1149-1151. ISSN 0036-8075
Abstract
While it has been known for some time that the c-Myc protein binds to random DNA sequences, no sequence-specific binding activity has been detected. At its carboxyl terminus, c-Myc contains a basic--helix-loop-helix (bHLH) motif, which is important for dimerization and specific DNA binding, as demonstrated for other bHLH protein family members. Of those studied, most bHLH proteins bind to sites that contain a CA- -TG consensus. In this study, the technique of selected and amplified binding-sequence (SAAB) imprinting was used to identify a DNA sequence that was recognized by c-Myc. A purified carboxyl-terminal fragment of human c-Myc that contained the bHLH domain bound in vitro in a sequence-specific manner to the sequence, CACGTG. These results suggest that some of the biological functions of Myc family proteins are accomplished by sequence-specific DNA binding that is mediated by the carboxyl-terminal region of the protein.
Item Type: | Article or Abstract |
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Additional Information: | This article is available to Science subscribers only at the link above. |
DOI: | 10.1126/science.2251503 |
PubMed ID: | 2251503 |
Grant Numbers: | T32 CA09437, ROI CA20525 |
Keywords or MeSH Headings: | Base Sequence; Binding Sites; DNA/metabolism; Glutathione Transferase; Leucine Zippers; Macromolecular Substances; Molecular Sequence Data; Oligonucleotides/metabolism; Polymerase Chain Reaction; Protein Conformation; Proto-Oncogene Proteins c-myc/metabolism; Recombinant Fusion Proteins/metabolism; Templates, Genetic; |
Subjects: | Molecules > Molecular structure Molecules > Proteins Molecules > Genes > Oncogenes |
Depositing User: | Library Staff |
Date Deposited: | 03 Dec 2008 22:04 |
Last Modified: | 07 May 2010 18:36 |
URI: | http://authors.fhcrc.org/id/eprint/131 |
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