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      A novel octamer binding transcription factor is differentially expressed in mouse embryonic cells

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      Cell
      Elsevier BV

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          Abstract

          We have identified a novel octamer binding factor (Oct-3) in P19 embryonal carcinoma cells. Oct-3, which recognizes the typical octamer motif (ATTTGCAT) as well as the AT-rich sequence TTAAAATTCA, is present in P19 stem cells but disappears when the cells are induced to differentiate by retinoic acid (RA). Cloned cDNA corresponding to Oct-3 encodes a protein of 377 amino acids. Oct-3 has a conserved POU domain, but the remaining part is distinct from other POU domain-containing proteins such as Oct-1 and Oct-2. mRNA of 1.5 kb coding for Oct-3 is abundant in P19 stem cells but is dramatically repressed during RA-induced differentiation. Repression of the 1.5 kb mRNA is rapid and specific to RA. In mouse, oct-3 mRNA is undetectable in all the adult organs examined. The N-terminal proline-rich region of Oct-3, when fused to the DNA binding domain of c-Jun, functions as a transcriptional activating domain. We suggest that Oct-3 is a novel octamer binding transcription factor that is developmentally regulated during mouse embryogenesis.

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          Most cited references35

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          Multiple nuclear factors interact with the immunoglobulin enhancer sequences

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            Transcriptional regulation in mammalian cells by sequence-specific DNA binding proteins

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              The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins.

              A 30-amino-acid segment of C/EBP, a newly discovered enhancer binding protein, shares notable sequence similarity with a segment of the cellular Myc transforming protein. Display of these respective amino acid sequences on an idealized alpha helix revealed a periodic repetition of leucine residues at every seventh position over a distance covering eight helical turns. The periodic array of at least four leucines was also noted in the sequences of the Fos and Jun transforming proteins, as well as that of the yeast gene regulatory protein, GCN4. The polypeptide segments containing these periodic arrays of leucine residues are proposed to exist in an alpha-helical conformation, and the leucine side chains extending from one alpha helix interdigitate with those displayed from a similar alpha helix of a second polypeptide, facilitating dimerization. This hypothetical structure is referred to as the "leucine zipper," and it may represent a characteristic property of a new category of DNA binding proteins.
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                Author and article information

                Journal
                Cell
                Cell
                Elsevier BV
                00928674
                February 1990
                February 1990
                : 60
                : 3
                : 461-472
                Article
                10.1016/0092-8674(90)90597-8
                1967980
                daa7679b-1834-42e3-b3ac-90be053d2bf1
                © 1990

                https://www.elsevier.com/tdm/userlicense/1.0/

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