| Autor: |
Andrews, N C, Kotkow, K J, Ney, P A, Erdjument-Bromage, H, Tempst, P, Orkin, S H |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; December 1993, Vol. 90 Issue: 24 p11488-11492, 5p |
| Abstrakt: |
Erythroid transcription factor NF-E2 is a tissue-restricted heterodimeric protein which recognizes an extended AP-1 motif [(T/C)TGCTGA(C/G)TCA(T/C)] found in the upstream locus control regions of the alpha- and beta-globin gene clusters. A cDNA clone encoding a cell-type-specific subunit of NF-E2, designated p45 NF-E2, has previously been characterized and shown to encode a basic-leucine zipper DNA-binding protein. Here we describe protein purification and cloning of cDNA that encodes the second basic-leucine zipper subunit of the native NF-E2 heterodimer. This polypeptide, designated p18, is widely expressed. It displays extensive homology to the v-maf oncogene product and a human retinal-specific protein, NRL. Unusual features in the basic region shared by v-Maf, NRL, and p18 place them in a distinct subfamily of AP-1-like proteins. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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