COGNATE DNA-BINDING SPECIFICITY RETAINED AFTER LEUCINE ZIPPER EXCHANGE BETWEEN GCN4 AND C/EBP
COGNATE DNA-BINDING SPECIFICITY RETAINED AFTER LEUCINE ZIPPER EXCHANGE BETWEEN GCN4 AND C/EBP
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DOI:
10.1126/science.2530632
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发表时间:
1989-11-17
期刊:
影响因子:
56.9
通讯作者:
MCKNIGHT, SL
中科院分区:
文献类型:
--
作者:
AGRE, P;JOHNSON, PF;MCKNIGHT, SL
Both C/EBP and GCN4 are sequence-specific DNA binding proteins that control gene expression. Recent evidence implicates C/EBP as a transcriptional regulator of genes involved in lipid and carbohydrate metabolism. The C/EBP protein binds avidly to the dyad symmetric sequence 5''-ATTGCGCAAT-3''; GCN4 regulates the transcription of genes that control amino acid biosynthesis in yeast, and binds avidly to the dyad symmetric sequence 5''-ATGA(G/C)TCAT-3''. Both C/EBP and GCN4 bind DNA via the same structural motif. This motif has been predicted to be bipartite, consisting of a dimerization interface termed the "leucine zipper" and a DNA contact surface termed the "basic region." Specificity of DNA binding has been predicted to be imparted by the basic region. As a test of this hypothesis, recombinant proteins were created wherein the basic regions and leucine zippers of GCN4 and C/EBP were reciprocally exchanged. In both of the recombinant polypeptides, DNA binding specificity is shown to track with the basic region.