The DNA Binding Domain of the Rat Liver Nuclear Protein C/EBP Is Bipartite
- 31 March 1989
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 243 (4899), 1681-1688
- https://doi.org/10.1126/science.2494700
Abstract
C/EBP is a rat liver nuclear protein capable of sequence-specific interaction with DNA. The DNA sequences to which C/EBP binds in vitro have been implicated in the control of messenger RNA synthesis. It has therefore been predicted that C/EBP will play a role in regulating gene expression in mammalian cells. The region of the C/EBP polypeptide required for direct interaction with DNA has been identified and shown to bear amino acid sequence relatedness with the product of the myc, fos, and jun proto-oncogenes. The arrangement of these related amino acid sequences led to the prediction of a new structural motif, termed the "leucine zipper," that plays a role in facilitating sequence-specific interaction between protein and DNA. Experimental tests now provide support for the leucine zipper hypothesis.Keywords
This publication has 36 references indexed in Scilit:
- Parallel Association of Fos and Jun Leucine Zippers Juxtaposes DNA Binding DomainsScience, 1989
- The role of the leucine zipper in the fos–jun interactionNature, 1988
- Fos and Jun bind cooperatively to the AP-1 site: reconstitution in vitro.Genes & Development, 1988
- Isolation of a recombinant copy of the gene encoding C/EBP.Genes & Development, 1988
- The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding ProteinsScience, 1988
- Saturation Mutagenesis of the Yeast his3 Regulatory Site: Requirements for Transcriptional Induction and for Binding by GCN4 Activator ProteinScience, 1986
- Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genesJournal of Molecular Biology, 1986
- The primary structure of transcription factor TFIIIA has 12 consecutive repeatsFEBS Letters, 1985
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences of the United States of America, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970