The DNA binding domain of the rat liver nuclear protein C/EBP is bipartite

William H. Landschulz; Peter F. Johnson; Steven L. McKnight

doi:10.1126/science.2494700

The DNA binding domain of the rat liver nuclear protein C/EBP is bipartite

William H. Landschulz, Peter F. Johnson, Steven L. McKnight

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542 Scopus citations

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.

Original language	English (US)
Pages (from-to)	1681-1688
Number of pages	8
Journal	Science
Volume	243
Issue number	4899
DOIs	https://doi.org/10.1126/science.2494700
State	Published - 1989

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title = "The DNA binding domain of the rat liver nuclear protein C/EBP is bipartite",

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.",

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AU - Landschulz, William H.

AU - Johnson, Peter F.

AU - McKnight, Steven L.

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AB - 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.

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The DNA binding domain of the rat liver nuclear protein C/EBP is bipartite

Abstract

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