The Y-box motif mediates redox-dependent transcriptional activation in mouse cells

J Biol Chem. 1995 Dec 22;270(51):30499-507. doi: 10.1074/jbc.270.51.30499.

Abstract

We show here that the OxyR response element (ORE) in the bacterial oxyR promoter can also function as a redox-dependent enhancer in mammalian cells. Fusion of ORE to an SV40 basal promoter driving chloramphenicol acetyltransferase (CAT) expression confers H2O2 inducibility to expression of the cat gene in mouse Hepa-1 hepatoma cells. Nuclear extracts from these cells contain DNA-binding proteins that specifically interact with ORE DNA, cannot be completed by cognate oligonucleotides to AP-1 or NF kappa B, and are constitutively expressed, since treatment with H2O2 causes no detectable changes in binding activity or DNA-protein interaction. Recombinant cDNA clones that express ORE-binding proteins were isolated from a mouse hepatoma expression library and found to be representatives of two different members of the murine Y-box family of transcription factors. Canonical Y-box and ORE oligonucleotides compete with each other for binding to Y-box proteins in gel shift assays and antibodies to FRGY2, a Xenopus Y-box protein, supershift both Y-box and ORE DNA-protein complexes. In addition, antisense oligonucleotides to mouse YB-1 mRNA abolish induction of ORE-mediated cat expression by H2O2, and luciferase reporter constructs containing ORE, or the Y-box from the human MHC class II HLA-DQ gene, exhibit identical dose-dependent H2O2 inducibilities, which can be abolished by addition of 2-mercaptoethanol to the culture medium. These results suggest that the Y-box proteins may be an integral component of a eukaryotic redox signaling pathway.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 3T3 Cells
  • Amino Acid Sequence
  • Animals
  • Bacteria / genetics
  • Base Sequence
  • CCAAT-Enhancer-Binding Proteins*
  • Cell Line
  • Cell Nucleus / metabolism
  • Chloramphenicol O-Acetyltransferase / biosynthesis
  • Cloning, Molecular
  • Consensus Sequence
  • DNA-Binding Proteins / biosynthesis
  • DNA-Binding Proteins / metabolism*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Gene Expression Regulation, Enzymologic / drug effects
  • Genes, MHC Class II*
  • HLA-DQ Antigens / biosynthesis
  • HLA-DQ Antigens / genetics*
  • Humans
  • Hydrogen Peroxide / pharmacology
  • Kinetics
  • Liver Neoplasms, Experimental
  • Male
  • Mice
  • Molecular Sequence Data
  • NFI Transcription Factors
  • Nuclear Proteins
  • Oligodeoxyribonucleotides
  • Oligonucleotides, Antisense / pharmacology
  • Oxidation-Reduction
  • Promoter Regions, Genetic
  • RNA, Messenger / biosynthesis
  • Rats
  • Recombinant Proteins / biosynthesis
  • Sequence Homology, Amino Acid
  • Signal Transduction
  • Simian virus 40 / genetics
  • Testis / metabolism
  • Thionucleotides
  • Transcription Factors / biosynthesis
  • Transcription Factors / metabolism*
  • Transcriptional Activation*
  • Transfection
  • Tumor Cells, Cultured
  • Xenopus
  • Y-Box-Binding Protein 1

Substances

  • CCAAT-Enhancer-Binding Proteins
  • DNA-Binding Proteins
  • HLA-DQ Antigens
  • NFI Transcription Factors
  • Nuclear Proteins
  • Oligodeoxyribonucleotides
  • Oligonucleotides, Antisense
  • RNA, Messenger
  • Recombinant Proteins
  • Thionucleotides
  • Transcription Factors
  • Y-Box-Binding Protein 1
  • YBX1 protein, human
  • Hydrogen Peroxide
  • Chloramphenicol O-Acetyltransferase

Associated data

  • GENBANK/L35549
  • GENBANK/M24069
  • GENBANK/M24070
  • GENBANK/M60419
  • GENBANK/M83888
  • GENBANK/X57621