Abstract
A novel method was developed for cloning of zinc-binding proteins. We used 65Zn2+ as a probe to screen a human lung cDNA library, and isolated QM using this approach. QM appears to be a negative regulator of c-Jun that acts by binding to the leucine zipper region of c-Jun. We demonstrated that QM bound zinc ions and that such binding was necessary for the interaction of QM with c-Jun. We also showed that protein kinase C introduced about 1 mol of phosphate into 1 mol of QM. The binding of QM to c-Jun was decreased by 60% when QM had been phosphorylated. These results suggest that QM is a novel zinc-binding transcription regulatory protein and that interaction between QM and c-Jun is regulated by zinc ions and phosphorylation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Cloning, Molecular
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DNA Primers
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DNA, Complementary
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DNA-Binding Proteins / biosynthesis
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DNA-Binding Proteins / isolation & purification
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DNA-Binding Proteins / metabolism*
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Gene Library
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Glutathione Transferase
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Humans
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Kinetics
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Leucine Zippers
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Lung / metabolism
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Phosphorylation
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Polymerase Chain Reaction
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Protein Kinase C / metabolism*
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Proto-Oncogene Proteins c-jun / metabolism*
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Recombinant Fusion Proteins / biosynthesis
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Recombinant Fusion Proteins / isolation & purification
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Recombinant Fusion Proteins / metabolism
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Ribosomal Protein L10
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Ribosomal Proteins
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Transcription Factors / biosynthesis
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Transcription Factors / isolation & purification
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Transcription Factors / metabolism*
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Tumor Suppressor Proteins
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Zinc / metabolism*
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Zinc / pharmacology
Substances
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DNA Primers
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DNA, Complementary
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DNA-Binding Proteins
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Proto-Oncogene Proteins c-jun
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RPL10 protein, human
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Recombinant Fusion Proteins
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Ribosomal Proteins
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Transcription Factors
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Tumor Suppressor Proteins
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Glutathione Transferase
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Protein Kinase C
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Zinc