Abstract
We have isolated a cDNA clone, PU.1, that codes for a new tissue-specific DNA binding protein. Analysis of the binding site by methylation interference and DNAase 1 protection revealed that the PU.1 protein recognized a purine-rich sequence, 5'-GAGGAA-3' (PU box). The PU.1 protein was shown to be a transcriptional activator that is expressed in macrophages and B cells. cDNA constructions used to generate proteins lacking portions of either the amino- or carboxy-terminal ends of the PU.1 protein placed the DNA binding domain in the highly basic carboxy-terminal domain of the protein. The amino acid sequence in the binding domain of PU.1 has considerable identity with proteins belonging to the ets oncogene family.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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B-Lymphocytes / metabolism*
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Base Sequence
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Cell Nucleus / metabolism
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Cloning, Molecular
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DNA / genetics
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DNA / isolation & purification
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DNA-Binding Proteins / genetics*
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Gene Expression Regulation
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Gene Library
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Genes*
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Immunoblotting
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Macrophages / metabolism*
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Methylation
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Mice
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Molecular Sequence Data
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Nucleic Acid Hybridization
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Oligonucleotide Probes
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Protein Biosynthesis
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Protein Conformation
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Protein-Tyrosine Kinases / genetics
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Proto-Oncogene Proteins / genetics*
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Proto-Oncogene Proteins c-ets
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Proto-Oncogenes*
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Restriction Mapping
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Retroviridae Proteins, Oncogenic
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Sequence Homology, Nucleic Acid
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Transcription Factors / genetics*
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Transcription, Genetic
Substances
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DNA-Binding Proteins
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Oligonucleotide Probes
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Proto-Oncogene Proteins
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Proto-Oncogene Proteins c-ets
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Retroviridae Proteins, Oncogenic
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Transcription Factors
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v-Spi-1 protein, Friend spleen focus-forming virus
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DNA
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Protein-Tyrosine Kinases