Abstract
Two forms of the transcription factor vHNF1 (HNF1 beta or LFB3) have been previously described, derived by alternative splicing from a common premessenger RNA, and have been called vHNF1-A and vHNF1-B. vHNF1 proteins share a homologous homeo-related DNA-binding domain with the HNF1 protein, initially characterized as a liver-restricted transcription factor, and bind to a similar sequence motif. Here we demonstrate that vHNF1-A is a stronger transactivator than vHNF1-B when assayed in transient transfections using two different promoters. vHNF1-A also binds DNA with a higher affinity suggesting that a region of the protein located immediately upstream of the homeodomain can modulate the protein/DNA interaction and transactivation. Both vHNF1 transcripts were found at a constant ratio in every tissue where vHNF1 expression could be detected, using a quantitative reverse transcriptase-polymerase chain reaction.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Base Sequence
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Binding, Competitive
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Cell Line
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DNA Primers
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DNA-Binding Proteins / biosynthesis
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DNA-Binding Proteins / metabolism*
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Female
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Genetic Variation
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Hepatocyte Nuclear Factor 1
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Hepatocyte Nuclear Factor 1-alpha
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Hepatocyte Nuclear Factor 1-beta
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Humans
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Kinetics
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Macromolecular Substances
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Molecular Sequence Data
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Nuclear Proteins*
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Oligodeoxyribonucleotides / metabolism
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Oligodeoxyribonucleotides / pharmacology
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Organ Specificity
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Polymerase Chain Reaction
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Rats
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Transcription Factors / biosynthesis
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Transcription Factors / metabolism*
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Transcription, Genetic
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Transfection
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Tumor Cells, Cultured
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Uterine Cervical Neoplasms
Substances
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DNA Primers
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DNA-Binding Proteins
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HNF1A protein, human
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HNF1B protein, human
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Hepatocyte Nuclear Factor 1-alpha
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Hnf1a protein, rat
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Macromolecular Substances
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Nuclear Proteins
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Oligodeoxyribonucleotides
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Transcription Factors
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Hepatocyte Nuclear Factor 1
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Hepatocyte Nuclear Factor 1-beta