Abstract
FIS protein is involved in several different cellular processes stimulating site-specific recombination in phages Mu and lambda as well as transcription of stable RNA operons in E.coli. We have performed a mutational analysis of fis and provide genetic and biochemical evidence that a truncated version of FIS lacking the N-terminal region is sufficient for specific DNA binding and for stimulating lambda excision. These mutants also retain their ability to autoregulate fis gene expression. Such mutant proteins, however, cannot stimulate the enhancer dependent DNA inversion reaction.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics*
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Bacterial Proteins / metabolism
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Bacteriophage lambda / genetics
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Bacteriophage mu / genetics
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Base Sequence
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Carrier Proteins / chemistry
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Carrier Proteins / genetics*
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Carrier Proteins / metabolism
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Chromosome Inversion*
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DNA Mutational Analysis
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / genetics*
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DNA-Binding Proteins / metabolism
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Enhancer Elements, Genetic / genetics
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Escherichia coli / genetics*
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Escherichia coli Proteins*
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Factor For Inversion Stimulation Protein
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Gene Expression Regulation, Bacterial / genetics
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Integration Host Factors
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Molecular Sequence Data
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Plasmids / genetics
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Recombination, Genetic / genetics*
Substances
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Bacterial Proteins
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Carrier Proteins
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DNA-Binding Proteins
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Escherichia coli Proteins
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Factor For Inversion Stimulation Protein
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Integration Host Factors
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integration host factor, E coli