Abstract
The prfA gene product of Gram-positive bacteria is unusual in being implicated in several cellular processes; cell wall synthesis, chromosome segregation, and DNA recombination and repair. However, no homology of PrfA with other proteins has been evident. Here we report a structural relationship between PrfA and the restriction enzyme PvuII, and thereby produce models that predict that PrfA binds DNA. Indeed, wild-type Bacillus stearothermophilus PrfA, but not a catalytic site mutant, nicked one strand of supercoiled plasmid templates leaving 5'-phosphate and 3'-hydroxyl termini. This activity, much lower on linear or relaxed circular double-stranded DNA or on single-stranded DNA, is consistent with a role for this protein in chromosome segregation, DNA recombination, or DNA repair.
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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Bacillus / genetics
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Bacillus / metabolism*
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Bacillus subtilis / genetics
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Bacillus subtilis / metabolism
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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DNA / metabolism*
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DNA Restriction Enzymes / genetics
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DNA Restriction Enzymes / metabolism*
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Deoxyribonucleases, Type II Site-Specific / genetics
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Escherichia coli Proteins
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Membrane Proteins / metabolism
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Models, Molecular
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Molecular Sequence Data
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Mutation
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Peptide Termination Factors
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Phylogeny
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Protein Conformation
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Sequence Alignment
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Sequence Analysis, Protein
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Trans-Activators / genetics
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Trans-Activators / metabolism*
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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FtsK protein, E coli
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Membrane Proteins
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Peptide Termination Factors
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Trans-Activators
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DNA
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DNA Restriction Enzymes
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CAGCTG-specific type II deoxyribonucleases
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Deoxyribonucleases, Type II Site-Specific