Abstract
The recombinases of the RecA family are often viewed only as DNA-pairing proteins - they bind to one DNA segment, align it with homologous sequences in another DNA segment, promote an exchange of DNA strands and then dissociate. To a first approximation, this description seems to fit the eukaryotic (Rad51 and Dmc1) and archaeal (RadA) RecA homologues. However, the bacterial RecA protein does much more, coupling ATP hydrolysis with DNA-strand exchange in a manner that greatly expands its repertoire of activities. This article explores the protein activities and experimental results that have identified RecA as a motor protein.
Publication types
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Research Support, N.I.H., Extramural
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Review
MeSH terms
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Adenosine Triphosphate / metabolism
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics*
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Bacterial Proteins / physiology
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DNA Replication*
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DNA, Bacterial / genetics
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DNA, Bacterial / metabolism
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Gene Expression Regulation, Bacterial*
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Gene Expression Regulation, Enzymologic*
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Hydrolysis
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Models, Genetic
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Molecular Motor Proteins / chemistry
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Molecular Motor Proteins / genetics*
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Molecular Motor Proteins / physiology
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Rec A Recombinases / chemistry
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Rec A Recombinases / genetics*
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Rec A Recombinases / physiology
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Structure-Activity Relationship
Substances
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Bacterial Proteins
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DNA, Bacterial
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Molecular Motor Proteins
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Adenosine Triphosphate
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Rec A Recombinases