Abstract
A novel RecA-like protein, differing from Dmc1 and Rad51, was characterized in Oryza sativa L. cv. Nipponbare. Because the protein is homologous to bacterial RadA, the gene was designated OsRadA. The open reading frame was predicted to encode a 66kDa protein of 619 amino acid residues and was found in plants but not animals or yeast. OsRadA showed D-loop and single-stranded DNA-dependent ATPase activities. Gene expression was found to be high in meristematic tissues, and was localized in the nucleus. An RNAi mutant of Arabidopsis thaliana RadA (AtRadA) was sensitive to mutagenic agents such as UV and MMC, suggesting that RadA functions in DNA repair.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Arabidopsis / drug effects
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Arabidopsis / radiation effects
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Arabidopsis Proteins / drug effects
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Arabidopsis Proteins / genetics
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Arabidopsis Proteins / metabolism
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Arabidopsis Proteins / radiation effects
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Archaeal Proteins / chemistry
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Archaeal Proteins / metabolism
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism
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Cell Proliferation
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Cloning, Molecular
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DNA Repair / physiology*
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / metabolism
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Gene Expression Regulation, Plant
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Mitomycin / adverse effects
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Molecular Sequence Data
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Mutation
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Oryza / cytology
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Oryza / genetics*
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Plant Proteins / genetics*
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Plant Proteins / metabolism*
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Rec A Recombinases / chemistry
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Rec A Recombinases / metabolism
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Sequence Homology, Amino Acid
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Subcellular Fractions
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Ultraviolet Rays / adverse effects
Substances
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Arabidopsis Proteins
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Archaeal Proteins
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Bacterial Proteins
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DNA-Binding Proteins
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Plant Proteins
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RadA protein, archaeal
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RadA protein, bacteria
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Mitomycin
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Rec A Recombinases