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      Mutation in recR gene of Deinococcus radiodurans and possible involvement of its product in the repair of DNA interstrand cross-links.

      Mutation Research
      Amino Acid Sequence, Bacteria, genetics, Bacterial Proteins, Base Sequence, Cloning, Molecular, DNA Repair, DNA, Bacterial, Genes, Bacterial, Molecular Sequence Data, Mutation, Sequence Homology, Amino Acid

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          Abstract

          We previously reported that some Deinococcus radiodurans mutants are sensitive to DNA interstrand cross-linking agents but resistant to UV and gamma-rays. We isolated DNA fragments from a D. radiodurans genomic library which complemented the mitomycin C sensitivity of one of these mutants. One 3.2kb-long fragment contains an open reading frame of approximately 700bp and the deduced amino acid sequence is very homologous to other prokaryotic RecR proteins. This open reading frame in the mitomycin C-sensitive mutant strain contains a frame shift mutation at its carboxyl terminal region. These data suggest that RecR protein plays an important role in the resistance to interstrand cross-links in this bacterium.

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