Down-regulation of radioresistance by LexA2 in Deinococcus radiodurans.
The extremely radioresistant bacterium Deinococcus radiodurans contains two LexA homologues (LexA1 and LexA2) that are possible transcriptional regulators associated with the DNA damage response. In this study, resequencing revealed that there was an additional cytosine nucleotide (nucleotide position 612) in the D. radiodurans lexA2 gene. Purified LexA2 possessed proteolytic activity that could be stimulated by RecA. In an effort to gain an insight into the role of LexA2 in the radiation response mechanism, recA, lexA1 and lexA2 disruptant strains were generated and investigated. The intracellular level of RecA increased in lexA1 and lexA2 disruptant strains following gamma-irradiation as in the wild-type strain. These results indicated that the two LexA homologues did not possess functional overlap regarding the induction of RecA. The lexA2 disruptant strains exhibited a much higher resistance to gamma-rays than the wild-type strain. Furthermore, a luciferase assay showed that pprA promoter activation was enhanced in the lexA2 disruptant strain following gamma-irradiation. The pprA gene encoding the novel radiation-inducible protein PprA plays a critical role in the radioresistance of D. radiodurans. The increase in radioresistance of the lexA2 disruptant strain is explained in part by the enhancement of pprA promoter activation.
Satoh
Katsuya
K
DNA Repair Protein Group, Quantum Beam Science Directorate, Japan Atomic Energy Agency, 1233 Watanuki, Takasaki 370-1292, Japan.|Gene Resource Research Group, Quantum Beam Science Directorate, Japan Atomic Energy Agency, 1233 Watanuki, Takasaki 370-1292, Japan.
Ohba
Hirofumi
H
DNA Repair Protein Group, Quantum Beam Science Directorate, Japan Atomic Energy Agency, 1233 Watanuki, Takasaki 370-1292, Japan.|Gene Resource Research Group, Quantum Beam Science Directorate, Japan Atomic Energy Agency, 1233 Watanuki, Takasaki 370-1292, Japan.
Sghaier
Haïtham
H
Material Science Laboratory, Department of Biological and Chemical Engineering, Faculty of Engineering, Gunma University, 1-5-1 Tenjin, Kiryu 376-8515, Japan.|Gene Resource Research Group, Quantum Beam Science Directorate, Japan Atomic Energy Agency, 1233 Watanuki, Takasaki 370-1292, Japan.
Narumi
Issay
I
DNA Repair Protein Group, Quantum Beam Science Directorate, Japan Atomic Energy Agency, 1233 Watanuki, Takasaki 370-1292, Japan.|Gene Resource Research Group, Quantum Beam Science Directorate, Japan Atomic Energy Agency, 1233 Watanuki, Takasaki 370-1292, Japan.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D003001:Cloning, Molecular; D003596:Cytosine; D034301:Deinococcus / Q000235:genetics* / Q000528:radiation effects; D015536:Down-Regulation; D005720:Gamma Rays; D017353:Gene Deletion; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D011938:Rec A Recombinases / Q000235:genetics; D016415:Sequence Alignment; D012697:Serine Endopeptidases / Q000235:genetics*; D000099160:LexA Repressor Protein
D001426:Bacterial Proteins; D003596:Cytosine; D011938:Rec A Recombinases; D012697:Serine Endopeptidases; D000099160:LexA Repressor Protein