DRA0336, another OxyR homolog, involved in the antioxidation mechanisms in Deinococcus radiodurans.
A novel OxyR (DR0615) with one conserved cysteine that senses hydrogen peroxide in Deinococcus radiodurans had been identified in our previous work. Comparative genomics revealed that D. radiodurans possesses another OxyR homolog, OxyR(2) (DRA0336). In this study, we constructed the deletion mutant of oxyR(2) and the double mutant of both the OxyR homologs to investigate the role of OxyR in response to oxidative stress in D. Radiodurans. Deletion of oxyR(2) resulted in an obviously increased sensitivity to hydrogen peroxide, and the double mutant for oxyR and oxyR(2) was significantly more sensitive than any of the two single mutants. The total catalase activity of the double mutant was lower than that of any of the single mutants, and reactive oxygen species (ROS) accumulated to a greater extent. DNA microarray analysis further suggested that oxyR(2) was involved in antioxidation mechanisms. Site-direct mutagenesis and complementation analysis revealed that C(228) in OxyR(2) was essential. This is the first report of the presence of two OxyR in one organism. These results suggest that D. radiodurans OxyR and OxyR(2) function together to protect the cell against oxidative stress.
Yin
Longfei
L
Key Laboratory for Nuclear-Agricultural Sciences of Chinese Ministry of Agriculture and Zhejiang Province, Institute of Nuclear-Agricultural Sciences, Zhejiang University, Hangzhou, P. R. China.
Wang
Liangyan
L
Lu
Huiming
H
Xu
Guangzhi
G
Chen
Huan
H
Zhan
Hongdan
H
Tian
Bing
B
Hua
Yuejin
Y
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002374:Catalase / Q000378:metabolism; D034301:Deinococcus / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D006861:Hydrogen Peroxide / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D016415:Sequence Alignment
D001426:Bacterial Proteins; D012097:Repressor Proteins; D006861:Hydrogen Peroxide; D002374:Catalase
FEMS Microbiol Rev. 2005 Apr;29(2):361-75
15808748
Mol Microbiol. 2002 Jul;45(1):9-15
12100544
Proc Natl Acad Sci U S A. 1989 May;86(10):3484-8
2471187
FEMS Microbiol Lett. 2007 Jun;271(1):118-25
17419762
Microbiol Mol Biol Rev. 2001 Mar;65(1):44-79
11238985
J Bacteriol. 2001 Aug;183(15):4571-9
11443092
J Bacteriol. 1983 Sep;155(3):1200-7
6411683
FEMS Microbiol Lett. 2005 Mar 15;244(2):251-7
15766776
Biochem Biophys Res Commun. 2003 Jun 27;306(2):354-60
12804570
Science. 1999 Sep 3;285(5433):1558-62
10477518
Mol Microbiol. 2008 Mar;67(6):1211-22
18208531
Appl Microbiol Biotechnol. 2006 Oct;72(4):790-6
16586106
Proc Natl Acad Sci U S A. 2002 May 14;99(10):6690-5
11983871
Trends Biotechnol. 2001 Mar;19(3):109-14
11179804
J Bacteriol. 1995 Mar;177(5):1285-91
7868603
PLoS One. 2008 Feb 13;3(2):e1602
18270589
Annu Rev Microbiol. 2003;57:395-418
14527285
Cell. 2001 Apr 6;105(1):103-13
11301006
J Bacteriol. 2001 Aug;183(15):4562-70
11443091
Science. 1998 Mar 13;279(5357):1718-21
9497290
Curr Opin Microbiol. 1999 Apr;2(2):188-94
10322176
Arch Biochem Biophys. 1989 Nov 15;275(1):244-51
2817898
Mutat Res. 1999 Oct 22;435(2):151-61
10556595
Proc Natl Acad Sci U S A. 1999 May 25;96(11):6161-5
10339558
Nat Rev Microbiol. 2005 Nov;3(11):882-92
16261171
J Biol Chem. 2004 Nov 19;279(47):48742-50
15361522
J Bacteriol. 2006 Dec;188(24):8335-42
17012382
Crit Rev Biochem Mol Biol. 2008 May-Jun;43(3):221-38
18568848