Journal of Biochemistry Advance Access originally published online on May 14, 2009
Journal of Biochemistry 2009 146(3):337-342; doi:10.1093/jb/mvp072
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RecX is Involved In the Switch between DNA Damage Response and Normal Metabolism in D. radiodurans
1State Key Laboratory of Microbial Technology, Shandong University, 250100 Jinan, China; and 2Institute of Nuclear-Agricultural Sciences, Zhejiang University, 310029 Hangzhou, China
*To whom correspondence should be addressed. Tel: +13-658612032, Fax: 086-531-88362928, E-mail: dhsheng{at}sdu.edu.cn
Received April 14, 2009; Accepted May 7, 2009
| Abstract |
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Apart from inhibiting RecA activity through protein–protein interactions, Deinococcus radiodurans RecX inhibits the expression of RecA and two other anti-oxidant proteins. To identify the repertoire of proteins regulated by RecX, comparative proteomic studies were undertaken on a wild-type strain (R1) and recX null mutant (RecX–). Two-dimensional electrophoresis followed by MALDI-TOF identification revealed 35 differentially expressed proteins, including 12 up-regulated and 23 down-regulated proteins in the mutant. The 12 up-regulated proteins are DNA repair proteins, stress response proteins, and metabolism-related proteins. Most of these have been previously characterized as ionizing radiation-induced proteins. The 23 down-regulated proteins are mainly involved in cellular metabolism, and some of these are key enzymes in the metabolic pathway. Thus, RecX is suggested to be involved in the switch between DNA damage response and normal metabolism in D. radiodurans.
Key Words: Deinococcus radiodurans, DNA repair, RecX, two-dimensional electrophoresis
Abbreviations: ACN, acetonitrile; CHAPS, 3-[(3-cholamidopropyl)dimethylammonio]-1-propane sulphonate; 2DE, two-dimensional electrophoresis; DTT, dithiothreitol; IR, ionizing radiation; MALDI, matrix-assisted laser desorption ionization mass spectroscopy; PAGE, polyacrylamide gel electrophoresis; SDS, sodium dodecyl sulfate; TFA, trifluoroacetic acid