Title |
PprM is necessary for up-regulation of katE1, encoding the major catalase of Deinococcus radiodurans, under unstressed culture conditions |
Author |
Sun-Wook Jeong1,2, Ho Seong Seo1, Min-Kyu Kim1, Jong-Il Choi3, Heon-Man Lim2, and Sangyong Lim1* |
Address |
1Research Division for Biotechnology, Korea Atomic Energy Research Institute, Jeongeup 56212, Republic of Korea, 2Department of Biological Sciences, College of Biological Sciences and Biotechnology, Chungnam National University, Daejeon 34134, Republic of Korea, 3Department of Biotechnology and Bioengineering, Chonnam National University, Gwangju 61186, Republic of Korea |
Bibliography |
Journal of Microbiology, 54(6),426-431, 2016,
|
DOI |
10.1007/s12275-016-6175-8
|
Key Words |
PprM, cold-shock protein, ROS, katE1, catalase
activity |
Abstract |
Deinococcus radiodurans is a poly-extremophilic organism,
capable of tolerating a wide variety of different stresses, such
as gamma/ultraviolet radiation, desiccation, and oxidative
stress. PprM, a cold shock protein homolog, is involved in
the radiation resistance of D. radiodurans, but its role in the
oxidative stress response has not been investigated. In this
study, we investigated the effect of pprM mutation on catalase
gene expression. pprM disruption decreased the mRNA and
protein levels of KatE1, which is the major catalase in D. radiodurans,
under normal culture conditions. A pprM mutant
strain (pprMMT) exhibited decreased catalase activity, and its
resistance to hydrogen peroxide (H2O2) decreased accordingly
compared with that of the wild-type strain. We confirmed
that RecG helicase negatively regulates katE1 under normal
culture conditions. Among katE1 transcriptional regulators,
the positive regulator drRRA was not altered in pprM-, while
the negative regulators perR, dtxR, and recG were activated
more than 2.5-fold in pprMMT. These findings suggest that
PprM is necessary for KatE1 production under normal culture
conditions by down-regulation of katE1 negative regulators. |