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Pleiotropic effects of a cold shock protein homolog PprM on the proteome of Deinococcus radiodurans
Affiliation:1. Molecular Biology Division, Bhabha Atomic Research Centre, Mumbai 400085, India;2. Homi Bhabha National Institute, Training School Complex, Anushakti Nagar, Mumbai 400094, India;1. Department of Functional Molecular Science, Graduate School of Biomedical & Health Sciences, Hiroshima University, Kasumi 1-2-3, Minami-ku, Hiroshima 734-8553, Japan;2. Advanced Medical Research Center, Yokohama City University, Fukuura 3-9, Kanazawa-ku, Yokohama 236-0004, Japan;1. Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, United States;2. Department of Chemistry, Davidson College, Davidson, NC 28035, United States;1. Department of Chemistry, East Carolina University, Greenville, NC 27858, USA;2. Center of Interdisciplinary Magnetic Resonance (CIMAR), National High Magnetic Field Laboratory (NHMFL), 1800 East, Paul Dirac Dr., Tallahassee, FL 32310, USA
Abstract:An extremophile D. radiodurans encodes a non-cold shock inducible cold shock protein homolog DR_0907 (also known as PprM). The DR_0907 ORF was deleted by knockout mutagenesis and the resultant deletion mutant (ΔpprM D. radiodurans) displayed growth defect as well as gamma-radiation sensitivity (D10 values = ΔpprM D. radiodurans: 12.1 kGy versus wild type (WT) D. radiodurans: 14 kGy). 2D gel based comparative proteomics revealed a comparable induction of DNA repair proteins in ΔpprM D. radiodurans and WT D. radiodurans recovering from 5 kGy gamma irradiation (60Co gamma source, dose rate: 2 kGy/h), suggesting that pprM does not cause radiation sensitivity through modulation of DdrO-regulated DNA repair genes. However, deletion of pprM did result in repression of several proteins that belonged to vital housekeeping pathways such as metabolism and protein homeostasis that might contribute to slow growth phenotype. These deficiencies intrinsic to ΔpprM D. radiodurans might also contribute to its radiation sensitivity.
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