Hsp20, a Small Heat Shock Protein of Deinococcus radiodurans, Confers Tolerance to Hydrogen Peroxide in Escherichia coli
2
조회
0
다운로드
0
인용
0
참고문헌
키워드
초록
The present study shows that DR1114 (Hsp20), a small heat shock protein of the radiationresistant bacterium Deinococcus radiodurans, enhances tolerance to hydrogen peroxide (H2O2) stress when expressed in Escherichia coli. A protein profile comparison showed that E. coli cells overexpressing D. radiodurans Hsp20 (EC-pHsp20) activated the redox state proteins, thus maintaining redox homeostasis. The cells also showed increased expression of pseudouridine (psi) synthases, which are important to the stability and proper functioning of structural RNA molecules. We found that the D. radiodurans mutant strain, which lacks a psi synthase (DR0896), was more sensitive to H2O2 stress than wild type. These suggest that an increased expression of proteins involved in the control of redox state homeostasis along with more stable ribosomal function may explain the improved tolerance of EC-pHsp20 to H2O2 stress.
Abstract
The present study shows that DR1114 (Hsp20), a small heat shock protein of the radiationresistant bacterium Deinococcus radiodurans, enhances tolerance to hydrogen peroxide (H2O2) stress when expressed in Escherichia coli. A protein profile comparison showed that E. coli cells overexpressing D. radiodurans Hsp20 (EC-pHsp20) activated the redox state proteins, thus maintaining redox homeostasis. The cells also showed increased expression of pseudouridine (psi) synthases, which are important to the stability and proper functioning of structural RNA molecules. We found that the D. radiodurans mutant strain, which lacks a psi synthase (DR0896), was more sensitive to H2O2 stress than wild type. These suggest that an increased expression of proteins involved in the control of redox state homeostasis along with more stable ribosomal function may explain the improved tolerance of EC-pHsp20 to H2O2 stress.
참고문헌 (26)
- Becker HF, "The yeast gene YNL292w encodes a pseudouridine synthase (PUS4)catalyzing the formation of psi55 in both mitochondrial and cytoplasmic tRNA", Nucleic Acids Res, 25, pp.4493~4499 (1997)
- Bepperling A, "Alternative bacterial two-component small heat shock protein systems", Proc. Natl. Acad. Sci. USA, 109, pp.20407~20412 (2012)
- Del Campo M, "Number, position, and significance of the pseudouridines in the large subunit ribosomal RNA of Haloarcula marismortui and Deinococcus radiodurans", RNA, 11, pp.210~219 (2005)
- DeJong W, "Evolution of the alpha-crystallin", small heat-shock protein family, 1993, pp.10, 103~126
- is essential in Pseudomonas aeruginosa, "BMC Microbiol", 2010, 271~
- Eyles S, "Nature’s molecular sponges: small heat shock proteins grow into their chaperone roles", Proc. Natl. Acad. Sci. USA, 107, pp.2727~2728 (2010)
- Fontecave M, "Iron-sulfur cluster biosynthesis in bacteria: mechanisms of cluster assembly and transfer", Arch. Biochem. Biophys, 474, pp.226~237 (2008)
- Giro M, "An in vivo system co-expressing cyanobacterial flavodoxin and ferredoxin-NADP+ reductase confers increased tolerance to oxidative stress in plants", FEBS Open Bio, 1, pp.7~13 (2011)
- Feder ME, "Heat-shock proteins, molecular chaperones and the stress response: evolutionary and ecological physiology", Annu. Rev. Physiol, 61, pp.243~282 (1999)
- Horwitz J, "Alpha-crystallin can function as a molecular chaperone", Proc. Natl. Acad. Sci. USA, 89, pp.10449~10453 (1992)
- Im S, "Comparative survival analysis of 12 histidine kinase mutants of Deinococcus radiodurans after exposure to DNA-damaging agents", Bioprocess Biosyst. Eng, 36, pp.781~789 (2013)
- Ishihama Y, "Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein", Mol. Cell Proteomics, 4, pp.1265~1272 (2005)
- Kaya Y, "A novel unanticipated type of pseudouridine synthase with homologs in bacteria, archea, and eukarya", RNA, 9, pp.711~721 (2003)
- Kim YH, "Analysis of aromatic catabolic pathways in Pseudomonas putida KT 2440 using a combined proteomic approach : 2-DE", MS and cleavable isotope-coded affinity tag analysis, 2006, pp.6, 1301~1318
- Kinghorn S, "Physiological analysis of the role of truB in Escherichia coli : a role for tRNA modification in extreme temperature resistance", Microbiology, 148, pp.3511~3520 (2002)
- Kota S, "PprA: a protein implicated in radioresistance of Deinococcus radiodurans stimulates catalase activity in Escherichia coli", Appl. Microbiol. Biotechnol, 72, pp.790~796 (2006)
- Li DC, "Thermotolerance and molecular chaperone function of the small heat shock protein HSP20 from hyperthermophilic archaeon, Sulfolobus solfataricus P2", Cell Stress Chaperones, 17, pp.103~108 (2012)
- Makarova K, "Genome of the extremely radiation-resistant bacterium Deinococcus radiodurans viewed from the perspective of comparative genomics", Microbiol. Mol. Biol. Rev, 65, pp.44~79 (2001)
- Ofengand J., "Ribosomal RNA pseudouridines and pseudouridine synthases", FEBS Lett, 514, pp.17~25 (2002)
- Pan J, "IrrE, a global regulator of extreme radiation resistance in Deinococcus radiodurans, enhances salt tolerance in Escherichia coli and Brassica napus", PLoS One, 4, pp.4422~ (2009)
- Rappsilber J, "Large scale proteomic analysis of human spliceosome", Genome Res, 12, pp.1231~1245 (2002)
- Rodriguez-Manzaneque MT, "Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae", Mol. Cell. Biol, 19, pp.8180~8190 (1999)
- Sage AE, "Molecular characterization of mutants affected in osmoprotectant-dependant induction of phospholipase C in Pseudomonas aeruginosa POA1", Mol. Microbiol, 23, pp.43~56 (1997)
- Schmid AK, "Global transcriptional and proteomic analysis of the Sig1 heat shock regulon of Deinococcus radiodurans", J. Bacteriol, 187, pp.3339~3351 (2005)
- Sun Y, "Small heat shock proteins:molecular structure and chaperone function", Cell Mol. Life Sci, 62, pp.2460~2476 (2005)
- Sunita S, "Domain organization and crystal structure of the catalytic domain of E. coli RluF, a pseudouridine synthase that acts on 23S rRNA", J. Mol. Biol, 359, pp.998~1009 (2006)