메뉴 건너뛰기




Volumn 6, Issue 3, 2015, Pages 1-8

Novel mechanism for scavenging of hypochlorite involving a periplasmic methionine-rich peptide and methionine sulfoxide reductase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; HYPOCHLORITE; METHIONINE; METHIONINE RICH PERIPLASMIC PROTEIN MRPX; METHIONINE SULFOXIDE REDUCTASE YEDY1; OXIDOREDUCTASE; PERIPLASMIC PROTEIN; PROTEIN NRSF; PROTEIN SIGF; TRANSCRIPTOME; UNCLASSIFIED DRUG; HYPOCHLOROUS ACID; METHIONINE SULFOXIDE REDUCTASE; SIGMA FACTOR;

EID: 84936951713     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00233-15     Document Type: Article
Times cited : (39)

References (42)
  • 2
    • 84884528066 scopus 로고    scopus 로고
    • Bacterial responses to reactive chlorine species
    • Gray MJ, Wholey W-Y, Jakob U. 2013. Bacterial responses to reactive chlorine species. Annu Rev Microbiol 67:141-160. http://dx.doi.org/ 10.1146/annurev-micro-102912-142520.
    • (2013) Annu Rev Microbiol , vol.67 , pp. 141-160
    • Gray, M.J.1    Wholey, W.-Y.2    Jakob, U.3
  • 3
    • 3142726522 scopus 로고    scopus 로고
    • Microbial perchlorate reduction: Rocket-fueled metabolism
    • Coates JD, Achenbach LA. 2004. Microbial perchlorate reduction: rocket-fueled metabolism. Nat Rev Microbiol 2:569-580. http:// dx.doi.org/10.1038/nrmicro926.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 569-580
    • Coates, J.D.1    Achenbach, L.A.2
  • 4
    • 0032729246 scopus 로고    scopus 로고
    • Purification and characterization of (per)chlorate reductase from the chlorate-respiring strain GR-1
    • Kengen SW, Rikken GB, Hagen WR, van Ginkel CG, Stams AJ. 1999. Purification and characterization of (per)chlorate reductase from the chlorate-respiring strain GR-1. J Bacteriol 181:6706-6711.
    • (1999) J Bacteriol , vol.181 , pp. 6706-6711
    • Kengen, S.W.1    Rikken, G.B.2    Hagen, W.R.3    van Ginkel, C.G.4    Stams, A.J.5
  • 5
    • 0029801773 scopus 로고    scopus 로고
    • Purification and characterization of chlorite dismutase: A novel oxygen-generating enzyme
    • Van Ginkel CG, Rikken GB, Kroon AG, Kengen SW. 1996. Purification and characterization of chlorite dismutase: a novel oxygen-generating enzyme. Arch Microbiol 166:321-326. http://dx.doi.org/10.1007/ s002030050390.
    • (1996) Arch Microbiol , vol.166 , pp. 321-326
    • Van Ginkel, C.G.1    Rikken, G.B.2    Kroon, A.G.3    Kengen, S.W.4
  • 6
    • 84883390764 scopus 로고    scopus 로고
    • Structure and evolution of chlorate reduction composite transposons
    • Clark IC, Melnyk RA, Engelbrektson A, Coates JD. 2013. Structure and evolution of chlorate reduction composite transposons. mBio 4(4): e00379-13. http://dx.doi.org/10.1128/mBio.00379-13.
    • (2013) mBio , vol.4 , Issue.4 , pp. e00379-e00413
    • Clark, I.C.1    Melnyk, R.A.2    Engelbrektson, A.3    Coates, J.D.4
  • 8
    • 0034781061 scopus 로고    scopus 로고
    • Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds
    • Pattison DI, Davies MJ. 2001. Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds. Chem Res Toxicol 14:1453-1464. http://dx.doi.org/10.1021/tx0155451.
    • (2001) Chem Res Toxicol , vol.14 , pp. 1453-1464
    • Pattison, D.I.1    Davies, M.J.2
  • 9
    • 33845960288 scopus 로고    scopus 로고
    • Comparative oxidation studies of methionine residues reflect a structural effect on chemical kinetics in rhG-CSF
    • Pan B, Abel J, Ricci MS, Brems DN, Wang DI, Trout BL. 2006. Comparative oxidation studies of methionine residues reflect a structural effect on chemical kinetics in rhG-CSF. Biochemistry 45:15430-15443. http://dx.doi.org/10.1021/bi061855c.
    • (2006) Biochemistry , vol.45 , pp. 15430-15443
    • Pan, B.1    Abel, J.2    Ricci, M.S.3    Brems, D.N.4    Wang, D.I.5    Trout, B.L.6
  • 10
    • 73249129955 scopus 로고    scopus 로고
    • Methionine oxidation contributes to bacterial killing by the myeloperoxidase system of neutrophils
    • Rosen H, Klebanoff SJ, Wang Y, Brot N, Heinecke JW, Fu X. 2009. Methionine oxidation contributes to bacterial killing by the myeloperoxidase system of neutrophils. Proc Natl Acad Sci U S A 106:18686-18691. http://dx.doi.org/10.1073/pnas.0909464106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 18686-18691
    • Rosen, H.1    Klebanoff, S.J.2    Wang, Y.3    Brot, N.4    Heinecke, J.W.5    Fu, X.6
  • 11
    • 84878675814 scopus 로고    scopus 로고
    • Methionine oxidation activates a transcription factor in response to oxidative stress
    • Drazic A, Miura H, Peschek J, Le Y, Bach NC, Kriehuber T, Winter J. 2013. Methionine oxidation activates a transcription factor in response to oxidative stress. Proc Natl Acad Sci U S A 110:9493-9498. http:// dx.doi.org/10.1073/pnas.1300578110.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 9493-9498
    • Drazic, A.1    Miura, H.2    Peschek, J.3    Le, Y.4    Bach, N.C.5    Kriehuber, T.6    Winter, J.7
  • 13
    • 84887458268 scopus 로고    scopus 로고
    • The RclR protein is a reactive chlorine-specific transcription factor in Escherichia coli
    • Parker BW, Schwessinger EA, Jakob U, Gray MJ. 2013. The RclR protein is a reactive chlorine-specific transcription factor in Escherichia coli. J Biol Chem 288:32574-32584. http://dx.doi.org/10.1074/jbc.M113.503516.
    • (2013) J Biol Chem , vol.288 , pp. 32574-32584
    • Parker, B.W.1    Schwessinger, E.A.2    Jakob, U.3    Gray, M.J.4
  • 14
    • 84903363935 scopus 로고    scopus 로고
    • Transposon and deletion mutagenesis of genes involved in perchlorate reduction in Azospira suillum PS
    • Melnyk RA, Clark IC, Liao A, Coates JD. 2013. Transposon and deletion mutagenesis of genes involved in perchlorate reduction in Azospira suillum PS. mBio 5(1):e00769-13. http://dx.doi.org/10.1128/mBio.00769-13.
    • (2013) mBio , vol.5 , Issue.1 , pp. e00769-e00813
    • Melnyk, R.A.1    Clark, I.C.2    Liao, A.3    Coates, J.D.4
  • 15
  • 16
    • 33644784103 scopus 로고    scopus 로고
    • A Caulobacter crescentus extracytoplasmic function sigma factor mediating the response to oxidative stress in stationary phase
    • Alvarez-Martinez CE, Baldini RL, Gomes SL. 2006. A Caulobacter crescentus extracytoplasmic function sigma factor mediating the response to oxidative stress in stationary phase. J Bacteriol 188:1835-1846. http:// dx.doi.org/10.1128/JB.188.5.1835-1846.2006.
    • (2006) J Bacteriol , vol.188 , pp. 1835-1846
    • Alvarez-Martinez, C.E.1    Baldini, R.L.2    Gomes, S.L.3
  • 18
    • 84866299413 scopus 로고    scopus 로고
    • Extracytoplasmic function (ECF) sigma factor σF is involved in Caulobacter crescentus response to heavy metal stress
    • Kohler C, Lourenço RF, Avelar GM, Gomes SL. 2012. Extracytoplasmic function (ECF) sigma factor σF is involved in Caulobacter crescentus response to heavy metal stress. BMC Microbiol 12:210. http://dx.doi.org/ 10.1186/1471-2180-12-210.
    • (2012) BMC Microbiol , vol.12 , pp. 210
    • Kohler, C.1    Lourenço, R.F.2    Avelar, G.M.3    Gomes, S.L.4
  • 19
    • 70350432754 scopus 로고    scopus 로고
    • The third pillar of bacterial signal transduction: Classification of the extracytoplasmic function (ECF) sigma factor protein family
    • Staroń A, Sofia HJ, Dietrich S, Ulrich LE, Liesegang H, Mascher T. 2009. The third pillar of bacterial signal transduction: classification of the extracytoplasmic function (ECF) sigma factor protein family. Mol Microbiol 74:557-581. http://dx.doi.org/10.1111/j.1365-2958.2009.06870.x.
    • (2009) Mol Microbiol , vol.74 , pp. 557-581
    • Staroń, A.1    Sofia, H.J.2    Dietrich, S.3    Ulrich, L.E.4    Liesegang, H.5    Mascher, T.6
  • 23
    • 0032441150 scopus 로고    scopus 로고
    • Cluster analysis and display of genome-wide expression patterns
    • Eisen MB, Spellman PT, Po Brown PO, Botstein D. 1998. Cluster analysis and display of genome-wide expression patterns. Proc Natl Acad Sci U S A 95:14863-14868. http://dx.doi.org/10.1073/pnas.95.25.14863.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 14863-14868
    • Eisen, M.B.1    Spellman, P.T.2    Po Brown, P.O.3    Botstein, D.4
  • 25
    • 45749103200 scopus 로고    scopus 로고
    • Analysis of methionine/ selenomethionine oxidation and methionine sulfoxide reductase function using methionine-rich proteins and antibodies against their oxidized forms
    • Le DT, Liang X, Fomenko DE, Raza AS, Chong CK, Carlson BA, Hatfield DL, Gladyshev VN. 2008. Analysis of methionine/ selenomethionine oxidation and methionine sulfoxide reductase function using methionine-rich proteins and antibodies against their oxidized forms. Biochemistry 47:6685-6694. http://dx.doi.org/10.1021/bi800422s.
    • (2008) Biochemistry , vol.47 , pp. 6685-6694
    • Le, D.T.1    Liang, X.2    Fomenko, D.E.3    Raza, A.S.4    Chong, C.K.5    Carlson, B.A.6    Hatfield, D.L.7    Gladyshev, V.N.8
  • 26
    • 0021711731 scopus 로고
    • Simple, rapid, and quantitative release of periplasmic proteins by chloroform
    • Ames GF, Prody C, Kustu S. 1984. Simple, rapid, and quantitative release of periplasmic proteins by chloroform. J Bacteriol 160:1181-1183.
    • (1984) J Bacteriol , vol.160 , pp. 1181-1183
    • Ames, G.F.1    Prody, C.2    Kustu, S.3
  • 27
    • 0344410068 scopus 로고    scopus 로고
    • Hypochlorite-induced oxidation of amino acids, peptides and proteins
    • Hawkins CL, Pattison DI, Davies MJ. 2003. Hypochlorite-induced oxidation of amino acids, peptides and proteins. Amino Acids 25:259-274. http://dx.doi.org/10.1007/s00726-003-0016-x.
    • (2003) Amino Acids , vol.25 , pp. 259-274
    • Hawkins, C.L.1    Pattison, D.I.2    Davies, M.J.3
  • 28
    • 0030449173 scopus 로고    scopus 로고
    • Methionine residues as endogenous antioxidants in proteins
    • Levine RL, Mosoni L, Berlett BS, Stadtman ER. 1996. Methionine residues as endogenous antioxidants in proteins. Proc Natl Acad Sci U S A 93:15036-15040. http://dx.doi.org/10.1073/pnas.93.26.15036.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 15036-15040
    • Levine, R.L.1    Mosoni, L.2    Berlett, B.S.3    Stadtman, E.R.4
  • 29
    • 12844259524 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases in prokaryotes
    • Ezraty B, Aussel L, Barras F. 2005. Methionine sulfoxide reductases in prokaryotes. Biochim Biophys Acta 1703:221-229. http://dx.doi.org/ 10.1016/j.bbapap.2004.08.017.
    • (2005) Biochim Biophys Acta , vol.1703 , pp. 221-229
    • Ezraty, B.1    Aussel, L.2    Barras, F.3
  • 30
    • 84863797987 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases preferentially reduce unfolded oxidized proteins and protect cells from oxidative protein unfolding
    • Tarrago L, Kaya A, Weerapana E, Marino SM, Gladyshev VN. 2012. Methionine sulfoxide reductases preferentially reduce unfolded oxidized proteins and protect cells from oxidative protein unfolding. J Biol Chem 287:24448-24459. http://dx.doi.org/10.1074/jbc.M112.374520.
    • (2012) J Biol Chem , vol.287 , pp. 24448-24459
    • Tarrago, L.1    Kaya, A.2    Weerapana, E.3    Marino, S.M.4    Gladyshev, V.N.5
  • 32
    • 84858437093 scopus 로고    scopus 로고
    • The STF2p hydrophilin from Saccharomyces cerevisiae is required for dehydration stress tolerance
    • López-Martínez G, Rodríguez-Porrata B, Margalef-Català M, Cordero-Otero R. 2012. The STF2p hydrophilin from Saccharomyces cerevisiae is required for dehydration stress tolerance. PLoS One 7:e33324. http:// dx.doi.org/10.1371/journal.pone.0033324.
    • (2012) PLoS One , vol.7
    • López-Martínez, G.1    Rodríguez-Porrata, B.2    Margalef-Català, M.3    Cordero-Otero, R.4
  • 34
    • 23044485986 scopus 로고    scopus 로고
    • Characterization of an Escherichia coli sulfite oxidase homologue reveals the role of a conserved active site cysteine in assembly and function
    • Brokx SJ, Rothery RA, Zhang G, Ng DP, Weiner JH. 2005. Characterization of an Escherichia coli sulfite oxidase homologue reveals the role of a conserved active site cysteine in assembly and function. Biochemistry 44:10339-10348. http://dx.doi.org/10.1021/bi050621a.
    • (2005) Biochemistry , vol.44 , pp. 10339-10348
    • Brokx, S.J.1    Rothery, R.A.2    Zhang, G.3    Ng, D.P.4    Weiner, J.H.5
  • 36
    • 84907962014 scopus 로고    scopus 로고
    • Chlorate reduction in Shewanella algae ACDC is a recently acquired metabolism characterized by gene loss, suboptimal regulation and oxidative stress
    • Clark IC, Melnyk RA, Iavarone AT, Novichkov PS, Coates JD. 2014. Chlorate reduction in Shewanella algae ACDC is a recently acquired metabolism characterized by gene loss, suboptimal regulation and oxidative stress. Mol Microbiol 94:107-125. http://dx.doi.org/10.1111/mmi.12746.
    • (2014) Mol Microbiol , vol.94 , pp. 107-125
    • Clark, I.C.1    Melnyk, R.A.2    Iavarone, A.T.3    Novichkov, P.S.4    Coates, J.D.5
  • 38
    • 70350588981 scopus 로고    scopus 로고
    • Survival of the fittest: How Brucella strains adapt to their intracellular niche in the host
    • Roop RM, Gaines JM, Anderson ES, Caswell CC, Martin DW. 2009. Survival of the fittest: how Brucella strains adapt to their intracellular niche in the host. Med Microbiol Immunol 198:221-238. http://dx.doi.org/ 10.1007/s00430-009-0123-8.
    • (2009) Med Microbiol Immunol , vol.198 , pp. 221-238
    • Roop, R.M.1    Gaines, J.M.2    Anderson, E.S.3    Caswell, C.C.4    Martin, D.W.5
  • 39
    • 77958471357 scopus 로고    scopus 로고
    • Differential expression analysis for sequence count data
    • Anders S, Huber W. 2010. Differential expression analysis for sequence count data. Genome Biol 11:R106. http://dx.doi.org/10.1186/gb-2010-11-10-r106.
    • (2010) Genome Biol , vol.11
    • Anders, S.1    Huber, W.2
  • 40
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • PfafflMW. 2001. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29:e45. http://dx.doi.org/10.1093/ nar/29.9.e45.
    • (2001) Nucleic Acids Res , vol.29
    • Pfaffl, M.W.1
  • 41
    • 81755163097 scopus 로고    scopus 로고
    • Evidence-based annotation of gene function in Shewanella oneidensis MR-1 using genomewide fitness profiling across 121 conditions
    • Deutschbauer A, Price MN, Wetmore KM, Shao W, Baumohl JK, Xu Z, Nguyen M, Tamse R, Davis RW, Arkin AP. 2011. Evidence-based annotation of gene function in Shewanella oneidensis MR-1 using genomewide fitness profiling across 121 conditions. PLoS Genet 7:e1002385. http://dx.doi.org/10.1371/journal.pgen.1002385.
    • (2011) PLoS Genet , vol.7
    • Deutschbauer, A.1    Price, M.N.2    Wetmore, K.M.3    Shao, W.4    Baumohl, J.K.5    Xu, Z.6    Nguyen, M.7    Tamse, R.8    Davis, R.W.9    Arkin, A.P.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.