메뉴 건너뛰기




Volumn 362, Issue 2, 2015, Pages

The role of Cercospora zeae-maydis homologs of Rhodobacter sphaeroides 1O2-resistance genes in resistance to the photoactivated toxin cercosporin

Author keywords

Aldehyde dehydrogenase; Aldo Keto reductase; Cercospora; Cercosporin; Glutathione S transferase; O acetylhomoserine (thiol) lyase; Peptide methionine sulphoxide reductase; Rhodobacter; Singlet oxygen; Succinyl CoA ligase

Indexed keywords

ALDEHYDE DEHYDROGENASE; ALDO REDUCTASE; CERCOSPORIN; GLUTATHIONE TRANSFERASE; KETO REDUCTASE; LYASE; MYCOTOXIN; O ACETYLHOMOSERINE LYASE; OXIDOREDUCTASE; PEPTIDE METHIONINE SULPHOXIDE REDUCTASE; SINGLET OXYGEN; SUCCINYL COENZYME A SYNTHETASE; TRANSCRIPTOME; UNCLASSIFIED DRUG; OXIDIZING AGENT; PERYLENE;

EID: 84944511718     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1093/femsle/fnu036     Document Type: Article
Times cited : (6)

References (19)
  • 1
    • 58749096683 scopus 로고    scopus 로고
    • The ABC transporter ATR1 is necessary for efflux of the toxin cercosporin in the fungus Cercospora nicotianae
    • Amnuaykanjanasin A, Daub ME. The ABC transporter ATR1 is necessary for efflux of the toxin cercosporin in the fungus Cercospora nicotianae. Fungal Genet Biol 2009;46: 146-58
    • (2009) Fungal Genet Biol , vol.46 , pp. 146-158
    • Amnuaykanjanasin, A.1    Daub, M.E.2
  • 2
    • 79958786333 scopus 로고    scopus 로고
    • Contribution of Hfq to photooxidative stress resistance and global regulation in Rhodobacter sphaeroides
    • BerghoffBA, Glaeser J, Sharma CM, et al. Contribution of Hfq to photooxidative stress resistance and global regulation in Rhodobacter sphaeroides. Mol Microbiol 2011;80:1479-95
    • (2011) Mol Microbiol , vol.80 , pp. 1479-1495
    • Berghoff, B.A.1    Glaeser, J.2    Sharma, C.M.3
  • 3
    • 0037428263 scopus 로고    scopus 로고
    • The CRG1 gene required for resistance to the singlet oxygen-generating cercosporin toxin in Cercospora nicotianae encodes a putative fungal transcription factor
    • Chung KR, Daub ME, Kuchler K, et al. The CRG1 gene required for resistance to the singlet oxygen-generating cercosporin toxin in Cercospora nicotianae encodes a putative fungal transcription factor. Biochem Bioph Res Co 2003;302:302-10
    • (2003) Biochem Bioph Res Co , vol.302 , pp. 302-310
    • Chung, K.R.1    Daub, M.E.2    Kuchler, K.3
  • 4
    • 84883402394 scopus 로고    scopus 로고
    • Reactive oxygen species in plant pathogenesis: the role of perylenequinone photosensitizers
    • Daub ME, Herrero S, Chung KR. Reactive oxygen species in plant pathogenesis: the role of perylenequinone photosensitizers. Antioxid Redox Sign 2013;19:970-89
    • (2013) Antioxid Redox Sign , vol.19 , pp. 970-989
    • Daub, M.E.1    Herrero, S.2    Chung, K.R.3
  • 5
    • 0026646095 scopus 로고
    • Reductive detoxification as a mechanism of fungal resistance to singlet oxygen-generating photosensitizers
    • Daub ME, Leisman GB, Clark RA, et al. Reductive detoxification as a mechanism of fungal resistance to singlet oxygen-generating photosensitizers. P Natl Acad Sci-Biol 1992;89:9588-92
    • (1992) P Natl Acad Sci-Biol , vol.89 , pp. 9588-9592
    • Daub, M.E.1    Leisman, G.B.2    Clark, R.A.3
  • 7
    • 36749010860 scopus 로고    scopus 로고
    • Biochemistry of oxidative stress.
    • Halliwell B. Biochemistry of oxidative stress. Biochem Soc T 2007;35:1147-50
    • (2007) Biochem Soc T , vol.35 , pp. 1147-1150
    • Halliwell, B.1
  • 8
    • 34548764378 scopus 로고    scopus 로고
    • Identification of genes differentially expressed in the phytopathogenic fungus Cercospora nicotianae between cercosporin toxin-resistant and -susceptible strains
    • Herrero S, Amnuaykanjanasin A, Daub ME. Identification of genes differentially expressed in the phytopathogenic fungus Cercospora nicotianae between cercosporin toxin-resistant and -susceptible strains. FEMS Microbiol Lett 2007;275: 326-37
    • (2007) FEMS Microbiol Lett , vol.275 , pp. 326-337
    • Herrero, S.1    Amnuaykanjanasin, A.2    Daub, M.E.3
  • 9
    • 33846227552 scopus 로고    scopus 로고
    • Genetic manipulation of vitamin B-6 biosynthesis in tobacco and fungi uncovers limitations to upregulation of the pathway
    • Herrero S, Daub ME. Genetic manipulation of vitamin B-6 biosynthesis in tobacco and fungi uncovers limitations to upregulation of the pathway. Plant Sci 2007;172:609-20
    • (2007) Plant Sci , vol.172 , pp. 609-620
    • Herrero, S.1    Daub, M.E.2
  • 10
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak KJ, Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 2001;25:402-2
    • (2001) Methods , vol.25 , pp. 402-402
    • Livak, K.J.1    Schmittgen, T.D.2
  • 11
    • 58149503635 scopus 로고    scopus 로고
    • RpoH(II) activates oxidative-stress defense systems and is controlled by RpoE in the singlet oxygen-dependent response in Rhodobacter sphaeroides
    • Nuss AM, Glaeser J, Klug G. RpoH(II) activates oxidative-stress defense systems and is controlled by RpoE in the singlet oxygen-dependent response in Rhodobacter sphaeroides. J Bacteriol 2009;191:220-30
    • (2009) J Bacteriol , vol.191 , pp. 220-230
    • Nuss, A.M.1    Glaeser, J.2    Klug, G.3
  • 12
    • 0034668118 scopus 로고    scopus 로고
    • Quantitative reverse transcription-polymerase chain reaction to study mRNA decay: comparison of endpoint and Real-Time methods
    • Schmittgen TD, Zakrajsek BA, Mills AG, et al. Quantitative reverse transcription-polymerase chain reaction to study mRNA decay: comparison of endpoint and Real-Time methods. Anal Biochem 2000;285:194-4
    • (2000) Anal Biochem , vol.285 , pp. 194-194
    • Schmittgen, T.D.1    Zakrajsek, B.A.2    Mills, A.G.3
  • 13
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily
    • Sheehan D, Meade G, Foley VM, et al. Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem J 2001;360:1-16
    • (2001) Biochem J , vol.360 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3
  • 14
    • 0001963674 scopus 로고
    • A convenient growth medium for Neurospora (medium N)
    • Vogel HJ. A convenient growth medium for Neurospora (medium N). Microbial Genet Bull 1956;13:42-3
    • (1956) Microbial Genet Bull , vol.13 , pp. 42-43
    • Vogel, H.J.1
  • 15
    • 0022542294 scopus 로고
    • Efficient cloning of genes of Neurospora crassa
    • Vollmer SJ, Yanofsky C. Efficient cloning of genes of Neurospora crassa. P Natl Acad Sci-Biol 1986;83:4869-73
    • (1986) P Natl Acad Sci-Biol , vol.83 , pp. 4869-4873
    • Vollmer, S.J.1    Yanofsky, C.2
  • 16
    • 0027182485 scopus 로고
    • A simple method of preparing plant samples for PCR
    • Wang H, Meiqing Q, Cutler AJ. A simple method of preparing plant samples for PCR. Nucleic Acids Res 1993;21: 4153-4
    • (1993) Nucleic Acids Res , vol.21 , pp. 4153-4154
    • Wang, H.1    Meiqing, Q.2    Cutler, A.J.3
  • 17
    • 0037082129 scopus 로고    scopus 로고
    • Peptide methionine sulfoxide reductase: structure, mechanism of action, and biological function
    • Weissbach H, Etienne F, Hoshi T, et al. Peptide methionine sulfoxide reductase: structure, mechanism of action, and biological function. Arch Biochem Biophys 2002;397:172-8
    • (2002) Arch Biochem Biophys , vol.397 , pp. 172-178
    • Weissbach, H.1    Etienne, F.2    Hoshi, T.3
  • 18
    • 0033562350 scopus 로고    scopus 로고
    • Development and validation of real-time quantitative reverse transcriptase-polymerase chain reaction for monitoring gene expression in cardiac myocytes in vitro
    • Winer J. Development and validation of real-time quantitative reverse transcriptase-polymerase chain reaction for monitoring gene expression in cardiac myocytes in vitro. Anal Biochem 1999;270:41-9
    • (1999) Anal Biochem , vol.270 , pp. 41-49
    • Winer, J.1
  • 19
    • 0024847671 scopus 로고
    • Roles of O-acetyl-L-homoserine sulfhydrylases in micro-organisms
    • Yamagata S. Roles of O-acetyl-L-homoserine sulfhydrylases in micro-organisms. Biochimie 1989;71:1125-43.
    • (1989) Biochimie , vol.71 , pp. 1125-1143
    • Yamagata, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.