메뉴 건너뛰기




Volumn 273, Issue 2, 2007, Pages 244-252

E1 component of pyruvate dehydrogenase complex does not regulate the expression of NADPH-ferredoxin reductase in Azotobacter vinelandii

Author keywords

E1 of pyruvate dehydrogenase complex; Ferredoxin I; NADPH ferredoxin reductase; Oxidative stress; Paraquat

Indexed keywords

FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; MUTANT PROTEIN; PARAQUAT; PYRUVATE DEHYDROGENASE COMPLEX; PYRUVATE DEHYDROGENASE COMPLEX E1; REGULATOR PROTEIN; SUPEROXIDE; UNCLASSIFIED DRUG;

EID: 34447558703     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2007.00797.x     Document Type: Article
Times cited : (7)

References (32)
  • 2
    • 0019805971 scopus 로고
    • Specific-purpose plasmid cloning vectors. II. Broad host range, high copy number, RSF1010-derived vectors, and a host-vector system for gene cloning in Pseudomonas
    • Bagdasarian M, Lurz R, Ruckert B, Franklin FC, Bagdasarian MM, Frey J Timmis KN (1981) Specific-purpose plasmid cloning vectors. II. Broad host range, high copy number, RSF1010-derived vectors, and a host-vector system for gene cloning in Pseudomonas. Gene 16 : 237 247.
    • (1981) Gene , vol.16 , pp. 237-247
    • Bagdasarian, M.1    Lurz, R.2    Ruckert, B.3    Franklin, F.C.4    Bagdasarian, M.M.5    Frey, J.6    Timmis, K.N.7
  • 5
    • 7644223774 scopus 로고    scopus 로고
    • Why is transcription coupled to translation in bacteria?
    • Gowrishankar J Harinarayanan R (2004) Why is transcription coupled to translation in bacteria? Mol Microbiol 54 : 598 603.
    • (2004) Mol Microbiol , vol.54 , pp. 598-603
    • Gowrishankar, J.1    Harinarayanan, R.2
  • 6
    • 0025078495 scopus 로고
    • Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli
    • Greenberg JT, Monach P, Chou JH, Josephy PD Demple B (1990) Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. Proc Natl Acad Sci USA 87 : 6181 6185.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6181-6185
    • Greenberg, J.T.1    Monach, P.2    Chou, J.H.3    Josephy, P.D.4    Demple, B.5
  • 7
    • 0018604132 scopus 로고
    • Paraquat and Escherichia coli. Mechanism of production of extracellular superoxide radical
    • Hassan HM Fridovich I (1979) Paraquat and Escherichia coli. Mechanism of production of extracellular superoxide radical. J Biol Chem 254 : 10846 10852.
    • (1979) J Biol Chem , vol.254 , pp. 10846-10852
    • Hassan, H.M.1    Fridovich, I.2
  • 8
    • 0029154763 scopus 로고
    • Azotobacter vinelandii NADPH-ferredoxin reductase: Cloning, sequencing, and overexpression
    • Isas JM, Yannone SM Burgess BK (1995) Azotobacter vinelandii NADPH-ferredoxin reductase: cloning, sequencing, and overexpression. J Biol Chem 270 : 21258 21263.
    • (1995) J Biol Chem , vol.270 , pp. 21258-21263
    • Isas, J.M.1    Yannone, S.M.2    Burgess, B.K.3
  • 9
    • 0033527754 scopus 로고    scopus 로고
    • Purification and biophysical characterization of a new [2Fe-2S] ferredoxin from Azotobacter vinelandii, a putative [Fe-S] cluster assembly/repair protein
    • Jung YS, Gao-Sheridan HS, Christiansen J, Dean DR Burgess BK (1999a) Purification and biophysical characterization of a new [2Fe-2S] ferredoxin from Azotobacter vinelandii, a putative [Fe-S] cluster assembly/repair protein. J Biol Chem 274 : 32402 32410.
    • (1999) J Biol Chem , vol.274 , pp. 32402-32410
    • Jung, Y.S.1    Gao-Sheridan, H.S.2    Christiansen, J.3    Dean, D.R.4    Burgess, B.K.5
  • 10
    • 0033614010 scopus 로고    scopus 로고
    • Complex formation between Azotobacter vinelandii ferredoxin I and its physiological electron donor NADPH-ferredoxin reductase
    • Jung YS, Roberts VA, Stout CD Burgess BK (1999b) Complex formation between Azotobacter vinelandii ferredoxin I and its physiological electron donor NADPH-ferredoxin reductase. J Biol Chem 274 : 2978 2987.
    • (1999) J Biol Chem , vol.274 , pp. 2978-2987
    • Jung, Y.S.1    Roberts, V.A.2    Stout, C.D.3    Burgess, B.K.4
  • 11
    • 0001759947 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli Rob transcription factor in complex with DNA
    • Kwon HJ, Bennik MH, Demple B Ellenberger T (2000) Crystal structure of the Escherichia coli Rob transcription factor in complex with DNA. Nat Struct Biol 7 : 424 430.
    • (2000) Nat Struct Biol , vol.7 , pp. 424-430
    • Kwon, H.J.1    Bennik, M.H.2    Demple, B.3    Ellenberger, T.4
  • 13
    • 0031038988 scopus 로고    scopus 로고
    • Identification of a penicillin-binding protein 3 homolog, PBP3x, in Pseudomonas aeruginosa: Gene cloning and growth phase-dependent expression
    • Liao X Hancock RE (1997) Identification of a penicillin-binding protein 3 homolog, PBP3x, in Pseudomonas aeruginosa: gene cloning and growth phase-dependent expression. J Bacteriol 179 : 1490 1496.
    • (1997) J Bacteriol , vol.179 , pp. 1490-1496
    • Liao, X.1    Hancock, R.E.2
  • 14
    • 0023870725 scopus 로고
    • Azotobacter vinelandii ferredoxin I: Cloning, sequencing, and mutant analysis
    • Morgan TV, Lundell DJ Burgess BK (1988) Azotobacter vinelandii ferredoxin I: cloning, sequencing, and mutant analysis. J Biol Chem 263 : 1370 1375.
    • (1988) J Biol Chem , vol.263 , pp. 1370-1375
    • Morgan, T.V.1    Lundell, D.J.2    Burgess, B.K.3
  • 15
    • 0032537554 scopus 로고    scopus 로고
    • Gene and subunit organization of bacterial pyruvate dehydrogenase complexes
    • Neveling U, Bringer-Meyer S Sahm H (1998) Gene and subunit organization of bacterial pyruvate dehydrogenase complexes. Biochim Biophys Acta 1385 : 367 372.
    • (1998) Biochim Biophys Acta , vol.1385 , pp. 367-372
    • Neveling, U.1    Bringer-Meyer, S.2    Sahm, H.3
  • 16
    • 0037771389 scopus 로고    scopus 로고
    • Are mitochondria a spontaneous and permanent source of reactive oxygen species?
    • Nohl H, Gille L, Kozlov A Staniek K (2003) Are mitochondria a spontaneous and permanent source of reactive oxygen species? Redox Rep 8 : 135 141.
    • (2003) Redox Rep , vol.8 , pp. 135-141
    • Nohl, H.1    Gille, L.2    Kozlov, A.3    Staniek, K.4
  • 17
    • 0033020793 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa fur overlaps with a gene encoding a novel outer membrane lipoprotein, OmlA
    • Ochsner UA, Vasil AI, Johnson Z Vasil ML (1999) Pseudomonas aeruginosa fur overlaps with a gene encoding a novel outer membrane lipoprotein, OmlA. J Bacteriol 181 : 1099 1109.
    • (1999) J Bacteriol , vol.181 , pp. 1099-1109
    • Ochsner, U.A.1    Vasil, A.I.2    Johnson, Z.3    Vasil, M.L.4
  • 18
    • 17644408447 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa SoxR does not conform to the archetypal paradigm for SoxR-dependent regulation of the bacterial oxidative stress adaptive response
    • Palma M, Zurita J, Ferreras JA, Worgall S, Larone DH, Shi L, Campagne F Quadri LE (2005) Pseudomonas aeruginosa SoxR does not conform to the archetypal paradigm for SoxR-dependent regulation of the bacterial oxidative stress adaptive response. Infect Immun 73 : 2958 2966.
    • (2005) Infect Immun , vol.73 , pp. 2958-2966
    • Palma, M.1    Zurita, J.2    Ferreras, J.A.3    Worgall, S.4    Larone, D.H.5    Shi, L.6    Campagne, F.7    Quadri, L.E.8
  • 19
    • 30944437009 scopus 로고    scopus 로고
    • Regulation of superoxide stress in Pseudomonas putida KT2440 is different from the SoxR paradigm in Escherichia coli
    • Park W, Pena-Llopis S, Lee Y Demple B (2006) Regulation of superoxide stress in Pseudomonas putida KT2440 is different from the SoxR paradigm in Escherichia coli. Biochem Biophys Res Commun 341 : 51 56.
    • (2006) Biochem Biophys Res Commun , vol.341 , pp. 51-56
    • Park, W.1    Pena-Llopis, S.2    Lee, Y.3    Demple, B.4
  • 20
    • 0035283587 scopus 로고    scopus 로고
    • Redox-operated genetic switches: The SoxR and OxyR transcription factors
    • Pomposiello PJ Demple B (2001) Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol 19 : 109 114.
    • (2001) Trends Biotechnol , vol.19 , pp. 109-114
    • Pomposiello, P.J.1    Demple, B.2
  • 21
    • 2942618508 scopus 로고    scopus 로고
    • Azotobacter vinelandii: A Pseudomonas in disguise?
    • Rediers H, Vanderleyden J De Mot R (2004) Azotobacter vinelandii: a Pseudomonas in disguise? Microbiology 150 : 1117 1119.
    • (2004) Microbiology , vol.150 , pp. 1117-1119
    • Rediers, H.1    Vanderleyden, J.2    De Mot, R.3
  • 22
    • 0033607180 scopus 로고    scopus 로고
    • In Azotobacter vinelandii, the E1 subunit of the pyruvate dehydrogenase complex binds fpr promoter region DNA and ferredoxin I
    • Regnstrom K, Sauge-Merle S, Chen K Burgess BK (1999) In Azotobacter vinelandii, the E1 subunit of the pyruvate dehydrogenase complex binds fpr promoter region DNA and ferredoxin I. Proc Natl Acad Sci USA 96 : 12389 12393.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 12389-12393
    • Regnstrom, K.1    Sauge-Merle, S.2    Chen, K.3    Burgess, B.K.4
  • 23
    • 0032169864 scopus 로고    scopus 로고
    • A novel DNA-binding motif in MarA: The first structure for an AraC family transcriptional activator
    • Rhee S, Martin RG, Rosner JL Davies DR (1998) A novel DNA-binding motif in MarA: the first structure for an AraC family transcriptional activator. Proc Natl Acad Sci USA 95 : 10413 10418.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10413-10418
    • Rhee, S.1    Martin, R.G.2    Rosner, J.L.3    Davies, D.R.4
  • 24
    • 0035464767 scopus 로고    scopus 로고
    • Laboratory evolution of toluene dioxygenase to accept 4-picoline as a substrate
    • Sakamoto T, Joern JM, Arisawa A Arnold FH (2001) Laboratory evolution of toluene dioxygenase to accept 4-picoline as a substrate. Appl Environ Microbiol 67 : 3882 3897.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 3882-3897
    • Sakamoto, T.1    Joern, J.M.2    Arisawa, A.3    Arnold, F.H.4
  • 25
    • 0032496372 scopus 로고    scopus 로고
    • Structure of Azotobacter vinelandii 7Fe ferredoxin at 1.35 Å resolution and determination of the [Fe-S] bonds with 0.01 Å accuracy
    • Stout CD, Stura EA McRee DE (1998) Structure of Azotobacter vinelandii 7Fe ferredoxin at 1.35 Å resolution and determination of the [Fe-S] bonds with 0.01 Å accuracy. J Biol Chem 278 : 629 639.
    • (1998) J Biol Chem , vol.278 , pp. 629-639
    • Stout, C.D.1    Stura, E.A.2    McRee, D.E.3
  • 26
    • 0025847944 scopus 로고
    • Does ferredoxin I (Azotobacter) represent a novel class of DNA-binding proteins that regulate gene expression in response to cellular iron (II)?
    • Thomson AJ (1991) Does ferredoxin I (Azotobacter) represent a novel class of DNA-binding proteins that regulate gene expression in response to cellular iron (II)? FEBS Lett 285 : 230 236.
    • (1991) FEBS Lett , vol.285 , pp. 230-236
    • Thomson, A.J.1
  • 27
    • 0033926141 scopus 로고    scopus 로고
    • Dual regulation of catecholate siderophore biosynthesis in Azotobacter vinelandii by iron and oxidative stress
    • Tindale AE, Mehrotra M, Ottem D Page WJ (2000) Dual regulation of catecholate siderophore biosynthesis in Azotobacter vinelandii by iron and oxidative stress. Microbiology 146 : 1617 1626.
    • (2000) Microbiology , vol.146 , pp. 1617-1626
    • Tindale, A.E.1    Mehrotra, M.2    Ottem, D.3    Page, W.J.4
  • 28
    • 0033673079 scopus 로고    scopus 로고
    • Sensing and protecting against superoxide stress in Escherichia coli-how many ways are there to trigger soxRS response?
    • Touati D (2000) Sensing and protecting against superoxide stress in Escherichia coli-how many ways are there to trigger soxRS response? Redox Rep 5 : 287 293.
    • (2000) Redox Rep , vol.5 , pp. 287-293
    • Touati, D.1
  • 29
    • 0002434812 scopus 로고
    • The Escherichia coli gus operon: Induction and expression of the gus operon in E. coli and the occurence and use of GUS in other bacteria
    • Gallagher, S.R., ed), pp. Academic Press, San Diego.
    • Wilson KJ, Hughes SG Jefferson RA (1992) The Escherichia coli gus operon: induction and expression of the gus operon in E. coli and the occurence and use of GUS in other bacteria. GUS Protocols: Using the GUS Gene as a Reporter of Gene Expression (Gallagher SR, ed), pp. 7 22. Academic Press, San Diego.
    • (1992) GUS Protocols: Using the GUS Gene As a Reporter of Gene Expression , pp. 7-22
    • Wilson, K.J.1    Hughes, S.G.2    Jefferson, R.A.3
  • 30
    • 0030998916 scopus 로고    scopus 로고
    • Identification of a palindromic sequence that is responsible for the up-regulation of NAPDH-ferredoxin reductase in a ferredoxin I deletion strain of Azotobacter vinelandii
    • Yannone SM Burgess BK (1997) Identification of a palindromic sequence that is responsible for the up-regulation of NAPDH-ferredoxin reductase in a ferredoxin I deletion strain of Azotobacter vinelandii. J Biol Chem 272 : 14454 14458.
    • (1997) J Biol Chem , vol.272 , pp. 14454-14458
    • Yannone, S.M.1    Burgess, B.K.2
  • 31
    • 0031807149 scopus 로고    scopus 로고
    • The seven-iron FdI from Azotobacter vinelandii regulates the expression of NADPH: Ferredoxin reductase via an oxidative stress response
    • Yannone SM Burgess BK (1998) The seven-iron FdI from Azotobacter vinelandii regulates the expression of NADPH: ferredoxin reductase via an oxidative stress response. J Biol Inorg Chem 3 : 253 258.
    • (1998) J Biol Inorg Chem , vol.3 , pp. 253-258
    • Yannone, S.M.1    Burgess, B.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.