메뉴 건너뛰기




Volumn 178, Issue 5, 2002, Pages 358-369

A novel haem compound accumulated in Escherichia coli overexpressing the cydDC operon, encoding an ABC-type transporter required for cytochrome assembly

Author keywords

ABC type transporter; Cytochrome bd; Escherichia coli; Haemprotein; Oxidase

Indexed keywords

ABC TRANSPORTER; CARBON MONOXIDE; CYANIDE; CYTOCHROME B; CYTOCHROME D; HEME DERIVATIVE;

EID: 0036400868     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-002-0467-6     Document Type: Article
Times cited : (16)

References (49)
  • 1
    • 0025219623 scopus 로고
    • Isolation of a Rhodobacter capsulatus mutant that lacks c-type cytochromes and excretes porphyrins
    • Biel SW, Biel AJ (1990) Isolation of a Rhodobacter capsulatus mutant that lacks c-type cytochromes and excretes porphyrins. J Bacteriol 172:1321-1326
    • (1990) J Bacteriol , vol.172 , pp. 1321-1326
    • Biel, S.W.1    Biel, A.J.2
  • 4
    • 0024558335 scopus 로고
    • One-step transformation of competent Escherichia coli: Transformation and storage of bacterial cells in the same solution
    • Chung CT, Niemala SL, Miller RH (1989) One-step transformation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc Natl Acad Sci USA 86:2172-2175
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2172-2175
    • Chung, C.T.1    Niemala, S.L.2    Miller, R.H.3
  • 5
    • 0033968656 scopus 로고    scopus 로고
    • Oxidase and periplasmic cytochrome assembly in Escherichia coli K-12: CydDC and CcmAB are not required for haem-membrane association
    • Cook GM, Poole RK (2000) Oxidase and periplasmic cytochrome assembly in Escherichia coli K-12: CydDC and CcmAB are not required for haem-membrane association. Microbiology 146:527-536
    • (2000) Microbiology , vol.146 , pp. 527-536
    • Cook, G.M.1    Poole, R.K.2
  • 6
    • 0030761574 scopus 로고    scopus 로고
    • Transcriptional regulation of the cydDC operon, encoding a hetero-dimeric ABC transporter required for assembly of cytochromes c and bd in Escherichia coli K12: Regulation by oxygen and alternative electron acceptors
    • Cook GM, Membrillo-Hernández J, Poole RK (1997) Transcriptional regulation of the cydDC operon, encoding a hetero-dimeric ABC transporter required for assembly of cytochromes c and bd in Escherichia coli K12: regulation by oxygen and alternative electron acceptors. J Bacteriol 179:6525-6530
    • (1997) J Bacteriol , vol.179 , pp. 6525-6530
    • Cook, G.M.1    Membrillo-Hernández, J.2    Poole, R.K.3
  • 7
    • 0025129999 scopus 로고
    • Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH, and the fnr gene product
    • Cotter PA, Chepuri V, Gennis RB, Gunsalus RP (1990) Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH, and the fnr gene product. J Bacteriol 172:6333-6338
    • (1990) J Bacteriol , vol.172 , pp. 6333-6338
    • Cotter, P.A.1    Chepuri, V.2    Gennis, R.B.3    Gunsalus, R.P.4
  • 8
    • 0028909392 scopus 로고
    • The oxygen affinity of cytochrome bo' in Escherichia coli determined by the deoxygenation of oxyleghemoglobin and oxymyoglobin; Km values for oxygen are in the submicromolar range
    • D'mello R, Hill S, Poole RK (1995) The oxygen affinity of cytochrome bo' in Escherichia coli determined by the deoxygenation of oxyleghemoglobin and oxymyoglobin; Km values for oxygen are in the submicromolar range. J Bacteriol 177: 867-870
    • (1995) J Bacteriol , vol.177 , pp. 867-870
    • D'mello, R.1    Hill, S.2    Poole, R.K.3
  • 9
    • 0029981912 scopus 로고    scopus 로고
    • The cytochrome bd quinol oxidase in Escherichia coli has an astonishingly high affinity for oxygen and two oxygen-binding haems: Implications for regulation of oxidase activity by substrate (oxygen) inhibition
    • D'mello R, Hill S, Poole RK (1996) The cytochromebd quinol oxidase in Escherichia coli has an astonishingly high affinity for oxygen and two oxygen-binding haems: implications for regulation of oxidase activity by substrate (oxygen) inhibition. Microbiology 142:755-763
    • (1996) Microbiology , vol.142 , pp. 755-763
    • D'mello, R.1    Hill, S.2    Poole, R.K.3
  • 10
    • 0027132575 scopus 로고
    • ABC transporters - Bacterial exporters
    • Fath, MJ, Kolter R (1993) ABC transporters - bacterial exporters. Microbiol Rev 57:995-1017
    • (1993) Microbiol Rev , vol.57 , pp. 995-1017
    • Fath, M.J.1    Kolter, R.2
  • 11
    • 0000598585 scopus 로고    scopus 로고
    • Respiration
    • Niedhardt FC, Cur-tiss R, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (eds). ASM, Washington DC
    • Gennis RB, Stewart V (1996) Respiration. In: Niedhardt FC, Cur-tiss R, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (eds) Escherichia coli and Salmonella: cellular and molecular biology, 2nd edn. ASM, Washington DC, pp 217-261
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Edn. , pp. 217-261
    • Gennis, R.B.1    Stewart, V.2
  • 12
    • 0023276114 scopus 로고
    • Identification of the cydC locus required for expression of the functional form of the cytochrome d terminal oxidase complex in Escherichia coli
    • Georgiou CD, Fang H, Gennis RB (1987) Identification of the cydC locus required for expression of the functional form of the cytochrome d terminal oxidase complex in Escherichia coli. J Bacteriol 169:2107-2112
    • (1987) J Bacteriol , vol.169 , pp. 2107-2112
    • Georgiou, C.D.1    Fang, H.2    Gennis, R.B.3
  • 13
    • 0017615828 scopus 로고
    • o portion of the magnesium ion-stimulated adenosine triphosphatase of Escherichia coli K12. The uncC424 allele
    • o portion of the magnesium ion-stimulated adenosine triphosphatase of Escherichia coli K12. TheuncC424 allele. Biochem J 164:193-198
    • (1977) Biochem J , vol.164 , pp. 193-198
    • Gibson, F.1    Cox, G.B.2    Downie, J.A.3    Radik, J.4
  • 14
    • 0029123812 scopus 로고
    • A simple procedure for gel electrophoresis and northern blotting of RNA
    • Goda SK, Minton NP (1995) A simple procedure for gel electrophoresis and northern blotting of RNA. Nucleic Acid Res 23:3357-3358
    • (1995) Nucleic Acid Res , vol.23 , pp. 3357-3358
    • Goda, S.K.1    Minton, N.P.2
  • 15
    • 0029917388 scopus 로고    scopus 로고
    • The temperature-sensitive growth and survival phenotypes of Escherichia coli cydDC and cydAB strains are due to deficiencies in cytochrome bd and are corrected by exogenous catalase and reducing agents
    • Goldman BS, Gabbert KK, Kranz RG (1996a) The temperature-sensitive growth and survival phenotypes of Escherichia coli cydDC and cydAB strains are due to deficiencies in cytochrome bd and are corrected by exogenous catalase and reducing agents. J Bacteriol 178:6348-6351
    • (1996) J Bacteriol , vol.178 , pp. 6348-6351
    • Goldman, B.S.1    Gabbert, K.K.2    Kranz, R.G.3
  • 16
    • 0029858253 scopus 로고    scopus 로고
    • Use of heme reporters for studies of cytochrome biosynthesis and heme transport
    • Goldman BS, Gabbert KK, Kranz RG (1996b) Use of heme reporters for studies of cytochrome biosynthesis and heme transport. J Bacteriol 178:6338-6347
    • (1996) J Bacteriol , vol.178 , pp. 6338-6347
    • Goldman, B.S.1    Gabbert, K.K.2    Kranz, R.G.3
  • 17
    • 0031574912 scopus 로고    scopus 로고
    • Molecular and immunological analysis of an ABC transporter required for cytochromec biogenesis
    • Goldman BS, Beckman DL, Bali A, Monika EM, Gabbert, KK, Kranz RG (1997) Molecular and immunological analysis of an ABC transporter required for cytochromec biogenesis. J Mol Biol 268:724-738
    • (1997) J Mol Biol , vol.268 , pp. 724-738
    • Goldman, B.S.1    Beckman, D.L.2    Bali, A.3    Monika, E.M.4    Gabbert, K.K.5    Kranz, R.G.6
  • 18
    • 0023802457 scopus 로고
    • The nucleotide sequence of the cyd locus encoding the two subunits of the cytochrome d terminal oxidase complex of Escherichia coli
    • Green GN, Fang H, Lin R, Newton G, Mather M, Georgiou CD, Gennis RB (1988) The nucleotide sequence of the cyd locus encoding the two subunits of the cytochrome d terminal oxidase complex of Escherichia coli. J Biol Chem 263:13138-13143
    • (1988) J Biol Chem , vol.263 , pp. 13138-13143
    • Green, G.N.1    Fang, H.2    Lin, R.3    Newton, G.4    Mather, M.5    Georgiou, C.D.6    Gennis, R.B.7
  • 19
    • 0015754147 scopus 로고
    • The reconstitution of oxidase activity in membranes derived from a 5-aminolaevulinic acid-requiring mutant of Escherichia coli
    • Haddock BA (1973) The reconstitution of oxidase activity in membranes derived from a 5-aminolaevulinic acid-requiring mutant of Escherichia coli. Biochem J 136:877-884
    • (1973) Biochem J , vol.136 , pp. 877-884
    • Haddock, B.A.1
  • 20
    • 0015839642 scopus 로고
    • Electron-transport chains of Escherichia coli: Reconstitution of respiration in a 5-aminolae-vulinic acid-requiring mutant
    • Haddock BA, Schairer HU (1973) Electron-transport chains of Escherichia coli: reconstitution of respiration in a 5-aminolae-vulinic acid-requiring mutant. Eur J Biochem 35:34-45
    • (1973) Eur J Biochem , vol.35 , pp. 34-45
    • Haddock, B.A.1    Schairer, H.U.2
  • 21
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins CF (1992) ABC transporters: from microorganisms to man. Annu Rev Cell Biol 8:67-113
    • (1992) Annu Rev Cell Biol , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 23
    • 0021272743 scopus 로고
    • 558-d complex from cells grown with limited oxygen and evidence of branched electron carrying systems
    • 558-d complex from cells grown with limited oxygen and evidence of branched electron carrying systems. J Biol Chem 259:3375-3381
    • (1984) J Biol Chem , vol.259 , pp. 3375-3381
    • Kita, K.1    Konishi, K.2    Anraku, Y.3
  • 24
    • 0028158185 scopus 로고
    • Azorhizobium caulinodans respires with at least four terminal oxidases
    • Kitts C, Ludwig RA (1994) Azorhizobium caulinodans respires with at least four terminal oxidases. J Bacteriol 176:886-895
    • (1994) J Bacteriol , vol.176 , pp. 886-895
    • Kitts, C.1    Ludwig, R.A.2
  • 25
    • 0031943304 scopus 로고    scopus 로고
    • The Escherichia coli ATP-binding cassette (ABC) proteins
    • Linton KJ, Higgins CF (1998) The Escherichia coli ATP-binding cassette (ABC) proteins. Mol Microbiol 28:5-13
    • (1998) Mol Microbiol , vol.28 , pp. 5-13
    • Linton, K.J.1    Higgins, C.F.2
  • 28
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to modify protein determination in membrane and lipoprotein samples
    • Markwell MAK, Haas SM, Bieber LL, Tolbert NE (1978) A modification of the Lowry procedure to modify protein determination in membrane and lipoprotein samples. Anal Biochem 87: 206-210
    • (1978) Anal Biochem , vol.87 , pp. 206-210
    • Markwell, M.A.K.1    Haas, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 29
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
    • Miller JH (1972) Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 30
    • 0033044722 scopus 로고    scopus 로고
    • Sequence analysis of cytochrome bd oxidase suggests a revised topology for subunit I
    • Osborne JP, Gennis RB (1999) Sequence analysis of cytochrome bd oxidase suggests a revised topology for subunit I. Biochim Biophys Acta 1410:32-50
    • (1999) Biochim Biophys Acta , vol.1410 , pp. 32-50
    • Osborne, J.P.1    Gennis, R.B.2
  • 31
    • 0035985617 scopus 로고    scopus 로고
    • Biochemistry, regulation and genomics of haem biosynthesis in prokaryotes
    • Poole RK (ed). Academic, London
    • O'Brian MR, Thöny-Meyer L (2002) Biochemistry, regulation and genomics of haem biosynthesis in prokaryotes. In: Poole RK (ed) Advances in microbial physiol, vol 46. Academic, London, 257-318
    • (2002) Advances in Microbial Physiol , vol.46 , pp. 257-318
    • O'Brian, M.R.1    Thöny-Meyer, L.2
  • 32
    • 0021104863 scopus 로고
    • Bacterial cytochrome oxidases. A structurally and functionally diverse group of electron-transfer proteins
    • Poole RK (1983) Bacterial cytochrome oxidases. A structurally and functionally diverse group of electron-transfer proteins. Biochim Biophys Acta 726:205-243
    • (1983) Biochim Biophys Acta , vol.726 , pp. 205-243
    • Poole, R.K.1
  • 33
    • 0016279021 scopus 로고
    • Energy-linked reduction of nicotinamide-adenine dinucleotide in membranes derived from normal and various respiratory-deficient mutant strains of Escherichia coli K12
    • Poole RK, Haddock BA (1974) Energy-linked reduction of nicotinamide-adenine dinucleotide in membranes derived from normal and various respiratory-deficient mutant strains of Escherichia coli K12. Biochem J 144:77-85
    • (1974) Biochem J , vol.144 , pp. 77-85
    • Poole, R.K.1    Haddock, B.A.2
  • 34
    • 0033928977 scopus 로고    scopus 로고
    • Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation
    • Poole RK (ed). Academic, London
    • Poole RK, Cook GM (2000) Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation. In: Poole RK (ed) Advances in microbial physiol, vol 43. Academic, London, pp 165-224
    • (2000) Advances in Microbial Physiol , vol.43 , pp. 165-224
    • Poole, R.K.1    Cook, G.M.2
  • 35
    • 0000556195 scopus 로고
    • Pathways of electrons to oxygen
    • Neidhardt FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, Umbarger HE (eds). ASM, Washington DC
    • Poole RK, Ingledew WJ (1987) Pathways of electrons to oxygen. In: Neidhardt FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, Umbarger HE (eds) Escherichia coli and Salmonella typhimurium: cellular and molecular biology. ASM, Washington DC, pp 170-200
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 170-200
    • Poole, R.K.1    Ingledew, W.J.2
  • 36
    • 17944386101 scopus 로고
    • Mutations affecting the cytochrome d-containing oxidase complex of Escherichia coli K12: Identification and mapping of a fourth locus, cydD
    • Poole RK, Williams HD, Downie JA, Gibson F (1989) Mutations affecting the cytochrome d-containing oxidase complex of Escherichia coli K12: identification and mapping of a fourth locus, cydD. J Gen Microbiol 135:1865-1874
    • (1989) J Gen Microbiol , vol.135 , pp. 1865-1874
    • Poole, R.K.1    Williams, H.D.2    Downie, J.A.3    Gibson, F.4
  • 37
    • 0027489253 scopus 로고
    • Cytochrome bd biosynthesis in Escherichia coli: The sequences of the cydC and cydD genes suggest that they encode the components of an ABC membrane transporter
    • Poole RK, Hatch L, Cleeter MWJ, Gibson F, Cox GB, Wu G (1993). Cytochrome bd biosynthesis in Escherichia coli: the sequences of the cydC and cydD genes suggest that they encode the components of an ABC membrane transporter. Mol Microbiol 10:421-430
    • (1993) Mol Microbiol , vol.10 , pp. 421-430
    • Poole, R.K.1    Hatch, L.2    Cleeter, M.W.J.3    Gibson, F.4    Cox, G.B.5    Wu, G.6
  • 38
    • 0028177039 scopus 로고
    • The cydD gene product, component of a heterodimeric ABC transporter, is required for assembly of periplasmic cytochrome c and of cytochrome bd in Escherichia coli
    • Poole RK, Gibson F, Wu G (1994) The cydD gene product, component of a heterodimeric ABC transporter, is required for assembly of periplasmic cytochrome c and of cytochrome bd in Escherichia coli. FEMS Microbiol Lett 117:217-224
    • (1994) FEMS Microbiol Lett , vol.117 , pp. 217-224
    • Poole, R.K.1    Gibson, F.2    Wu, G.3
  • 41
    • 0029858145 scopus 로고    scopus 로고
    • The stationary-phase-exit defect of cydC (surB) mutants is due to the lack of a functional terminal cytochrome oxidase
    • Siegele DA, Imlay KRC, Imlay JA (1996) The stationary-phase-exit defect of cydC (surB) mutants is due to the lack of a functional terminal cytochrome oxidase. J Bacteriol 178:6091-6096
    • (1996) J Bacteriol , vol.178 , pp. 6091-6096
    • Siegele, D.A.1    Imlay, K.R.C.2    Imlay, J.A.3
  • 42
    • 0031938408 scopus 로고    scopus 로고
    • Requirement for ubiquinone downstream of cytochrome(s) b in the oxygen-terminated respiratory chains of Escherichia coli K-12 revealed using a null mutant allele of ubiCA
    • Søballe B, Poole RK (1998) Requirement for ubiquinone downstream of cytochrome(s) b in the oxygen-terminated respiratory chains of Escherichia coli K-12 revealed using a null mutant allele of ubiCA. Microbiology 144:361-373
    • (1998) Microbiology , vol.144 , pp. 361-373
    • Søballe, B.1    Poole, R.K.2
  • 43
    • 0037990786 scopus 로고    scopus 로고
    • Biogenesis of respiratory cytochromes in bacteria
    • Tḧny-Meyer L (1997) Biogenesis of respiratory cytochromes in bacteria. Microbiol Biol Rev 61:337-376
    • (1997) Microbiol Biol Rev , vol.61 , pp. 337-376
    • Thöny-Meyer, L.1
  • 44
    • 0030067649 scopus 로고    scopus 로고
    • Effect of micro-aerophilic cell growth conditions on expression of the aerobic (cyoABCDE and cydAB) and anaerobic (narGHJI, frdABCD, and dmsABC) respiratory pathway genes in Escherichia coli
    • Tseng CP, Albrecht J, Gunsalus RP (1996) Effect of micro-aerophilic cell growth conditions on expression of the aerobic (cyoABCDE and cydAB) and anaerobic (narGHJI, frdABCD, and dmsABC) respiratory pathway genes in Escherichia coli. J Bacteriol 178:1094-1098
    • (1996) J Bacteriol , vol.178 , pp. 1094-1098
    • Tseng, C.P.1    Albrecht, J.2    Gunsalus, R.P.3
  • 45
    • 0028931946 scopus 로고
    • Distribution of the flavohaemoglobin, HMP, between periplasm and cytoplasm in Escherichia coli
    • Vasudevan SG, Tang P, Dixon NE, Poole RK (1995) Distribution of the flavohaemoglobin, HMP, between periplasm and cytoplasm in Escherichia coli. FEMS Microbiol Lett 125:219-224
    • (1995) FEMS Microbiol Lett , vol.125 , pp. 219-224
    • Vasudevan, S.G.1    Tang, P.2    Dixon, N.E.3    Poole, R.K.4
  • 46
    • 0034652126 scopus 로고    scopus 로고
    • Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: A di-heme active site?
    • Vos MH, Borisov VB, Liebl U, Martin JL, Konstantinov AA (2000) Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: a di-heme active site? Proc Natl Acad Sci USA 97:1554-1559
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1554-1559
    • Vos, M.H.1    Borisov, V.B.2    Liebl, U.3    Martin, J.L.4    Konstantinov, A.A.5
  • 48
    • 0021766171 scopus 로고
    • Bacterial proteins with CO-binding b- or c-type haem. Functions and absorption spectroscopy
    • Wood PM (1984) Bacterial proteins with CO-binding b- or c-type haem. Functions and absorption spectroscopy. Biochim Biophys Acta 768, 293-317
    • (1984) Biochim Biophys Acta , vol.768 , pp. 293-317
    • Wood, P.M.1
  • 49
    • 0030741757 scopus 로고    scopus 로고
    • The cydR gene product, required for regulation of cytochrome bd expression in the obligate aerobe Azotobacter vinelandii, is an Fnr-like protein
    • Wu G, Hill S, Kelly MJS, Sawers G, Poole RK (1997) The cydR gene product, required for regulation of cytochrome bd expression in the obligate aerobe Azotobacter vinelandii, is an Fnr-like protein. Microbiology 143:2197-2207
    • (1997) Microbiology , vol.143 , pp. 2197-2207
    • Wu, G.1    Hill, S.2    Kelly, M.J.S.3    Sawers, G.4    Poole, R.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.