메뉴 건너뛰기




Volumn 142, Issue 2, 1996, Pages 389-400

The second aconitase (AcnB) of Escherichia coli

Author keywords

Aconitase; Citric acid cycle; Escherichia coli; Iron sulphur proteins; Protein domains

Indexed keywords

ACONITATE HYDRATASE; POLYPEPTIDE;

EID: 0030067082     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/13500872-142-2-389     Document Type: Article
Times cited : (31)

References (30)
  • 1
    • 0028809657 scopus 로고
    • Spectroscopic characterisation of an aconitase (AcnA) of Escherichia coli
    • Bennett, B., Gruer, M. J., Guest, J. R. & Thomson, A. J. (1995). Spectroscopic characterisation of an aconitase (AcnA) of Escherichia coli. Eur J Biochem 233, 317-326.
    • (1995) Eur J Biochem , vol.233 , pp. 317-326
    • Bennett, B.1    Gruer, M.J.2    Guest, J.R.3    Thomson, A.J.4
  • 2
    • 0002739485 scopus 로고    scopus 로고
    • Integrated linkage map of Escherichia coli K-12, edition 9
    • Edited by F. C. Neidhardt, R. Curtiss, III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. Reznikoff, M. Riley, M. Schaechter & H. E. Umbarger. Washington, DC: American Society for Microbiology
    • Berlyn, M. B., Low K. B. & Rudd K. E. (1996). Integrated linkage map of Escherichia coli K-12, edition 9. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, 2nd edn. Edited by F. C. Neidhardt, R. Curtiss, III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. Reznikoff, M. Riley, M. Schaechter & H. E. Umbarger. Washington, DC: American Society for Microbiology.
    • (1996) Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, 2nd Edn.
    • Berlyn, M.B.1    Low, K.B.2    Rudd, K.E.3
  • 3
    • 0018963867 scopus 로고
    • Genetic and physical characterization of lambda transducing phages (λfrdA) containing the fumarate reductase gene of Escherichia coli K12
    • Cole, S. T. & Guest, J. R. (1980). Genetic and physical characterization of lambda transducing phages (λfrdA) containing the fumarate reductase gene of Escherichia coli K12. Mol & Gen Genet 178, 409-418.
    • (1980) Mol & Gen Genet , vol.178 , pp. 409-418
    • Cole, S.T.1    Guest, J.R.2
  • 4
    • 0027297916 scopus 로고
    • Iron regulatory factor expressed from recombinant baculovirus: Conversion between the RNA-binding apo-protein and Fe-S cluster containing aconitase
    • Emery-Goodman, A., Hirling, H., Scarpellino, L., Henderson, B. & Kuhn, L. (1993). Iron regulatory factor expressed from recombinant baculovirus: conversion between the RNA-binding apo-protein and Fe-S cluster containing aconitase. Nucleic Acids Res 21, 1457-1461.
    • (1993) Nucleic Acids Res , vol.21 , pp. 1457-1461
    • Emery-Goodman, A.1    Hirling, H.2    Scarpellino, L.3    Henderson, B.4    Kuhn, L.5
  • 5
    • 0028290288 scopus 로고
    • Systematic sequencing of the Escherichia coli genome : Analysis of the 2-4-4-1 min (110,917-193,643 bp) region
    • Fujita, U., Mori, H., Yura, T. & Ishihama, A. (1994). Systematic sequencing of the Escherichia coli genome : analysis of the 2-4-4-1 min (110,917-193,643 bp) region. Nucleic Acids Res 22, 1637-1639.
    • (1994) Nucleic Acids Res , vol.22 , pp. 1637-1639
    • Fujita, U.1    Mori, H.2    Yura, T.3    Ishihama, A.4
  • 6
    • 0027131432 scopus 로고
    • Recombinant iron-regulatory factor functions as an iron-responsive-element-binding protein, a tianslational repressor and an aconitase
    • Gray, N. K., Quick, S., Goossen, B., Constable, A., Hirling, H., Kuhn, L. C. & Hentze, M. W. (1993). Recombinant iron-regulatory factor functions as an iron-responsive-element-binding protein, a tianslational repressor and an aconitase. Eur J Biochem 218, 657-667.
    • (1993) Eur J Biochem , vol.218 , pp. 657-667
    • Gray, N.K.1    Quick, S.2    Goossen, B.3    Constable, A.4    Hirling, H.5    Kuhn, L.C.6    Hentze, M.W.7
  • 8
    • 0020363515 scopus 로고
    • Preferential codon usage in prokaryotic genes : The optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes
    • Grosjean, H. & Fiers, W. (1982). Preferential codon usage in prokaryotic genes : the optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes. Gene 18, 199-209.
    • (1982) Gene , vol.18 , pp. 199-209
    • Grosjean, H.1    Fiers, W.2
  • 9
    • 0028113546 scopus 로고
    • Two genetically-distinct and differentially-regulated aconitases (AcnA and AcnB) in Escherichia coli
    • Gruer, M. J. & Guest, J. R. (1994). Two genetically-distinct and differentially-regulated aconitases (AcnA and AcnB) in Escherichia coli. Microbiology 140, 2531-2541.
    • (1994) Microbiology , vol.140 , pp. 2531-2541
    • Gruer, M.J.1    Guest, J.R.2
  • 10
    • 0026442487 scopus 로고
    • Oxygen-regulated gene expression in Escherichia coli
    • Guest, J. R. (1992). Oxygen-regulated gene expression in Escherichia coli. J Gen Microbiol 138, 2253-2263.
    • (1992) J Gen Microbiol , vol.138 , pp. 2253-2263
    • Guest, J.R.1
  • 11
    • 0029477755 scopus 로고
    • The Leeuwenhoek Lecture, 1995. Adaptation to life without oxygen
    • Guest, J. R. (1995). The Leeuwenhoek Lecture, 1995. Adaptation to life without oxygen. Philos Trans R Soc Lond B Biol Sci 350, 189-202.
    • (1995) Philos Trans R Soc Lond B Biol Sci , vol.350 , pp. 189-202
    • Guest, J.R.1
  • 12
    • 0028131454 scopus 로고
    • Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase activity
    • Guo, B., Yu, Y. & Leibold, E. A. (1994). Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase activity. J Biol Chem 269, 24252-24260.
    • (1994) J Biol Chem , vol.269 , pp. 24252-24260
    • Guo, B.1    Yu, Y.2    Leibold, E.A.3
  • 13
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. (1983). Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166, 557-580.
    • (1983) J Mol Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 14
    • 0027717217 scopus 로고
    • Characterization of a second RNA-binding protein in rodents with specificity for iron-responsive elements
    • Henderson, B. R., Seiser, C. & Kuhn, L. C. (1993). Characterization of a second RNA-binding protein in rodents with specificity for iron-responsive elements. J Biol Chem 268, 27327-27334.
    • (1993) J Biol Chem , vol.268 , pp. 27327-27334
    • Henderson, B.R.1    Seiser, C.2    Kuhn, L.C.3
  • 15
    • 0024598146 scopus 로고
    • Fast and sensitive multiple sequence alignments on a microcomputer
    • Higgins, D. G. & Sharp, P. M. (1989). Fast and sensitive multiple sequence alignments on a microcomputer. Comp Appl Biosci 5, 151-153.
    • (1989) Comp Appl Biosci , vol.5 , pp. 151-153
    • Higgins, D.G.1    Sharp, P.M.2
  • 16
    • 0028009430 scopus 로고
    • Mutational analysis of the [4Fe-4S]-cluster converting iron regulatory factor from its RNA-binding form to cytoplasmic aconitase
    • Hirling, H., Henderson, B. R. & Kuhn, L. C. (1994). Mutational analysis of the [4Fe-4S]-cluster converting iron regulatory factor from its RNA-binding form to cytoplasmic aconitase. EMBO J 13, 453-461.
    • (1994) EMBO J , vol.13 , pp. 453-461
    • Hirling, H.1    Henderson, B.R.2    Kuhn, L.C.3
  • 17
    • 0021112587 scopus 로고
    • The role of iron in the activation-inactivation of aconitase
    • Kennedy, M. C., Emptage, M. H., Drey er, J.-L. & Bienert, H. (1983). The role of iron in the activation-inactivation of aconitase. J Biol Chem 258, 11098-11105.
    • (1983) J Biol Chem , vol.258 , pp. 11098-11105
    • Kennedy, M.C.1    Emptage, M.H.2    Dreyer, J.-L.3    Bienert, H.4
  • 18
    • 0028960504 scopus 로고
    • Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding
    • Khoroshilova, N., Beinert, H. & Kiley, P. J. (1995). Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding. Proc Natl Acad Sci USA 92, 2499-2503.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2499-2503
    • Khoroshilova, N.1    Beinert, H.2    Kiley, P.J.3
  • 19
    • 0027479724 scopus 로고
    • A double life: Cytosolic aconitase as a regulatory RNA binding protein
    • Klausner, R. D. & Rouault, T. A. (1993). A double life: cytosolic aconitase as a regulatory RNA binding protein. Mol Biol Cell 4, 1-5.
    • (1993) Mol Biol Cell , vol.4 , pp. 1-5
    • Klausner, R.D.1    Rouault, T.A.2
  • 20
    • 0023669069 scopus 로고
    • The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic library
    • Kohara, Y., Akiyama, K. & Isono, K. (1987). The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell 50, 495-508.
    • (1987) Cell , vol.50 , pp. 495-508
    • Kohara, Y.1    Akiyama, K.2    Isono, K.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0025943925 scopus 로고
    • The aconitase of Escherichia coli: Purification of the enzyme and molecular cloning and map location of the gene (acn)
    • Prodromou, C., Haynes, M. J. & Guest J. R. (1991). The aconitase of Escherichia coli: purification of the enzyme and molecular cloning and map location of the gene (acn). J Gen Microbiol 137, 2505-2515.
    • (1991) J Gen Microbiol , vol.137 , pp. 2505-2515
    • Prodromou, C.1    Haynes, M.J.2    Guest, J.R.3
  • 23
    • 0026517563 scopus 로고
    • The aconitase of Escherichia coli: Nucleotide sequence of the aconitase gene and amino acid sequence similarity with mitochondrial aconitases, the iron-responsive-element-binding protein and isopropylmalate isomerases
    • Prodromou, C., Artymiuk, P. J. & Guest, J. R. (1992). The aconitase of Escherichia coli: nucleotide sequence of the aconitase gene and amino acid sequence similarity with mitochondrial aconitases, the iron-responsive-element-binding protein and isopropylmalate isomerases. Eur J Biochem 204, 599-609.
    • (1992) Eur J Biochem , vol.204 , pp. 599-609
    • Prodromou, C.1    Artymiuk, P.J.2    Guest, J.R.3
  • 24
    • 0027213864 scopus 로고
    • Identification of the L-tartrate dehydratase genes (ttdA and ttdB) of Escherichia coli and evolutionary relationship with the Class I fumarase genes
    • Reaney, S. K., Begg, C., Bungard, S. J. & Guest, J. R. (1993). Identification of the L-tartrate dehydratase genes (ttdA and ttdB) of Escherichia coli and evolutionary relationship with the Class I fumarase genes. J Gen Microbiol 139, 1523-1530.
    • (1993) J Gen Microbiol , vol.139 , pp. 1523-1530
    • Reaney, S.K.1    Begg, C.2    Bungard, S.J.3    Guest, J.R.4
  • 25
    • 0024383933 scopus 로고
    • The structure of aconitase
    • Robbins, A. H. & Stout, C. D. (1989). The structure of aconitase. Proteins 5, 289-312.
    • (1989) Proteins , vol.5 , pp. 289-312
    • Robbins, A.H.1    Stout, C.D.2
  • 26
    • 0025289939 scopus 로고
    • The nucleotide sequence of leuC from Salmonella typhimurium
    • Rosenthal, E. R. & Calvo, J. M. (1990). The nucleotide sequence of leuC from Salmonella typhimurium. Nucleic Acids Res 18, 3072.
    • (1990) Nucleic Acids Res , vol.18 , pp. 3072
    • Rosenthal, E.R.1    Calvo, J.M.2
  • 28
    • 0000507749 scopus 로고
    • Matrices for detecting distant relationships
    • Edited by M. O. Dayhoff. Washington, DC: National Biomedical Research Foundation
    • Schwartz, R. M. & Dayhoff, M. O. (1979). Matrices for detecting distant relationships. In Atlas of Protein Sequences and Structure, pp. 353-358. Edited by M. O. Dayhoff. Washington, DC: National Biomedical Research Foundation.
    • (1979) Atlas of Protein Sequences and Structure , pp. 353-358
    • Schwartz, R.M.1    Dayhoff, M.O.2
  • 29
    • 0020480286 scopus 로고
    • An interactive graphics program for comparing and aligning nucleic acid and amino acid sequences
    • Staden, R. (1982). An interactive graphics program for comparing and aligning nucleic acid and amino acid sequences. Nucleic Acids Res 10, 2951-2961.
    • (1982) Nucleic Acids Res , vol.10 , pp. 2951-2961
    • Staden, R.1
  • 30
    • 0028339794 scopus 로고
    • Catalytic formation of a nitrogenase iron-sulfur cluster
    • Zheng, L. & Dean, D. R. (1994). Catalytic formation of a nitrogenase iron-sulfur cluster. J Biol Chem 269, 18723-18726.
    • (1994) J Biol Chem , vol.269 , pp. 18723-18726
    • Zheng, L.1    Dean, D.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.