메뉴 건너뛰기




Volumn 307, Issue 1, 2010, Pages 41-47

A purified mutant HemA protein from Salmonella enterica serovar Typhimurium lacks bound heme and is defective for heme-mediated regulation in vivo

Author keywords

HemA; Heme; Salmonella

Indexed keywords

BACTERIAL PROTEIN; HEMA PROTEIN; HEME; MUTANT PROTEIN; UNCLASSIFIED DRUG;

EID: 77951953046     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2010.01967.x     Document Type: Article
Times cited : (24)

References (31)
  • 1
    • 0001918155 scopus 로고    scopus 로고
    • Biosynthesis of hemes
    • Neidhardt, F.C. Curtiss, R.III. Ingraham, J.L. Lin, E.C.C. Low, K.B. Magasanik, B. Reznikoff, W.S. Riley, M. Schaechter, M. Umbarger, H.E. eds), American Society of Microbiology
    • Beale SI (1996) Biosynthesis of hemes. Escherichia coli and Salmonella: Cellular and Molecular Biology (Neidhardt FC, Curtiss R III., Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M Umbarger HE, eds), pp. 731 748. American Society of Microbiology
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 731-748
    • Beale, S.I.1
  • 3
    • 0020443521 scopus 로고
    • Complete analysis of cellular nucleotides by two-dimensional thin layer chromatography
    • Bochner BR Ames BN (1982) Complete analysis of cellular nucleotides by two-dimensional thin layer chromatography. J Biol Chem 257 : 9759 9769. (Pubitemid 13205141)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.16 , pp. 9759-9769
    • Bochner, B.R.1    Ames, B.N.2
  • 4
    • 41049111259 scopus 로고    scopus 로고
    • S (RpoS) stability in Escherichia coli via the action of multiple anti-adaptors
    • DOI 10.1111/j.1365-2958.2008.06146.x
    • Bougdour A, Cunning C, Baptiste PJ, Elliott T Gottesman S (2008) Multiple pathways for regulation of sigmaS (RpoS) stability in Escherichia coli via the action of multiple anti-adaptors. Mol Microbiol 68 : 298 313. (Pubitemid 351422952)
    • (2008) Molecular Microbiology , vol.68 , Issue.2 , pp. 298-313
    • Bougdour, A.1    Cunning, C.2    Baptiste, P.J.3    Elliott, T.4    Gottesman, S.5
  • 5
    • 0032750527 scopus 로고    scopus 로고
    • Predicted structure and fold recognition for the glutamyl tRNA reductase family of proteins
    • Brody SS, Gough SP Kannangara CG (1999) Predicted structure and fold recognition for the glutamyl tRNA reductase family of proteins. Proteins 37 : 485 493.
    • (1999) Proteins , vol.37 , pp. 485-493
    • Brody, S.S.1    Gough, S.P.2    Kannangara, C.G.3
  • 7
    • 0027173647 scopus 로고
    • Detection and quantitation of heme-containing proteins by chemiluminescence
    • DOI 10.1006/abio.1993.1110
    • Dorward DW (1993) Detection and quantitation of heme-containing proteins by chemiluminescence. Anal Biochem 209 : 219 223. (Pubitemid 23130176)
    • (1993) Analytical Biochemistry , vol.209 , Issue.2 , pp. 219-223
    • Dorward, D.W.1
  • 8
    • 0002263294 scopus 로고
    • Heme: Determination as pyridine hemochromes
    • Smith, K.M. (eds), Elsevier Science Inc.
    • Fuhrhop JH Smith KM (1975) Heme: determination as pyridine hemochromes. Porphyrins and Metalloporphyrins (Smith KM, eds), pp. 804 807. Elsevier Science Inc.
    • (1975) Porphyrins and Metalloporphyrins , pp. 804-807
    • Fuhrhop, J.H.1    Smith, K.M.2
  • 9
    • 0029737827 scopus 로고    scopus 로고
    • The stability of holomyoglobin is determined by heme affinity
    • Hargrove MS Olson JS (1996) The stability of holomyoglobin is determined by heme affinity. Biochemistry 35 : 11310 11318.
    • (1996) Biochemistry , vol.35 , pp. 11310-11318
    • Hargrove, M.S.1    Olson, J.S.2
  • 10
    • 0024149272 scopus 로고
    • Biosynthesis of delta-aminolevulinate in greening barley leaves. IX. Structure of the substrate, mode of gabaculine inhibition, and the catalytic mechanism of glutamate-1-semialdehyde aminotransferase
    • Hoober JK, Kahn A, Ash DE, Gough S Kannangara CG (1988) Biosynthesis of delta-aminolevulinate in greening barley leaves. IX. Structure of the substrate, mode of gabaculine inhibition, and the catalytic mechanism of glutamate-1-semialdehyde aminotransferase. Carlsberg Res Commun 53 : 11 25.
    • (1988) Carlsberg Res Commun , vol.53 , pp. 11-25
    • Hoober, J.K.1    Kahn, A.2    Ash, D.E.3    Gough, S.4    Kannangara, C.G.5
  • 12
    • 0026686195 scopus 로고
    • Glutamyl-transfer RNA: A precursor of heme and chlorophyll biosynthesis
    • Jahn K, Verkamp E Soll D (1992) Glutamyl-transfer RNA: a precursor of heme and chlorophyll biosynthesis. Trends Biochem Sci 17 : 215 218.
    • (1992) Trends Biochem Sci , vol.17 , pp. 215-218
    • Jahn, K.1    Verkamp, E.2    Soll, D.3
  • 13
    • 34447526071 scopus 로고    scopus 로고
    • Structural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins
    • Landfried DA, Vuletich DA, Pond MP Lecomte JT (2007) Structural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins. Gene 398 : 12 28.
    • (2007) Gene , vol.398 , pp. 12-28
    • Landfried, D.A.1    Vuletich, D.A.2    Pond, M.P.3    Lecomte, J.T.4
  • 14
    • 21444433241 scopus 로고    scopus 로고
    • Complex formation between glutamyl-tRNA reductase and glutamate-1- semialdehyde 2,1-aminomutase in Escherichia coli during the initial reactions of porphyrin biosynthesis
    • DOI 10.1074/jbc.M500440200
    • Lüer C, Schauer S, Mobius K, Schulze J, Schubert WD, Heinz DW, Jahn D Moser J (2005) Complex formation between glutamyl-tRNA reductase and glutamate-1-semialdehyde 2,1-aminomutase in Escherichia coli during the initial reactions of porphyrin biosynthesis. J Biol Chem 280 : 18568 18572. (Pubitemid 41379554)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.19 , pp. 18568-18572
    • Luer, C.1    Schauer, S.2    Mobius, K.3    Schulze, J.4    Schubert, W.-D.5    Heinz, D.W.6    Jahn, D.7    Moser, J.8
  • 17
    • 0035803598 scopus 로고    scopus 로고
    • V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis
    • DOI 10.1093/emboj/20.23.6583
    • Moser J, Wolf-Dieter S, Beler V, Bringemeier I, Jahn D Heinz DW (2001) V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis. EMBO J 20 : 6583 6590. (Pubitemid 33134189)
    • (2001) EMBO Journal , vol.20 , Issue.23 , pp. 6583-6590
    • Moser, J.1    Schubert, W.-D.2    Beier, V.3    Bringemeier, I.4    Jahn, D.5    Heinz, D.W.6
  • 19
    • 21644490055 scopus 로고    scopus 로고
    • Physical and kinetic interactions between glutamyl-tRNA reductase and glutamate-1-semialdehyde aminotransferase of Chlamydomonas reinhardtii
    • DOI 10.1074/jbc.M502483200
    • Nogaj LA Beale SI (2005) Physical and kinetic interactions between glutamyl-tRNA reductase and glutamate-1-semialdehyde aminotransferase of Chlamydomonas reinhardtii. J Biol Chem 280 : 24301 24307. (Pubitemid 40934511)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24301-24307
    • Nogaj, L.A.1    Beale, S.I.2
  • 20
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L, Grimsley G Gray T (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4 : 2411 2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 22
    • 0026528899 scopus 로고
    • Glutamyl-tRNA reductase activity in Bacillus subtilis is dependent on the hemA gene product
    • Schroder I, Hederstedt L, Kannangara CG Gough P (1992) Glutamyl-tRNA reductase activity in Bacillus subtilis is dependent on the hemA gene product. Biochem J 281 : 843 850.
    • (1992) Biochem J , vol.281 , pp. 843-850
    • Schroder, I.1    Hederstedt, L.2    Kannangara, C.G.3    Gough, P.4
  • 23
    • 21144441269 scopus 로고    scopus 로고
    • Glutamyl-tRNA reductase of Chlorobium vibrioforme is a dissociable homodimer that contains one tightly bound heme per subunit
    • DOI 10.1128/JB.187.13.4444-4450.2005
    • Srivastava A Beale SI (2005) Glutamyl-tRNA reductase of Chlorobium vibrioforme is a dissociable homodimer that contains one tightly bound heme per subunit. J Bacteriol 187 : 4444 4450. (Pubitemid 40880954)
    • (2005) Journal of Bacteriology , vol.187 , Issue.13 , pp. 4444-4450
    • Srivastava, A.1    Beale, S.I.2
  • 24
    • 24744463539 scopus 로고    scopus 로고
    • The Chlamydomonas reinhardtii gtr gene encoding the tetrapyrrole biosynthetic enzyme glutamyl-tRNA reductase: Structure of the gene and properties of the expressed enzyme
    • DOI 10.1007/s11103-005-6803-x
    • Srivastava A, Lake V, Nogaj LA, Mayer SM, Willows RD Beale SI (2005) The Chlamydomonas reinhardtii gtr gene encoding the tetrapyrrole biosynthetic enzyme glutamyl-tRNA reductase: structure of the gene and properties of the expressed enzyme. Plant Mol Biol 58 : 643 658. (Pubitemid 41297945)
    • (2005) Plant Molecular Biology , vol.58 , Issue.5 , pp. 643-658
    • Srivastava, A.1    Lake, V.2    Nogaj, L.A.3    Mayer, S.M.4    Willows, R.D.5    Beale, S.I.6
  • 25
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier FW Moffatt BA (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189 : 113 130.
    • (1986) J Mol Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 26
    • 0026640644 scopus 로고
    • Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression
    • Verkamp E, Jahn M, Jahn D, Kumar AM Soll D (1992) Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression. J Biol Chem 267 : 8275 8280.
    • (1992) J Biol Chem , vol.267 , pp. 8275-8280
    • Verkamp, E.1    Jahn, M.2    Jahn, D.3    Kumar, A.M.4    Soll, D.5
  • 28
    • 0344361618 scopus 로고    scopus 로고
    • Regulation of heme biosynthesis in Salmonella typhimurium: Activity of glutamyl-tRNA reductase (HemA) is greatly elevated during heme limitation by a mechanism which increases abundance of the protein
    • Wang LY, Brown L, Elliott M Elliott T (1997) Regulation of heme biosynthesis in Salmonella typhimurium: activity of glutamyl-tRNA reductase (HemA) is greatly elevated during heme limitation by a mechanism which increases abundance of the protein. J Bacteriol 179 : 2907 2914. (Pubitemid 27194438)
    • (1997) Journal of Bacteriology , vol.179 , Issue.9 , pp. 2907-2914
    • Wang, L.Y.1    Brown, L.2    Elliott, M.3    Elliott, T.4
  • 29
    • 0032986721 scopus 로고    scopus 로고
    • Conditional stability of the HemA protein (Glutamyl-tRNA reductase) regulates heme biosynthesis in Salmonella typhimurium
    • Wang L, Elliott M Elliott T (1999a) Conditional stability of the HemA protein (glutamyl-tRNA reductase) regulates heme biosynthesis in Salmonella typhimurium. J Bacteriol 181 : 1211 1219. (Pubitemid 29119560)
    • (1999) Journal of Bacteriology , vol.181 , Issue.4 , pp. 1211-1219
    • Wang, L.1    Elliott, M.2    Elliott, T.3
  • 30
    • 0032841896 scopus 로고    scopus 로고
    • A mutant HemA protein with positive charge close to the N terminus is stabilized against heme-regulated proteolysis in Salmonella typhimurium
    • Wang L, Wilson S Elliott T (1999b) A mutant HemA protein with positive charge close to the N terminus is stabilized against heme-regulated proteolysis in Salmonella typhimurium. J Bacteriol 181 : 6033 6041. (Pubitemid 29459914)
    • (1999) Journal of Bacteriology , vol.181 , Issue.19 , pp. 6033-6041
    • Wang, L.1    Wilson, S.2    Elliott, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.