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Volumn 154, Issue 1, 2007, Pages 30-39

Nuclear gyrB encodes a functional subunit of the Plasmodium falciparum gyrase that is involved in apicoplast DNA replication

Author keywords

Apicoplast; Gyrase; Novobiocin; Plasmodium falciparum; Replication

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DNA; ENZYME; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; GYRASE A; GYRASE B; UNCLASSIFIED DRUG;

EID: 34249986680     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2007.04.001     Document Type: Article
Times cited : (66)

References (49)
  • 1
    • 0032987667 scopus 로고    scopus 로고
    • The apicoplast as a potential therapeutic target in Toxoplasma and other apicomplexan parasites
    • Soldati D. The apicoplast as a potential therapeutic target in Toxoplasma and other apicomplexan parasites. Parasitol Today 15 (1999) 5-7
    • (1999) Parasitol Today , vol.15 , pp. 5-7
    • Soldati, D.1
  • 2
    • 0032815207 scopus 로고    scopus 로고
    • Apicomplexan plastids as drug targets
    • McFadden G.I., and Roos D.S. Apicomplexan plastids as drug targets. Trends Microbiol 7 (1999) 328-333
    • (1999) Trends Microbiol , vol.7 , pp. 328-333
    • McFadden, G.I.1    Roos, D.S.2
  • 3
    • 0344549379 scopus 로고    scopus 로고
    • Nuclear-encoded proteins target to the plastid in Toxoplasma gondii and Plasmodium falciparum
    • Waller R.F., Keeling P.J., Donald R.G.K., et al. Nuclear-encoded proteins target to the plastid in Toxoplasma gondii and Plasmodium falciparum. Proc Natl Acad Sci USA 95 (1998) 12352-12357
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12352-12357
    • Waller, R.F.1    Keeling, P.J.2    Donald, R.G.K.3
  • 4
    • 0034678922 scopus 로고    scopus 로고
    • Protein trafficking to the plastid of Plasmodium falciparum is via the secretory pathway
    • Waller R.F., Reed M.B., Cowman A.F., and McFadden G.I. Protein trafficking to the plastid of Plasmodium falciparum is via the secretory pathway. EMBO J 19 (2000) 1794-1802
    • (2000) EMBO J , vol.19 , pp. 1794-1802
    • Waller, R.F.1    Reed, M.B.2    Cowman, A.F.3    McFadden, G.I.4
  • 5
    • 0035126479 scopus 로고    scopus 로고
    • Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum
    • Surolia N., and Surolia A. Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum. Nat Med 7 (2001) 167-173
    • (2001) Nat Med , vol.7 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 6
    • 0033520336 scopus 로고    scopus 로고
    • Inhibitors of the non-mevalonate pathway of isoprenoid biosynthesis as antimalarial drugs
    • Jomaa H., Wiesner J., Sanderbrand S., et al. Inhibitors of the non-mevalonate pathway of isoprenoid biosynthesis as antimalarial drugs. Science 285 (1999) 1573-1575
    • (1999) Science , vol.285 , pp. 1573-1575
    • Jomaa, H.1    Wiesner, J.2    Sanderbrand, S.3
  • 7
    • 2342520626 scopus 로고    scopus 로고
    • Metabolic maps and functions of the Plasmodium falciparum apicoplast
    • Ralph S.A., van Dooren G.G., Waller R.F., et al. Metabolic maps and functions of the Plasmodium falciparum apicoplast. Nat Microbiol Rev 2 (2004) 203-216
    • (2004) Nat Microbiol Rev , vol.2 , pp. 203-216
    • Ralph, S.A.1    van Dooren, G.G.2    Waller, R.F.3
  • 8
    • 0036230756 scopus 로고    scopus 로고
    • The genome of Plasmodium falciparum encodes an active delta-aminolevulinic acid dehydratase
    • Sato S., and Wilson R.J.M. The genome of Plasmodium falciparum encodes an active delta-aminolevulinic acid dehydratase. Curr Genet 40 (2002) 391-398
    • (2002) Curr Genet , vol.40 , pp. 391-398
    • Sato, S.1    Wilson, R.J.M.2
  • 9
    • 0037189526 scopus 로고    scopus 로고
    • Processing of an apicoplast leader sequence in Plasmodium falciparum, and the identification of a putative leader cleavage enzyme
    • van Dooren G.G., Su V., DiOmbrian M.C., and McFadden G.I. Processing of an apicoplast leader sequence in Plasmodium falciparum, and the identification of a putative leader cleavage enzyme. J Biol Chem 277 (2002) 23612-23619
    • (2002) J Biol Chem , vol.277 , pp. 23612-23619
    • van Dooren, G.G.1    Su, V.2    DiOmbrian, M.C.3    McFadden, G.I.4
  • 10
    • 1342325384 scopus 로고    scopus 로고
    • δ-Aminolevulinic acid dehydrase from Plasmodium falciparum- indigenous vs imported
    • Danasekaran S., Chandra N.R., Sagar K.C., Rangarajan P.N., and Padmanaban G. δ-Aminolevulinic acid dehydrase from Plasmodium falciparum- indigenous vs imported. J Biol Chem 279 (2004) 6934-6942
    • (2004) J Biol Chem , vol.279 , pp. 6934-6942
    • Danasekaran, S.1    Chandra, N.R.2    Sagar, K.C.3    Rangarajan, P.N.4    Padmanaban, G.5
  • 11
    • 1942444611 scopus 로고    scopus 로고
    • Enzymes for heme biosynthesis are found in both the mitochondrion and plastid of the malaria parasite Plasmodium falciparum
    • Sato S., Clough B., Coates L., and Wilson R.J.M. Enzymes for heme biosynthesis are found in both the mitochondrion and plastid of the malaria parasite Plasmodium falciparum. Protist 155 (2004) 117-125
    • (2004) Protist , vol.155 , pp. 117-125
    • Sato, S.1    Clough, B.2    Coates, L.3    Wilson, R.J.M.4
  • 12
  • 13
    • 0029034851 scopus 로고
    • Plasmodium falciparum: alterations in organelle transcript abundance during the erythrocytic cycle
    • Feagin J.E., and Drew M.E. Plasmodium falciparum: alterations in organelle transcript abundance during the erythrocytic cycle. Exp Parasitol 80 (1995) 430-440
    • (1995) Exp Parasitol , vol.80 , pp. 430-440
    • Feagin, J.E.1    Drew, M.E.2
  • 14
    • 0030590259 scopus 로고    scopus 로고
    • Complete gene map of the plastid-like DNA of the malaria parasite Plasmodium falciparum
    • Wilson R.J.M., Denny P.W., Preiser P.R., et al. Complete gene map of the plastid-like DNA of the malaria parasite Plasmodium falciparum. J Mol Biol 261 (1996) 155-172
    • (1996) J Mol Biol , vol.261 , pp. 155-172
    • Wilson, R.J.M.1    Denny, P.W.2    Preiser, P.R.3
  • 15
    • 0033180232 scopus 로고    scopus 로고
    • Antibiotic inhibitors of organelle protein synthesis in Plasmodium falciparum
    • Clough B., Rangachari K., Strath M., Preiser P.R., and Wilson R.J.M. Antibiotic inhibitors of organelle protein synthesis in Plasmodium falciparum. Protist 150 (1999) 189-195
    • (1999) Protist , vol.150 , pp. 189-195
    • Clough, B.1    Rangachari, K.2    Strath, M.3    Preiser, P.R.4    Wilson, R.J.M.5
  • 16
    • 0033180525 scopus 로고    scopus 로고
    • Protein synthesis in the plastid of Plasmodium falciparum
    • Roy A., Cox R.A., Williamson D.H., and Wilson R.J.M. Protein synthesis in the plastid of Plasmodium falciparum. Protist 150 (1999) 183-188
    • (1999) Protist , vol.150 , pp. 183-188
    • Roy, A.1    Cox, R.A.2    Williamson, D.H.3    Wilson, R.J.M.4
  • 17
    • 16244385594 scopus 로고    scopus 로고
    • The apicoplast of Plasmodium falciparum is translationally active
    • Chaubey S., Kumar A., Singh D., and Habib S. The apicoplast of Plasmodium falciparum is translationally active. Mol Microbiol 56 (2005) 81-89
    • (2005) Mol Microbiol , vol.56 , pp. 81-89
    • Chaubey, S.1    Kumar, A.2    Singh, D.3    Habib, S.4
  • 18
    • 0040982083 scopus 로고    scopus 로고
    • A plastid of probable green algal origin in apicomplexan parasites
    • Kohler S., Delwiche C.F., Denny P.W., et al. A plastid of probable green algal origin in apicomplexan parasites. Science 275 (1997) 1485-1489
    • (1997) Science , vol.275 , pp. 1485-1489
    • Kohler, S.1    Delwiche, C.F.2    Denny, P.W.3
  • 19
    • 0035194239 scopus 로고    scopus 로고
    • Large amounts of apicoplast nucleoid DNA and its segregation in Toxoplasma gondii
    • Matsuzaki M., Kikuchi T., Kojima S., and Koroiwa T. Large amounts of apicoplast nucleoid DNA and its segregation in Toxoplasma gondii. Protoplasma 218 (2001) 180-191
    • (2001) Protoplasma , vol.218 , pp. 180-191
    • Matsuzaki, M.1    Kikuchi, T.2    Kojima, S.3    Koroiwa, T.4
  • 20
    • 0030245576 scopus 로고    scopus 로고
    • Organelle DNAs: the bit players in malaria parasite DNA replication
    • Williamson D.H., Preiser P.R., and Wilson R.J.M. Organelle DNAs: the bit players in malaria parasite DNA replication. Parasitol Today 12 (1996) 357-362
    • (1996) Parasitol Today , vol.12 , pp. 357-362
    • Williamson, D.H.1    Preiser, P.R.2    Wilson, R.J.M.3
  • 21
    • 0031444101 scopus 로고    scopus 로고
    • A plastid organelle as a drug target in apicomplexan parasites
    • Fichera M.E., and Roos D.S. A plastid organelle as a drug target in apicomplexan parasites. Nature 390 (1997) 407-409
    • (1997) Nature , vol.390 , pp. 407-409
    • Fichera, M.E.1    Roos, D.S.2
  • 23
    • 0037241820 scopus 로고    scopus 로고
    • Replication of the Plasmodium falciparum apicoplast DNA initiates within the inverted repeat region
    • Singh D., Chaubey S., and Habib S. Replication of the Plasmodium falciparum apicoplast DNA initiates within the inverted repeat region. Mol Biochem Parasitol 126 (2003) 9-14
    • (2003) Mol Biochem Parasitol , vol.126 , pp. 9-14
    • Singh, D.1    Chaubey, S.2    Habib, S.3
  • 24
    • 11144344532 scopus 로고    scopus 로고
    • Multiple replication origins within the inverted repeat region of the Plasmodium falciparum apicoplast genome are differentially activated
    • Singh D., Kumar A., Raghu Ram E.V.S., and Habib S. Multiple replication origins within the inverted repeat region of the Plasmodium falciparum apicoplast genome are differentially activated. Mol Biochem Parasitol 139 (2005) 99-106
    • (2005) Mol Biochem Parasitol , vol.139 , pp. 99-106
    • Singh, D.1    Kumar, A.2    Raghu Ram, E.V.S.3    Habib, S.4
  • 25
    • 17844368368 scopus 로고    scopus 로고
    • The plastidic DNA replication enzyme complex of Plasmodium falciparum
    • Seow F., Sato S., Janssen C.S., et al. The plastidic DNA replication enzyme complex of Plasmodium falciparum. Mol. Biochem. Parasitol. 141 (2005) 145-153
    • (2005) Mol. Biochem. Parasitol. , vol.141 , pp. 145-153
    • Seow, F.1    Sato, S.2    Janssen, C.S.3
  • 26
    • 0031431683 scopus 로고    scopus 로고
    • Topoisomerase II inhibitors induce cleavage of nuclear and 35 kb plastid DNAs in the malarial parasite Plasmodium falciparum
    • Weissig V., Vetro-Widenhouse T.S., and Rowe T.C. Topoisomerase II inhibitors induce cleavage of nuclear and 35 kb plastid DNAs in the malarial parasite Plasmodium falciparum. DNA Cell Biol. 16 (1997) 1483-1492
    • (1997) DNA Cell Biol. , vol.16 , pp. 1483-1492
    • Weissig, V.1    Vetro-Widenhouse, T.S.2    Rowe, T.C.3
  • 27
    • 0032742420 scopus 로고    scopus 로고
    • Malarial genome comes into view
    • Pennisi E. Malarial genome comes into view. Science 286 (1999) 1263-1265
    • (1999) Science , vol.286 , pp. 1263-1265
    • Pennisi, E.1
  • 28
    • 13444291112 scopus 로고    scopus 로고
    • Expression and characterization of the ATP-binding domain of a malarial Plasmodium vivax gene homologous to the B subunit of the bacterial topopisomerase DNA gyrase
    • Khor V., Yowell C., Dame J.B., and Rowe T.C. Expression and characterization of the ATP-binding domain of a malarial Plasmodium vivax gene homologous to the B subunit of the bacterial topopisomerase DNA gyrase. Mol Biochem Parasitol 140 (2005) 107-117
    • (2005) Mol Biochem Parasitol , vol.140 , pp. 107-117
    • Khor, V.1    Yowell, C.2    Dame, J.B.3    Rowe, T.C.4
  • 29
    • 0017892683 scopus 로고
    • Cultivation of malarial parasites
    • Trager W., and Jensen J.B. Cultivation of malarial parasites. Nature 273 (1978) 621-622
    • (1978) Nature , vol.273 , pp. 621-622
    • Trager, W.1    Jensen, J.B.2
  • 30
    • 0018704491 scopus 로고
    • Synchronization of Plasmodium falciparum erythrocytic stages in culture
    • Lambros C., and Vandenberg J.P. Synchronization of Plasmodium falciparum erythrocytic stages in culture. J Parasitol 65 (1979) 418-420
    • (1979) J Parasitol , vol.65 , pp. 418-420
    • Lambros, C.1    Vandenberg, J.P.2
  • 31
    • 0032078828 scopus 로고    scopus 로고
    • Predicted and observed alleles of Plasmodium falciparum merozoite surface protein-1 (MSP-1), a potential malaria vaccine antigen
    • Qari S.H., Shi Y.-P., Goldman I.F., Nahlen B.L., Tibayrenc, and Lal A.A. Predicted and observed alleles of Plasmodium falciparum merozoite surface protein-1 (MSP-1), a potential malaria vaccine antigen. Mol Biochem Parasitol 92 (1998) 241-252
    • (1998) Mol Biochem Parasitol , vol.92 , pp. 241-252
    • Qari, S.H.1    Shi, Y.-P.2    Goldman, I.F.3    Nahlen, B.L.4    Tibayrenc5    Lal, A.A.6
  • 32
    • 0026015398 scopus 로고
    • Preparative high-yield electroelution of proteins after separation by sodium dodecyl sulphate polyacrylamide gel electrophoresis and its application to analysis of amino acid sequence and to raise antibodies
    • Ohhashi T., Moritani C., Andoh H., et al. Preparative high-yield electroelution of proteins after separation by sodium dodecyl sulphate polyacrylamide gel electrophoresis and its application to analysis of amino acid sequence and to raise antibodies. J Chromatogr 585 (1991) 153-159
    • (1991) J Chromatogr , vol.585 , pp. 153-159
    • Ohhashi, T.1    Moritani, C.2    Andoh, H.3
  • 33
    • 0021267177 scopus 로고
    • Identification, developmental regulation, and response to heat shock of two antigenically related forms of a major nuclear envelope protein in Drosophila embryos: application of an improved method for affinity purification of antibodies using polypeptides immobilised on nitrocellulose blots
    • Smith D.E., and Fisher P.A. Identification, developmental regulation, and response to heat shock of two antigenically related forms of a major nuclear envelope protein in Drosophila embryos: application of an improved method for affinity purification of antibodies using polypeptides immobilised on nitrocellulose blots. J Cell Biol 99 (1984) 20-28
    • (1984) J Cell Biol , vol.99 , pp. 20-28
    • Smith, D.E.1    Fisher, P.A.2
  • 34
    • 0027419771 scopus 로고
    • The 43 kDa N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs
    • Ali J.A., Jackson A.P., Howells A.J., and Maxwell A. The 43 kDa N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs. Biochemistry 32 (1993) 2717-2724
    • (1993) Biochemistry , vol.32 , pp. 2717-2724
    • Ali, J.A.1    Jackson, A.P.2    Howells, A.J.3    Maxwell, A.4
  • 35
    • 3343010591 scopus 로고    scopus 로고
    • Localization of organellar proteins in Plasmodium falciparum using a novel set of transfection vectors and a new immunofluorescence fixation method
    • Tonkin C.J., van Dooren G.G., Spurck T.P., et al. Localization of organellar proteins in Plasmodium falciparum using a novel set of transfection vectors and a new immunofluorescence fixation method. Mol Biochem Parasitol 137 (2004) 13-21
    • (2004) Mol Biochem Parasitol , vol.137 , pp. 13-21
    • Tonkin, C.J.1    van Dooren, G.G.2    Spurck, T.P.3
  • 36
    • 0027968068 scopus 로고
    • ClustalW: Improving the sensitivity of multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.J., and Gibson T.J. ClustalW: Improving the sensitivity of multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.J.2    Gibson, T.J.3
  • 37
    • 0023769808 scopus 로고
    • Structure and energetics of ligand binding to proteins: Escherichia coli dihydtofolate reductase-trimethoprim, a drug receptor system
    • Dauber-Osguthorpe P., Roberts V.A., Osguthorpe D.J., Wolff J., Genest M., and Hagler A.T. Structure and energetics of ligand binding to proteins: Escherichia coli dihydtofolate reductase-trimethoprim, a drug receptor system. Proteins Struct Funct Genet 4 (1988) 31-47
    • (1988) Proteins Struct Funct Genet , vol.4 , pp. 31-47
    • Dauber-Osguthorpe, P.1    Roberts, V.A.2    Osguthorpe, D.J.3    Wolff, J.4    Genest, M.5    Hagler, A.T.6
  • 38
    • 0000243829 scopus 로고
    • Procheck-a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. Procheck-a program to check the stereochemical quality of protein structures. J Appl Cryst 26 (1993) 47-60
    • (1993) J Appl Cryst , vol.26 , pp. 47-60
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 40
    • 0141633042 scopus 로고    scopus 로고
    • Discovery of gene function by expression profiling of the malaria parasite life cycle
    • Le Roch K.G., Zhou Y., Blair P.L., et al. Discovery of gene function by expression profiling of the malaria parasite life cycle. Science 301 (2003) 1503-1508
    • (2003) Science , vol.301 , pp. 1503-1508
    • Le Roch, K.G.1    Zhou, Y.2    Blair, P.L.3
  • 42
    • 0023686315 scopus 로고
    • Activity of fluoroquinolone antibiotics against Plasmodium falciparum in vitro
    • Divo A.A., Sartorelli A.C., Patton C.L., and Bia F.J. Activity of fluoroquinolone antibiotics against Plasmodium falciparum in vitro. Antimicrob Agents Chemother 32 (1988) 1182-1186
    • (1988) Antimicrob Agents Chemother , vol.32 , pp. 1182-1186
    • Divo, A.A.1    Sartorelli, A.C.2    Patton, C.L.3    Bia, F.J.4
  • 43
    • 0019878168 scopus 로고
    • DNA gyrase: affinity chromatography on novobiocin sepharose and catalytic properties
    • Staudenbauer W.L., and Orr E. DNA gyrase: affinity chromatography on novobiocin sepharose and catalytic properties. Nucleic Acids Res 9 (1981) 3589-3603
    • (1981) Nucleic Acids Res , vol.9 , pp. 3589-3603
    • Staudenbauer, W.L.1    Orr, E.2
  • 44
    • 33847266418 scopus 로고    scopus 로고
    • The effects anti-bacterials on the malaria parasite Plasmodium falciparum
    • Goodman C.D., Su V., and McFadden G.I. The effects anti-bacterials on the malaria parasite Plasmodium falciparum. Mol Biochem Parasitol 152 (2007) 181-191
    • (2007) Mol Biochem Parasitol , vol.152 , pp. 181-191
    • Goodman, C.D.1    Su, V.2    McFadden, G.I.3
  • 46
    • 0034737716 scopus 로고    scopus 로고
    • Dimerization of Escherichia coli DNA gyrase B provides a structural mechanism for activating the ATPase catalytic center
    • Brino L., Urzhumtsev A., Mousli M., et al. Dimerization of Escherichia coli DNA gyrase B provides a structural mechanism for activating the ATPase catalytic center. J Biol Chem 275 (2000) 9468-9475
    • (2000) J Biol Chem , vol.275 , pp. 9468-9475
    • Brino, L.1    Urzhumtsev, A.2    Mousli, M.3
  • 47
    • 0025282176 scopus 로고
    • Quinolone resistance-determining region in the DNA gyrase gyrA gene of Escherichia coli
    • Yoshida H., Bogaki M., Nakamura M., and Nakamura S. Quinolone resistance-determining region in the DNA gyrase gyrA gene of Escherichia coli. Antimicrob Agents Chemother 34 (1990) 1271-1272
    • (1990) Antimicrob Agents Chemother , vol.34 , pp. 1271-1272
    • Yoshida, H.1    Bogaki, M.2    Nakamura, M.3    Nakamura, S.4
  • 48
    • 0037416980 scopus 로고    scopus 로고
    • Active-site residues of Escherichia coli DNA gyrase required in coupling ATP hydrolysis to DNA supercoiling and amino acid substitutions leading to novobiocin resistance
    • Gross C.H., Parsons J.D., Grossman T.H., et al. Active-site residues of Escherichia coli DNA gyrase required in coupling ATP hydrolysis to DNA supercoiling and amino acid substitutions leading to novobiocin resistance. Antimicrob Agents Chemother 47 (2003) 1037-1046
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 1037-1046
    • Gross, C.H.1    Parsons, J.D.2    Grossman, T.H.3
  • 49
    • 33750711671 scopus 로고    scopus 로고
    • Abundance of intrinsically unstructured proteins in Plasmodium falciparum and other apicomplexan parasite proteomes
    • Feng Z.-P., Zhang X., Han P., Arora N., Anders R.F., and Norton R.S. Abundance of intrinsically unstructured proteins in Plasmodium falciparum and other apicomplexan parasite proteomes. Mol Biochem Parasitol 150 (2006) 256-267
    • (2006) Mol Biochem Parasitol , vol.150 , pp. 256-267
    • Feng, Z.-P.1    Zhang, X.2    Han, P.3    Arora, N.4    Anders, R.F.5    Norton, R.S.6


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