메뉴 건너뛰기




Volumn 7, Issue 7, 2012, Pages

Molecular characterization of NAD+-dependent DNA ligase from Wolbachia endosymbiont of lymphatic filarial parasite Brugia malayi

Author keywords

[No Author keywords available]

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE DEPENDENT DNA LIGASE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; ZINC BINDING PROTEIN;

EID: 84864003594     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0041113     Document Type: Article
Times cited : (12)

References (35)
  • 1
    • 0037388065 scopus 로고    scopus 로고
    • Doxycycline in the treatment of human onchocerciasis: kinetics of Wolbachia endobacteria reduction and of inhibition of embryogenesis in female Onchocerca worms
    • Hoerauf A, Mand S, Volkmann L, Büttner M, Debrekyei YM, et al. (2003) Doxycycline in the treatment of human onchocerciasis: kinetics of Wolbachia endobacteria reduction and of inhibition of embryogenesis in female Onchocerca worms. Microbes Infect 5: 261-273.
    • (2003) Microbes Infect , vol.5 , pp. 261-273
    • Hoerauf, A.1    Mand, S.2    Volkmann, L.3    Büttner, M.4    Debrekyei, Y.M.5
  • 2
    • 0035212089 scopus 로고    scopus 로고
    • A new approach to the treatment of filariasis
    • Taylor MJ, Hoerauf A, (2001) A new approach to the treatment of filariasis. Curr Op Infect Dis 14: 727-731.
    • (2001) Curr Op Infect Dis , vol.14 , pp. 727-731
    • Taylor, M.J.1    Hoerauf, A.2
  • 3
    • 21144432943 scopus 로고    scopus 로고
    • The Wolbachia Genome of Brugia malayi: Endosymbiont Evolution within a Human Pathogenic Nematode
    • Foster J, Ganatra M, Kamal I, Ware J, Makarova K, et al. (2005) The Wolbachia Genome of Brugia malayi: Endosymbiont Evolution within a Human Pathogenic Nematode. PLoS Biol 3: 0599-0614.
    • (2005) PLoS Biol , vol.3 , pp. 0599-0614
    • Foster, J.1    Ganatra, M.2    Kamal, I.3    Ware, J.4    Makarova, K.5
  • 5
    • 0015836893 scopus 로고
    • Genetics and function of DNA ligase in Escherichia coli
    • Gottesman MM, Hicks ML, Gellert M, (1973) Genetics and function of DNA ligase in Escherichia coli. J Mol Biol 77: 531-547.
    • (1973) J Mol Biol , vol.77 , pp. 531-547
    • Gottesman, M.M.1    Hicks, M.L.2    Gellert, M.3
  • 6
    • 0031972353 scopus 로고    scopus 로고
    • Structure and function of mammalian DNA ligases
    • Tomkinson AE, Mackey ZB, (1998) Structure and function of mammalian DNA ligases. Mutat Res 407: 1-9.
    • (1998) Mutat Res , vol.407 , pp. 1-9
    • Tomkinson, A.E.1    Mackey, Z.B.2
  • 7
    • 0016273515 scopus 로고
    • DNA ligase: Structure, mechanism and function
    • Lehman IR, (1974) DNA ligase: Structure, mechanism and function. Science 186: 790-797.
    • (1974) Science , vol.186 , pp. 790-797
    • Lehman, I.R.1
  • 8
    • 0034327406 scopus 로고    scopus 로고
    • Structural and mechanistic conservation in DNA ligases
    • Doherty AJ, Suh SW, (2000) Structural and mechanistic conservation in DNA ligases. Nucleic Acids Res 28: 4051-4058.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4051-4058
    • Doherty, A.J.1    Suh, S.W.2
  • 10
    • 24044548989 scopus 로고    scopus 로고
    • NAD+-dependent DNA Ligase (Rv3014c) from Mycobacterium tuberculosis. Crystal Structure of the adenylation domain and identification of novel inhibitors
    • Srivastava SK, Tripathi RP, Ramachandran R, (2005) NAD+-dependent DNA Ligase (Rv3014c) from Mycobacterium tuberculosis. Crystal Structure of the adenylation domain and identification of novel inhibitors. J Biol Chem 280: 30273-30281.
    • (2005) J Biol Chem , vol.280 , pp. 30273-30281
    • Srivastava, S.K.1    Tripathi, R.P.2    Ramachandran, R.3
  • 12
    • 0035965270 scopus 로고    scopus 로고
    • NAD+-dependent DNA Ligase Encoded by a Eukaryotic Virus
    • Sriskanda V, Moyer RW, Shuman S, (2001) NAD+-dependent DNA Ligase Encoded by a Eukaryotic Virus. J Biol Chem 276: 36100-36109.
    • (2001) J Biol Chem , vol.276 , pp. 36100-36109
    • Sriskanda, V.1    Moyer, R.W.2    Shuman, S.3
  • 13
    • 0035040993 scopus 로고    scopus 로고
    • Cloning and functional characterization of an NAD(+)-dependent DNA ligase from Staphylococcus aureus
    • Kaczmarek FS, Zaniewski RP, Gootz TD, Danley DE, Mansour MN, (2001) Cloning and functional characterization of an NAD(+)-dependent DNA ligase from Staphylococcus aureus. J Bacteriol 183: 3016-3024.
    • (2001) J Bacteriol , vol.183 , pp. 3016-3024
    • Kaczmarek, F.S.1    Zaniewski, R.P.2    Gootz, T.D.3    Danley, D.E.4    Mansour, M.N.5
  • 14
  • 15
    • 0034424041 scopus 로고    scopus 로고
    • The NAD-dependent ligase encoded by yerG is an essential gene of Bacillus subtilis
    • Petit MA, Ehrlich SD, (2000) The NAD-dependent ligase encoded by yerG is an essential gene of Bacillus subtilis. Nucleic Acids Res 28: 4642-4648.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4642-4648
    • Petit, M.A.1    Ehrlich, S.D.2
  • 16
    • 34547637078 scopus 로고    scopus 로고
    • Evaluation of NAD+-Dependent DNA Ligase of Mycobacteria as a Potential Target for antibiotics
    • Machala MK, Rychta E, Brzostek A, Sayer HR, Galewicz AR, et al. (2007) Evaluation of NAD+-Dependent DNA Ligase of Mycobacteria as a Potential Target for antibiotics. Antimicrob Agents Chemother 51: 2888-2897.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 2888-2897
    • Machala, M.K.1    Rychta, E.2    Brzostek, A.3    Sayer, H.R.4    Galewicz, A.R.5
  • 17
    • 67649118279 scopus 로고    scopus 로고
    • The α-proteobacteria: The Darwin finches of the bacterial world
    • Ettema TJ, Andersson SG, (2009) The α-proteobacteria: The Darwin finches of the bacterial world. Biol Lett 5: 429-432.
    • (2009) Biol Lett , vol.5 , pp. 429-432
    • Ettema, T.J.1    Andersson, S.G.2
  • 18
    • 19844378240 scopus 로고    scopus 로고
    • Protein signatures distinctive of alpha proteobacteria and its subgroups and a model for α-proteobacterial evolution
    • Gupta RS, (2005) Protein signatures distinctive of alpha proteobacteria and its subgroups and a model for α-proteobacterial evolution. Crit Rev Microbiol 31: 101-135.
    • (2005) Crit Rev Microbiol , vol.31 , pp. 101-135
    • Gupta, R.S.1
  • 19
    • 0035870144 scopus 로고    scopus 로고
    • Mutational analyses of Aquifex pyrophilus DNA ligase define essential domains for self-adenylation and DNA binding activity
    • Lim JH, Choi J, Kim W, Ahn BY, Han YS, (2001) Mutational analyses of Aquifex pyrophilus DNA ligase define essential domains for self-adenylation and DNA binding activity. Arch Biochem Biophys 388: 253-260.
    • (2001) Arch Biochem Biophys , vol.388 , pp. 253-260
    • Lim, J.H.1    Choi, J.2    Kim, W.3    Ahn, B.Y.4    Han, Y.S.5
  • 20
    • 3242806042 scopus 로고    scopus 로고
    • Mutational analyses of the thermostable NAD(+)-dependent DNA ligase from Thermus filiformis
    • Jeon HJ, Shin HJ, Choi JJ, Hoe HS, Kim SK, et al. (2004) Mutational analyses of the thermostable NAD(+)-dependent DNA ligase from Thermus filiformis. FEMS Microbiol Lett 237: 111-118.
    • (2004) FEMS Microbiol Lett , vol.237 , pp. 111-118
    • Jeon, H.J.1    Shin, H.J.2    Choi, J.J.3    Hoe, H.S.4    Kim, S.K.5
  • 21
    • 0031046294 scopus 로고    scopus 로고
    • A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins
    • Bork P, Hofmann K, Andrew P, Neuwald F, Altschul SF, et al. (1997) A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins. FASEB J 11: 68-76.
    • (1997) FASEB J , vol.11 , pp. 68-76
    • Bork, P.1    Hofmann, K.2    Andrew, P.3    Neuwald, F.4    Altschul, S.F.5
  • 22
    • 0033946342 scopus 로고    scopus 로고
    • A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures
    • Georlette D, JoÂnsson ZO, Petegem FV, Chessa JP, Beeumen JV, et al. (2000) A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures. Eur J Biochem 267: 3502-3512.
    • (2000) Eur J Biochem , vol.267 , pp. 3502-3512
    • Georlette, D.1    JoÂnsson, Z.O.2    Petegem, F.V.3    Chessa, J.P.4    Beeumen, J.V.5
  • 24
    • 0141994876 scopus 로고    scopus 로고
    • Specific and Potent Inhibition of NAD+-dependent DNA Ligase by Pyridochromanones
    • Brötz-Oesterhelt H, Knezevic I, Bartel S, Lampe T, Warnecke-Eberz U, et al. (2003) Specific and Potent Inhibition of NAD+-dependent DNA Ligase by Pyridochromanones. J Biol Chem 278: 39435-39442.
    • (2003) J Biol Chem , vol.278 , pp. 39435-39442
    • Brötz-Oesterhelt, H.1    Knezevic, I.2    Bartel, S.3    Lampe, T.4    Warnecke-Eberz, U.5
  • 25
    • 4344576453 scopus 로고    scopus 로고
    • Unique ligation properties of eukaryotic NAD+-dependent DNA ligase from Melanoplus sanguinipes entomopoxvirus
    • Lu J, Tong J, Feng H, Huang J, Afonso CL, et al. (2004) Unique ligation properties of eukaryotic NAD+-dependent DNA ligase from Melanoplus sanguinipes entomopoxvirus. Biochim Biophys Acta 1701: 37- 48.
    • (2004) Biochim Biophys Acta , vol.1701 , pp. 37-48
    • Lu, J.1    Tong, J.2    Feng, H.3    Huang, J.4    Afonso, C.L.5
  • 26
    • 26444603875 scopus 로고    scopus 로고
    • Characterization of a Thermophilic ATP-Dependent DNA Ligase from the Euryarchaeon Pyrococcus horikoshii
    • Keppetipola N, Shuman S, (2005) Characterization of a Thermophilic ATP-Dependent DNA Ligase from the Euryarchaeon Pyrococcus horikoshii. J Bacteriol 187: 6902-6908.
    • (2005) J Bacteriol , vol.187 , pp. 6902-6908
    • Keppetipola, N.1    Shuman, S.2
  • 27
    • 33846383445 scopus 로고    scopus 로고
    • Cloning and expression of a DNA ligase from the hyperthermophilic archaeon Staphylothermus marinus and properties of the enzyme
    • Seo MS, Kim YJ, Choi JJ, Lee MS, Kim JH, et al. (2007) Cloning and expression of a DNA ligase from the hyperthermophilic archaeon Staphylothermus marinus and properties of the enzyme. J Biotechnol 128: 519-530.
    • (2007) J Biotechnol , vol.128 , pp. 519-530
    • Seo, M.S.1    Kim, Y.J.2    Choi, J.J.3    Lee, M.S.4    Kim, J.H.5
  • 28
    • 77649259910 scopus 로고    scopus 로고
    • Denaturation and solvent effect on the conformation and fibril formation of TGFBIp
    • Grothe HL, Little MR, Cho AS, Huang AJW, Yuan C, (2009) Denaturation and solvent effect on the conformation and fibril formation of TGFBIp. Mol Vis 15: 2617-2626.
    • (2009) Mol Vis , vol.15 , pp. 2617-2626
    • Grothe, H.L.1    Little, M.R.2    Cho, A.S.3    Huang, A.J.W.4    Yuan, C.5
  • 30
    • 65549156021 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel immunoreactive ATPase/RNAhelicase in human filarial parasite Brugia malayi
    • Singh M, Srivastava KK, Bhattacharya SM, (2009) Molecular cloning and characterization of a novel immunoreactive ATPase/RNAhelicase in human filarial parasite Brugia malayi. Parasitol Res 104: 753-761.
    • (2009) Parasitol Res , vol.104 , pp. 753-761
    • Singh, M.1    Srivastava, K.K.2    Bhattacharya, S.M.3
  • 31
    • 44349189806 scopus 로고    scopus 로고
    • K2D2: Estimation of protein secondary structure from circular dichroism spectra
    • Perez-Iratxeta C, Andrade-Navarro MA, (2008) K2D2: Estimation of protein secondary structure from circular dichroism spectra. BMC Struct Biol 8: 25.
    • (2008) BMC Struct Biol , vol.8 , pp. 25
    • Perez-Iratxeta, C.1    Andrade-Navarro, M.A.2
  • 32
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modelling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • Bates PA, Kelley LA, MacCallum RM, Sternberg MJ, (2001) Enhancement of protein modelling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM. Proteins 5: 39-46.
    • (2001) Proteins , vol.5 , pp. 39-46
    • Bates, P.A.1    Kelley, L.A.2    MacCallum, R.M.3    Sternberg, M.J.4
  • 34
    • 2442688825 scopus 로고    scopus 로고
    • A non-isotopic method for the determination of activity of the thermostable NAD-dependent DNA ligase from Thermus thermophilus HB8
    • Muerhoff AS, Dawson GJ, Desai SM, (2004) A non-isotopic method for the determination of activity of the thermostable NAD-dependent DNA ligase from Thermus thermophilus HB8. J Virol Methods 119: 171-176.
    • (2004) J Virol Methods , vol.119 , pp. 171-176
    • Muerhoff, A.S.1    Dawson, G.J.2    Desai, S.M.3
  • 35
    • 67349249852 scopus 로고    scopus 로고
    • An endosymbiotic bacterium in a plant-parasitic nematode: Member of a new Wolbachia supergroup
    • Haegeman A, Vanholme B, Jacob J, Vandekerckhove TTM, Claeys M, et al. (2009) An endosymbiotic bacterium in a plant-parasitic nematode: Member of a new Wolbachia supergroup. Int J Parasitol 39: 1045-1054.
    • (2009) Int J Parasitol , vol.39 , pp. 1045-1054
    • Haegeman, A.1    Vanholme, B.2    Jacob, J.3    Vandekerckhove, T.T.M.4    Claeys, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.