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Volumn 39, Issue 7, 2011, Pages 2943-2953

Structural insights into catalytic and substrate binding mechanisms of the strategic EndA nuclease from Streptococcus pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; ASPARAGINE; ENDONUCLEASE; ENDONUCLEASE ENDA; GLYCINE; HISTIDINE; LEUCINE; UNCLASSIFIED DRUG;

EID: 79954620932     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq1152     Document Type: Article
Times cited : (33)

References (48)
  • 2
    • 77951092006 scopus 로고    scopus 로고
    • Streptococcus pneumoniae: Epidemiology and risk factors, evolution of antimicrobial resistance, and impact of vaccines
    • Lynch, J.P. 3rd and Zhanel, G.G. (2010) Streptococcus pneumoniae: epidemiology and risk factors, evolution of antimicrobial resistance, and impact of vaccines. Curr. Opin. Pulm. Med., 16, 217-225.
    • (2010) Curr. Opin. Pulm. Med. , vol.16 , pp. 217-225
    • Lynch III, J.P.1    Zhanel, G.G.2
  • 3
    • 0026633235 scopus 로고
    • Pneumococcal disease during HIV infection. Epidemiologic clinical, and immunologic perspectives
    • Janoff, E.N., Breiman, R.F., Daley, C.L. and Hopewell, P.C. (1992) Pneumococcal disease during HIV infection. Epidemiologic, clinical, and immunologic perspectives. Ann. Intern. Med., 117, 314-324.
    • (1992) Ann. Intern. Med. , vol.117 , pp. 314-324
    • Janoff, E.N.1    Breiman, R.F.2    Daley, C.L.3    Hopewell, P.C.4
  • 4
    • 0030829370 scopus 로고    scopus 로고
    • Invasive pneumococcal disease in the immunocompromised host
    • Janoff, E.N. and Rubins, J.B. (1997) Invasive pneumococcal disease in the immunocompromised host. Microb. Drug Resist., 3, 215-232. (Pubitemid 27347255)
    • (1997) Microbial Drug Resistance , vol.3 , Issue.3 , pp. 215-232
    • Janoff, E.N.1    Rubins, J.B.2
  • 5
    • 9744261123 scopus 로고    scopus 로고
    • Pneumococcal vaccines
    • WHO
    • WHO. (2003) Pneumococcal vaccines. Weekly Epidemiological Record, 78, 110 119.
    • (2003) Weekly Epidemiological Record , vol.78 , Issue.110 , pp. 119
  • 6
    • 45249085501 scopus 로고    scopus 로고
    • Invasive pneumococcal disease in HIV seropositive children and adolescents
    • DOI 10.2223/JPED.1762
    • Mattei, S.M., Falleiros-Carvalho, L.H. and Cavalcante, N.J. (2008) Invasive pneumococcal disease in HIV seropositive children and adolescents. J. Pediatr. (Rio J.), 84, 276-280. (Pubitemid 351840296)
    • (2008) Jornal de Pediatria , vol.84 , Issue.3 , pp. 276-280
    • Mattei, S.M.1    Falleiros-Carvalho, L.H.2    Cavalcante, N.J.F.3
  • 7
    • 72149117409 scopus 로고    scopus 로고
    • Acute bacterial meningitis in infants and children
    • Kim, K.S. (2010) Acute bacterial meningitis in infants and children. Lancet Infect. Dis., 10, 32-42.
    • (2010) Lancet Infect. Dis. , vol.10 , pp. 32-42
    • Kim, K.S.1
  • 8
    • 0027465174 scopus 로고
    • Deaths in bacteremic pneumococcal pneumonia: A comparison of two populations - Huntington, WVa, and Stockholm, Sweden
    • Ortqvist, A., Kalin, M., Julander, I. and Mufson, MA. (1993) Deaths in bacteremic pneumococcal pneumonia. A comparison of two populations-Huntington, WVa, and Stockholm, Sweden. Chest, 103, 710-716. (Pubitemid 23086161)
    • (1993) Chest , vol.103 , Issue.3 , pp. 710-716
    • Ortqvist, A.1    Kalin, M.2    Julander, I.3    Mufson, M.A.4
  • 9
    • 1342281657 scopus 로고    scopus 로고
    • The innate immune response to pneumococcal lung infection: The untold story
    • DOI 10.1016/j.it.2003.12.006
    • KadiogluA. and Andrew, P.W. (2004) The innate immune response to pneumococcal lung infection: the untold story. Trends Immunol., 25, 143-149. (Pubitemid 38249488)
    • (2004) Trends in Immunology , vol.25 , Issue.3 , pp. 143-149
    • Kadioglu, A.1    Andrew, P.W.2
  • 11
    • 0000220470 scopus 로고
    • Bactericidal action of histone
    • Hirsch, J.G (1958) Bactericidal action of histone. J. Exp. Med., 108, 925-944.
    • (1958) J. Exp. Med. , vol.108 , pp. 925-944
    • Hirsch, J.G.1
  • 12
    • 0037007656 scopus 로고    scopus 로고
    • Neutrophil elastase targets virulence factors of enterobacteria
    • DOI 10.1038/417091a
    • Weinrauch, Y., Drujan, D., Shapiro, S.D., Weiss, J. and ZychlinskyA. (2002) Neutrophil elastase targets virulence factors of enterobacteria. Nature, 417, 91-94. (Pubitemid 34498822)
    • (2002) Nature , vol.417 , Issue.6884 , pp. 91-94
    • Weinrauch, Y.1    Drujan, D.2    Shapiro, S.D.3    Weiss, J.4    Zychlinsky, A.5
  • 13
    • 0016524794 scopus 로고
    • Identification of a deoxyribonuclease implicated in genetic transformation of Diplococcus pneumoniae
    • Lacks, S., Greenberg, B. and Neuberger, M. (1975) Identification of a deoxyribonuclease implicated in genetic transformation of Diplococcus pneumoniae. J. Bacteriol., 123, 222-232.
    • (1975) J. Bacteriol. , vol.123 , pp. 222-232
    • Lacks, S.1    Greenberg, B.2    Neuberger, M.3
  • 14
    • 0016622399 scopus 로고
    • Membrane location of a deoxyribonuclease implicated in the genetic transformation of Diplococcus pneumoniae
    • Lacks, S. and Neuberger, M. (1975) Membrane location of a deoxyribonuclease implicated in the genetic transformation of Diplococcus pneumoniae. J. Bacteriol., 124, 1321-1329.
    • (1975) J. Bacteriol. , vol.124 , pp. 1321-1329
    • Lacks, S.1    Neuberger, M.2
  • 15
    • 0025315488 scopus 로고
    • Genetic and structural characterization of EndA. A membrane-bound nuclease required for transformation of Streptococcus pneumoniae
    • PuyetA., Greenberg, B. and Lacks, SA. (1990) Genetic and structural characterization of endA. A membrane-bound nuclease required for transformation of Streptococcus pneumoniae. J. Mol. Biol., 213, 727-738. (Pubitemid 20213212)
    • (1990) Journal of Molecular Biology , vol.213 , Issue.4 , pp. 727-738
    • Puyet, A.1    Greenberg, B.2    Lacks, S.A.3
  • 16
    • 0017401236 scopus 로고
    • Nuclease detection in SDS polyacrylamide gel electrophoresis
    • RosenthalA.L. and Lacks, SA. (1977) Nuclease detection in SDS-polyacrylamide gel electrophoresis. Anal. Biochem., 80, 76-90. (Pubitemid 8123718)
    • (1977) Analytical Biochemistry , vol.80 , Issue.1 , pp. 76-90
    • Rosenthal, A.L.1    Lacks, S.A.2
  • 17
    • 0016155830 scopus 로고
    • Role of a deoxyribonuclease in the genetic transformation of Diplococcus pneumoniae
    • Lacks, S., Greenberg, B. and Neuberger, M. (1974) Role of a deoxyribonuclease in the genetic transformation of Diplococcus pneumoniae. Proc Natl Acad. Sci. USA, 71, 2305-2309.
    • (1974) Proc Natl Acad. Sci. USA , vol.71 , pp. 2305-2309
    • Lacks, S.1    Greenberg, B.2    Neuberger, M.3
  • 18
    • 32944482526 scopus 로고    scopus 로고
    • An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellular traps
    • DOI 10.1016/j.cub.2006.01.056, PII S0960982206011079
    • Beiter, K., Wartha, F., Albiger, B., Normark, S., ZychlinskyA. and Henriques-Normark, B. (2006) An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellular traps. Curr. Biol., 16, 401-407. (Pubitemid 43259351)
    • (2006) Current Biology , vol.16 , Issue.4 , pp. 401-407
    • Beiter, K.1    Wartha, F.2    Albiger, B.3    Normark, S.4    Zychlinsky, A.5    Henriques-Normark, B.6
  • 19
    • 32944465559 scopus 로고    scopus 로고
    • DNase expression allows the pathogen group A Streptococcus to escape killing in neutrophil extracellular traps
    • DOI 10.1016/j.cub.2005.12.039, PII S0960982206010219
    • Buchanan, J.T., SimpsonA.J., Aziz, R.K., Liu, GY., Kristian, SA., Kotb, M., Feramisco, J. and Nizet, V. (2006) DNase expression allows the pathogen group A Streptococcus to escape killing in neutrophil extracellular traps. Curr. Biol., 16, 396-400. (Pubitemid 43259350)
    • (2006) Current Biology , vol.16 , Issue.4 , pp. 396-400
    • Buchanan, J.T.1    Simpson, A.J.2    Aziz, R.K.3    Liu, G.Y.4    Kristian, S.A.5    Kotb, M.6    Feramisco, J.7    Nizet, V.8
  • 20
    • 79551485130 scopus 로고    scopus 로고
    • Mutational and biochemical analysis of the DNA-entry nuclease EndA from Streptococcus pneumoniae
    • doi:10.1093/nar/gkq802 [Epub ahead of print, 15 September]
    • Midon, M., Schafer, P., PingoudA., Ghosh, M., MoonA.F., Cuneo, M.J., London, R.E. and Meiss, G (2010) Mutational and biochemical analysis of the DNA-entry nuclease EndA from Streptococcus pneumoniae. Nucleic Acids Res., doi:10.1093/nar/gkq802 [Epub ahead of print, 15 September].
    • (2010) Nucleic Acids Res.
    • Midon, M.1    Schafer, P.2    Pingoud, A.3    Ghosh, M.4    Moon, A.F.5    Cuneo, M.J.6    London, R.E.7    Meiss, G.8
  • 21
    • 0031936811 scopus 로고    scopus 로고
    • Comparative studies of protein crystallization by vapour-diffusion and microbatch techniques
    • DOI 10.1107/S0907444997005374
    • Chayen, N.E. (1998) Comparative studies of protein crystallization by vapour-diffusion and microbatch techniques. Acta Crystallogr. D Biol. Crystallogr., 54, 8-15. (Pubitemid 28111113)
    • (1998) Acta Crystallographica Section D: Biological Crystallography , vol.54 , Issue.1 , pp. 8-15
    • Chayen, N.E.1
  • 22
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol., 276, 307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 23
    • 77951587361 scopus 로고    scopus 로고
    • A synergistic approach to protein crystallization: Combination of a fixed-arm carrier with surface entropy reduction
    • Moon A.F., Mueller GA. Zhong X. Pedersen L.C. (2010) A synergistic approach to protein crystallization: combination of a fixed-arm carrier with surface entropy reduction. Protein Sci. 19; 901-913.
    • (2010) Protein Sci , vol.19 , pp. 901-913
    • Moon, A.F.1    Mueller, G.A.2    Zhong, X.3    Pedersen, L.C.4
  • 27
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, TA., Zou, JY., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A, 47(Pt 2), 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-4680. (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 30
    • 0033560706 scopus 로고    scopus 로고
    • Protein structure and gene cloning of Syncephalastrum racemosum nuclease
    • Ho, H.C. and Liao, T.H. (1999) Protein structure and gene cloning of Syncephalastrum racemosum nuclease. Biochem. J., 339(Pt 2), 261-267.
    • (1999) Biochem. J. , vol.339 , Issue.PART 2 , pp. 261-267
    • Ho, H.C.1    Liao, T.H.2
  • 31
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L. and Rosenstrom, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res., 38(Suppl.), W545-W549.
    • (2010) Nucleic Acids Res. , vol.38 , Issue.SUPPL.
    • Holm, L.1    Rosenstrom, P.2
  • 32
    • 23044476578 scopus 로고    scopus 로고
    • Structural insights into the mechanism of nuclease A, a ββα metal nuclease from Anabaena
    • DOI 10.1074/jbc.M501798200
    • Ghosh, M., Meiss, G, PingoudA., London, R.E. and Pedersen, L.C. (2005) Structural insights into the mechanism of nuclease A, a betabeta alpha metal nuclease from Anabaena. J. Biol. Chem., 280, 27990-27997. (Pubitemid 41076916)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.30 , pp. 27990-27997
    • Ghosh, M.1    Meiss, G.2    Pingoud, A.3    London, R.E.4    Pedersen, L.C.5
  • 33
    • 34247161866 scopus 로고    scopus 로고
    • The nuclease A-inhibitor complex is characterized by a novel metal ion bridge
    • DOI 10.1074/jbc.M605986200
    • Ghosh, M., Meiss, G., Pingoud, A.M., London, R.E. and Pedersen, L.C. (2007) The nuclease A-inhibitor complex is characterized by a novel metal ion bridge. J. Biol. Chem., 282, 5682-5690. (Pubitemid 47093736)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.8 , pp. 5682-5690
    • Ghosh, M.1    Meiss, G.2    Pingoud, A.M.3    London, R.E.4    Pedersen, L.C.5
  • 34
    • 0033591238 scopus 로고    scopus 로고
    • The active site of Serratia endonuclease contains a conserved magnesium-water cluster
    • DOI 10.1006/jmbi.1999.2729
    • Miller, M.D., Cai, J. and Krause, K.L. (1999) The active site of Serratia endonuclease contains a conserved magnesium-water cluster. J. Mol. Biol., 288, 975-987. (Pubitemid 29248646)
    • (1999) Journal of Molecular Biology , vol.288 , Issue.5 , pp. 975-987
    • Miller, M.D.1    Cai, J.2    Krause, K.L.3
  • 36
    • 75349114909 scopus 로고    scopus 로고
    • Crystal structure of the EndoG/EndoGI complex: Mechanism of EndoG inhibition
    • Loll, B., Gebhardt, M., Wahle, E. and MeinhartA. (2009) Crystal structure of the EndoG/EndoGI complex: mechanism of EndoG inhibition. Nucleic Acids Res., 37, 7312-7320.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 7312-7320
    • Loll, B.1    Gebhardt, M.2    Wahle, E.3    Meinhart, A.4
  • 38
    • 0030829154 scopus 로고    scopus 로고
    • Identification and characterization of a catalytic base in bacterial luciferase by chemical rescue of a dark mutant
    • DOI 10.1021/bi9722554
    • Huang, S. and Tu, S.C. (1997) Identification and characterization of a catalytic base in bacterial luciferase by chemical rescue of a dark mutant. Biochemistry, 36, 14609-14615. (Pubitemid 27524380)
    • (1997) Biochemistry , vol.36 , Issue.48 , pp. 14609-14615
    • Huang, S.1    Tu, S.-C.2
  • 39
    • 17544377403 scopus 로고    scopus 로고
    • Rescue of the catalytic activity of an H42A mutant of horseradish peroxidase by exogenous imidazoles
    • DOI 10.1074/jbc.271.25.14891
    • Newmyer, S.L. and de Montellano, P.R. (1996) Rescue of the catalytic activity of an H42A mutant of horseradish peroxidase by exogenous imidazoles. J. Biol. Chem., 271, 14891-14896. (Pubitemid 26197570)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.25 , pp. 14891-14896
    • Newmyer, S.L.1    De Ortiz Montellano, P.R.2
  • 40
    • 0033520066 scopus 로고    scopus 로고
    • (S)-Mandelate dehydrogenase from Pseudomonas putida: Mutations of the catalytic base histidine-274 and chemical rescue of activity
    • Lehoux, I.E. and Mitra, B. (1999) (S)-Mandelate dehydrogenase from Pseudomonas putida: mutations of the catalytic base histidine-274 and chemical rescue of activity. Biochemistry, 38, 9948-9955.
    • (1999) Biochemistry , vol.38 , pp. 9948-9955
    • Lehoux, I.E.1    Mitra, B.2
  • 41
    • 25844477108 scopus 로고    scopus 로고
    • Chemical rescue of I-site cleavage in living cells and in vitro discriminates between the cytomegalovirus protease, assemblin, and its precursor, pUL80a
    • DOI 10.1074/jbc.M506876200
    • McCartney, SA., Brignole, E.J., Kolegraff, K.N., LovelandA.N., Ussin, L.M. and Gibson, W. (2005) Chemical rescue of I-site cleavage in living cells and in vitro discriminates between the cytomegalovirus protease, assemblin, and its precursor, pUL80a. J. Biol. Chem., 280, 33206-33212. (Pubitemid 41397116)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.39 , pp. 33206-33212
    • McCartney, S.A.1    Brignole, E.J.2    Kolegraff, K.N.3    Loveland, A.N.4    Ussin, L.M.5    Gibson, W.6
  • 42
    • 0027414010 scopus 로고
    • Measurement of deoxyribonuclease I activity in human tissues and body fluids by a single radial enzyme-diffusion method
    • Nadano, D., Yasuda, T. and Kishi, K. (1993) Measurement of deoxyribonuclease I activity in human tissues and body fluids by a single radial enzyme-diffusion method. Clin. Chem., 39, 448-452. (Pubitemid 23099010)
    • (1993) Clinical Chemistry , vol.39 , Issue.3 , pp. 448-452
    • Nadano, D.1    Yasuda, T.2    Kishi, K.3
  • 43
    • 0042525860 scopus 로고    scopus 로고
    • DNA binding and cleavage by the periplasmic nuclease Vvn: A novel structure with a known active site
    • DOI 10.1093/emboj/cdg377
    • Li, C.L., Hor, L.I., Chang, Z.F., Tsai, L.C., Yang, W.Z. and Yuan, H.S. (2003) DNA binding and cleavage by the periplasmic nuclease Vvn: a novel structure with a known active site. EMBO J., 22, 4014-4025. (Pubitemid 36975727)
    • (2003) EMBO Journal , vol.22 , Issue.15 , pp. 4014-4025
    • Li, C.-L.1    Hor, L.-I.2    Chang, Z.-F.3    Tsai, L.-C.4    Yang, W.-Z.5    Yuan, H.S.6
  • 44
    • 34047123641 scopus 로고    scopus 로고
    • The Conserved Asparagine in the HNH Motif Serves an Important Structural Role in Metal Finger Endonucleases
    • DOI 10.1016/j.jmb.2007.02.044, PII S0022283607002252
    • Huang, H. and Yuan, H.S. (2007) The conserved asparagine in the HNH motif serves an important structural role in metal finger endonucleases. J. Mol. Biol., 368, 812-821. (Pubitemid 46527620)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.3 , pp. 812-821
    • Huang, H.1    Yuan, H.S.2
  • 45
    • 0020009108 scopus 로고
    • Isoelectric focusing of multiple forms of DNase in thin layers of polyacrylamide gel and detection of enzymatic activity with a zymogram method following separation
    • Kim, H.S. and Liao, T.H. (1982) Isoelectric focusing of multiple forms of DNase in thin layers of polyacrylamide gel and detection of enzymatic activity with a zymogram method following separation. Anal. Biochem., 119, 96-101.
    • (1982) Anal. Biochem. , vol.119 , pp. 96-101
    • Kim, H.S.1    Liao, T.H.2
  • 46
    • 0024316964 scopus 로고
    • Genetic analysis of human deoxyribonuclease I by immunoblotting and the zymogram method following isoelectric focusing
    • DOI 10.1016/0003-2697(89)90175-9
    • Yasuda, T., Mizuta, K., Ikehara, Y. and Kishi, K. (1989) Genetic analysis of human deoxyribonuclease I by immunoblotting and the zymogram method following isoelectric focusing. Anal. Biochem., 183, 84-88. (Pubitemid 20009777)
    • (1989) Analytical Biochemistry , vol.183 , Issue.1 , pp. 84-88
    • Yasuda, T.1    Mizuta, K.2    Ikehara, Y.3    Kishi, K.4
  • 48
    • 36048945922 scopus 로고    scopus 로고
    • ImageJ for microscopy
    • Collins, T.J. (2007) ImageJ for microscopy. Biotechniques, 43, 25-30.
    • (2007) Biotechniques , vol.43 , pp. 25-30
    • Collins, T.J.1


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