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Volumn 35, Issue 1, 2004, Pages 46-53

Cloning, expression, and characterization of uracil-DNA glycosylase of Chlamydia pneumoniae in Escherichia coli

Author keywords

Chlamydia pneumoniae; Expression; Purification; Uracil DNA glycosylase

Indexed keywords

CHLAMYDIA; CHLAMYDIA PNEUMONIAE; CHLAMYDOPHILA PNEUMONIAE; ESCHERICHIA COLI;

EID: 10644268702     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2003.12.013     Document Type: Article
Times cited : (13)

References (40)
  • 1
    • 0037090332 scopus 로고    scopus 로고
    • Mechanistic comparisons among base excision repair glycosylases
    • M.L. Dodson, R.S. Lloyd, Mechanistic comparisons among base excision repair glycosylases, Free Radic. Biol. Med. 32 (2002) 678-682.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 678-682
    • Dodson, M.L.1    Lloyd, R.S.2
  • 2
    • 0024278706 scopus 로고
    • Sequence analysis, expression, and conservation of Escherichia coli uracil DNA glycosylase and its gene (ung)
    • U. Varshney, T. Hutcheon, J.H. van de Sande, Sequence analysis, expression, and conservation of Escherichia coli uracil DNA glycosylase and its gene (ung), J. Biol. Chem. 263 (1988) 7776-7784.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7776-7784
    • Varshney, U.1    Hutcheon, T.2    Van De Sande, J.H.3
  • 3
    • 0021717558 scopus 로고
    • Cloning and characterization of the alkA gene of Escherichia coli that encodes 3-methyladenine DNA glycosylase II
    • Y. Nakabeppu, H. Kondo, M. Sekiguchi, Cloning and characterization of the alkA gene of Escherichia coli that encodes 3-methyladenine DNA glycosylase II, J. Biol. Chem. 259 (1984) 13723-13729.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13723-13729
    • Nakabeppu, Y.1    Kondo, H.2    Sekiguchi, M.3
  • 4
    • 0024393445 scopus 로고
    • Purification and characterization of Escherichia coli endonuclease III from the cloned nth gene
    • H. Asahara, P.M. Wistort, J.F. Bank, R.H. Bakerian, R.P. Cunningham, Purification and characterization of Escherichia coli endonuclease III from the cloned nth gene, Biochemistry 28 (1989) 4444-4449.
    • (1989) Biochemistry , vol.28 , pp. 4444-4449
    • Asahara, H.1    Wistort, P.M.2    Bank, J.F.3    Bakerian, R.H.4    Cunningham, R.P.5
  • 5
    • 0034734383 scopus 로고    scopus 로고
    • Structure and function in the uracil-DNA glycosylase superfamily
    • H.P. Laurence, Structure and function in the uracil-DNA glycosylase superfamily, Mutat. Res. 460 (2000) 165-181.
    • (2000) Mutat. Res. , vol.460 , pp. 165-181
    • Laurence, H.P.1
  • 7
    • 0029082577 scopus 로고
    • Herpes simplex virus type 1 (HSV-1) uracil-DNA glycosylase: Functional expression in Escherichia coli, biochemical characterization, and selective inhibition by 6-(p-n-octylanilino) uracil
    • R. Argnani, F. Focher, S. Zucchini, A. Verri, G.E. Wright, S. Spadari, R. Manservigi, Herpes simplex virus type 1 (HSV-1) uracil-DNA glycosylase: functional expression in Escherichia coli, biochemical characterization, and selective inhibition by 6-(p-n-octylanilino) uracil, Virology 211 (1995) 307-311.
    • (1995) Virology , vol.211 , pp. 307-311
    • Argnani, R.1    Focher, F.2    Zucchini, S.3    Verri, A.4    Wright, G.E.5    Spadari, S.6    Manservigi, R.7
  • 8
    • 0024969622 scopus 로고
    • Molecular cloning and primary structure of the uracil-DNA glycosylase gene from Saccharomyces cerevisiae
    • K.J. Percival, M.B. Klein, P.M. Burgers, Molecular cloning and primary structure of the uracil-DNA glycosylase gene from Saccharomyces cerevisiae, J. Biol. Chem. 264 (1989) 2593-2598.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2593-2598
    • Percival, K.J.1    Klein, M.B.2    Burgers, P.M.3
  • 9
    • 0030841051 scopus 로고    scopus 로고
    • Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene
    • H. Nilsen, M. Otterlei, T. Haug, K. Solum, T.A. Nagelhus, F. Skorpen, H.E. Krokan, Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene, Nucleic Acids Res. 25 (1997) 750-755.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 750-755
    • Nilsen, H.1    Otterlei, M.2    Haug, T.3    Solum, K.4    Nagelhus, T.A.5    Skorpen, F.6    Krokan, H.E.7
  • 10
    • 0029805081 scopus 로고    scopus 로고
    • A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase
    • P. Gallinari, J. Jiricny, A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase, Nature 383 (1996) 735-738.
    • (1996) Nature , vol.383 , pp. 735-738
    • Gallinari, P.1    Jiricny, J.2
  • 12
    • 0033602148 scopus 로고    scopus 로고
    • Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors
    • K.A. Haushalter, P.T. Stukenberg, M.W. Kirschner, G.L. Verdine, Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors, Curr. Biol. 9 (1999) 174-185.
    • (1999) Curr. Biol. , vol.9 , pp. 174-185
    • Haushalter, K.A.1    Stukenberg, P.T.2    Kirschner, M.W.3    Verdine, G.L.4
  • 13
    • 0035839610 scopus 로고    scopus 로고
    • Biochemical characterization of uracil processing activities in the hyperthermophilic archaeon Pyrobaculum aerophilum
    • A.A. Sartori, P. Schär, S. Fitz-Gibbon, J.H. Miller, J. Jiricny, Biochemical characterization of uracil processing activities in the hyperthermophilic archaeon Pyrobaculum aerophilum, J. Biol. Chem. 276 (2001) 29979-29986.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29979-29986
    • Sartori, A.A.1    Schär, P.2    Fitz-Gibbon, S.3    Miller, J.H.4    Jiricny, J.5
  • 14
    • 0037124349 scopus 로고    scopus 로고
    • A novel uracil-DNA glycosylase with broad substrate specificity and an unusual active site
    • A.A. Sartori, S. Fitz-Gibbon, H. Yang, J.H. Miller, J. Jiricny, A novel uracil-DNA glycosylase with broad substrate specificity and an unusual active site, EMBO J. 21 (2002) 3182-3191.
    • (2002) EMBO J. , vol.21 , pp. 3182-3191
    • Sartori, A.A.1    Fitz-Gibbon, S.2    Yang, H.3    Miller, J.H.4    Jiricny, J.5
  • 15
    • 0033951180 scopus 로고    scopus 로고
    • Characterization of a thermostable DNA glycosylase specific for U/G and T/G mismatches from the hyperthermophilic archaeon Pyrobaculum aerophilum
    • H. Yang, S. Fitz-Gibbon, E.M. Marcotte, J.H. Tai, E.C. Hyman, J.H. Miller, Characterization of a thermostable DNA glycosylase specific for U/G and T/G mismatches from the hyperthermophilic archaeon Pyrobaculum aerophilum, J. Bacteriol. 182 (2000) 1272-1279.
    • (2000) J. Bacteriol. , vol.182 , pp. 1272-1279
    • Yang, H.1    Fitz-Gibbon, S.2    Marcotte, E.M.3    Tai, J.H.4    Hyman, E.C.5    Miller, J.H.6
  • 16
    • 0033120232 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: Structure and glycosylase mechanism revisited
    • G. Xiao, M. Tordava, J. Jagadeesh, A.C. Droha, J.T. Stivers, G. L. Gilliland, Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited, Proteins 35 (1999) 13-24.
    • (1999) Proteins , vol.35 , pp. 13-24
    • Xiao, G.1    Tordava, M.2    Jagadeesh, J.3    Droha, A.C.4    Stivers, J.T.5    Gilliland, G.L.6
  • 18
    • 0035907352 scopus 로고    scopus 로고
    • The role of leucine 191 of Escherichia coli uracil DNA glycosylase in the formation of a highly stable complex with the substrate mimic, Ugi, and in uracil excision from the synthetic substrates
    • P. Handa, S. Roy, U. Varshney, The role of leucine 191 of Escherichia coli uracil DNA glycosylase in the formation of a highly stable complex with the substrate mimic, Ugi, and in uracil excision from the synthetic substrates, J. Biol. Chem. 276 (2001) 17324-17331.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17324-17331
    • Handa, P.1    Roy, S.2    Varshney, U.3
  • 19
    • 0037100702 scopus 로고    scopus 로고
    • Effects of mutations at tyrosine 66 and asparagine 123 in the active site pocket of Escherichia coli uracil DNA glycosylase on uracil excision from synthetic DNA oligomers: Evidence for the occurrence of long-range interactions between the enzyme and substrate
    • P. Handa, N. Acharya, U. Varshney, Effects of mutations at tyrosine 66 and asparagine 123 in the active site pocket of Escherichia coli uracil DNA glycosylase on uracil excision from synthetic DNA oligomers: evidence for the occurrence of long-range interactions between the enzyme and substrate, Nucleic Acids Res. 30 (2002) 3086-3095.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3086-3095
    • Handa, P.1    Acharya, N.2    Varshney, U.3
  • 20
    • 0028934537 scopus 로고
    • Crystal structure and mutational analysis of human uracil-DNA glycosylase: Structural basis for specificity and catalysis
    • C.D. Mol, A.S. Arvai, G. Slupphaug, B. Kavli, I. Alseth, H.E. Krokan, J.A. Tainer, Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis, Cell 80 (1995) 869-878.
    • (1995) Cell , vol.80 , pp. 869-878
    • Mol, C.D.1    Arvai, A.S.2    Slupphaug, G.3    Kavli, B.4    Alseth, I.5    Krokan, H.E.6    Tainer, J.A.7
  • 21
    • 0029904839 scopus 로고    scopus 로고
    • A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA
    • G. Slupphaug, C.D. Mol, B. Kavli, A.S. Arvai, H.E. Krokan, J.A. Tainer, A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA, Nature 384 (1996) 87-92.
    • (1996) Nature , vol.384 , pp. 87-92
    • Slupphaug, G.1    Mol, C.D.2    Kavli, B.3    Arvai, A.S.4    Krokan, H.E.5    Tainer, J.A.6
  • 22
    • 0028959237 scopus 로고
    • The structural basis of specific base-excision repair by uracil-DNA glycosylase
    • R. Savva, K. McAuley-Hecht, T. Brown, L. Pearl, The structural basis of specific base-excision repair by uracil-DNA glycosylase, Nature 373 (1995) 487-493.
    • (1995) Nature , vol.373 , pp. 487-493
    • Savva, R.1    McAuley-Hecht, K.2    Brown, T.3    Pearl, L.4
  • 23
    • 0030996226 scopus 로고    scopus 로고
    • A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein A
    • T.A. Nagelhus, T. Haug, K.K. Singh, K.F. Keshav, F. Skorpen, M. Otterlei, S. Bharati, T. Lindmo, S. Benichou, R. Benarous, H.E. Krokan, A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein A, J. Biol. Chem. 272 (1997) 6561-6566.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6561-6566
    • Nagelhus, T.A.1    Haug, T.2    Singh, K.K.3    Keshav, K.F.4    Skorpen, F.5    Otterlei, M.6    Bharati, S.7    Lindmo, T.8    Benichou, S.9    Benarous, R.10    Krokan, H.E.11
  • 24
    • 0037151021 scopus 로고    scopus 로고
    • Direct interaction between uracil-DNa glycosylase and a proliferating cell nuclear antigen homolog in the crenarchaeon Pyrobaculum aerophilum
    • H. Yang, J.H. Chiang, S. Fitz-Gibbon, M. Lebel, A.A. Sartori, J. Jiricny, M.M. Slupska, J.H. Miller, Direct interaction between uracil-DNA glycosylase and a proliferating cell nuclear antigen homolog in the crenarchaeon Pyrobaculum aerophilum, J. Biol. Chem. 277 (2002) 22271-22278.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22271-22278
    • Yang, H.1    Chiang, J.H.2    Fitz-Gibbon, S.3    Lebel, M.4    Sartori, A.A.5    Jiricny, J.6    Slupska, M.M.7    Miller, J.H.8
  • 25
    • 0035907374 scopus 로고    scopus 로고
    • Chimeras between single-stranded DNA-binding proteins from Escherichia coli and Mycobacterium tuberculosis reveal that their C-terminal domains interact with uracil DNA glycosylases
    • P. Handa, N. Acharya, U. Varshney, Chimeras between single-stranded DNA-binding proteins from Escherichia coli and Mycobacterium tuberculosis reveal that their C-terminal domains interact with uracil DNA glycosylases, J. Biol. Chem. 276 (2001) 16992-16997.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16992-16997
    • Handa, P.1    Acharya, N.2    Varshney, U.3
  • 26
    • 0026724896 scopus 로고
    • The presence of uracil-DNA glycosylase in insects is dependent upon developmental complexity
    • B. Dudley, A. Hammond, W.A. Deutsch, The presence of uracil-DNA glycosylase in insects is dependent upon developmental complexity, J. Biol. Chem. 267 (1992) 11964-11967.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11964-11967
    • Dudley, B.1    Hammond, A.2    Deutsch, W.A.3
  • 27
    • 0027509159 scopus 로고
    • Cell cycle regulation of a human cyclin-like gene encoding uracil-DNA glycosylase
    • S.J. Muller, S. Caradonna, Cell cycle regulation of a human cyclin-like gene encoding uracil-DNA glycosylase, J. Biol. Chem. 268 (1993) 1310-1319.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1310-1319
    • Muller, S.J.1    Caradonna, S.2
  • 29
    • 0032902885 scopus 로고    scopus 로고
    • DNA repair enzyme uracil DNA glycosylase is specifically incorporated into human immunodeficiency virus type 1 viral particles through a Vpr-independent mechanism
    • K.E. Willetts, F. Rey, I. Agostini, J.M. Navarro, Y. Baudat, R. Vigne, J. Sire, DNA repair enzyme uracil DNA glycosylase is specifically incorporated into human immunodeficiency virus type 1 viral particles through a Vpr-independent mechanism, J. Virol. 73 (1999) 1682-1688.
    • (1999) J. Virol. , vol.73 , pp. 1682-1688
    • Willetts, K.E.1    Rey, F.2    Agostini, I.3    Navarro, J.M.4    Baudat, Y.5    Vigne, R.6    Sire, J.7
  • 30
    • 0037687289 scopus 로고    scopus 로고
    • Functional role of HIV-1 virion-associated uracil DNA glycosylase 2 in the correction of G:U mispairs to G:C pairs
    • S. Priet, J.M. Navarro, N. Gros, G. Quérat, J. Sire, Functional role of HIV-1 virion-associated uracil DNA glycosylase 2 in the correction of G:U mispairs to G:C pairs, J. Biol. Chem. 278 (2003) 4566-4571.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4566-4571
    • Priet, S.1    Navarro, J.M.2    Gros, N.3    Quérat, G.4    Sire, J.5
  • 31
    • 0023040808 scopus 로고
    • Potential danger to pregnant women of Chlamydia psittaci from sheep
    • D. Buxton, Potential danger to pregnant women of Chlamydia psittaci from sheep, Vet. Rec. 118 (1986) 510-511.
    • (1986) Vet. Rec. , vol.118 , pp. 510-511
    • Buxton, D.1
  • 34
    • 0029775277 scopus 로고    scopus 로고
    • Association of Chlamydia pneumoniae IgA antibodies with recently symptomatic asthma
    • D.L. Hahn, T. Anttila, P. Saikku, Association of Chlamydia pneumoniae IgA antibodies with recently symptomatic asthma, Epidemiol. Infect. 117 (1996) 513-517.
    • (1996) Epidemiol. Infect. , vol.117 , pp. 513-517
    • Hahn, D.L.1    Anttila, T.2    Saikku, P.3
  • 36
  • 40
    • 0033554424 scopus 로고    scopus 로고
    • Role of electrophilic and general base catalysis in the mechanism of Escherichia coli uracil DNA glycosylase
    • A.C. Drohat, J. Jagadeesh, E. Ferguson, J.T. Stivers, Role of electrophilic and general base catalysis in the mechanism of Escherichia coli uracil DNA glycosylase, Biochemistry 38 (1999) 11861-11875.
    • (1999) Biochemistry , vol.38 , pp. 11861-11875
    • Drohat, A.C.1    Jagadeesh, J.2    Ferguson, E.3    Stivers, J.T.4


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