메뉴 건너뛰기




Volumn 8, Issue 9, 2013, Pages

Structure Determination and Biochemical Characterization of a Putative HNH Endonuclease from Geobacter metallireducens GS-15

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; ENDONUCLEASE; ENDONUCLEASE HNH; UNCLASSIFIED DRUG; ZINC;

EID: 84883619709     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0072114     Document Type: Article
Times cited : (11)

References (30)
  • 1
    • 0037146816 scopus 로고    scopus 로고
    • Reduction kinetics of Fe(III), Co(III), U(VI), Cr(VI), and Tc(VII) in cultures of dissimilatory metal-reducing bacteria
    • Liu C, Gorby YA, Zachara JM, Fredrickson JK, Brown CF, (2002) Reduction kinetics of Fe(III), Co(III), U(VI), Cr(VI), and Tc(VII) in cultures of dissimilatory metal-reducing bacteria. Biotechnology and bioengineering 80: 637-649.
    • (2002) Biotechnology and Bioengineering , vol.80 , pp. 637-649
    • Liu, C.1    Gorby, Y.A.2    Zachara, J.M.3    Fredrickson, J.K.4    Brown, C.F.5
  • 2
    • 73249128769 scopus 로고    scopus 로고
    • Hydrogen production by geobacter species and a mixed consortium in a microbial electrolysis cell
    • Call DF, Wagner RC, Logan BE, (2009) Hydrogen production by geobacter species and a mixed consortium in a microbial electrolysis cell. Applied and environmental microbiology 75: 7579-7587.
    • (2009) Applied and Environmental Microbiology , vol.75 , pp. 7579-7587
    • Call, D.F.1    Wagner, R.C.2    Logan, B.E.3
  • 3
    • 0027523571 scopus 로고
    • Geobacter metallireducens gen. nov. sp. nov., a microorganism capable of coupling the complete oxidation of organic compounds to the reduction of iron and other metals
    • Lovley DR, Giovannoni SJ, White DC, Champine JE, Phillips EJ, et al. (1993) Geobacter metallireducens gen. nov. sp. nov., a microorganism capable of coupling the complete oxidation of organic compounds to the reduction of iron and other metals. Archives of microbiology 159: 336-344.
    • (1993) Archives of Microbiology , vol.159 , pp. 336-344
    • Lovley, D.R.1    Giovannoni, S.J.2    White, D.C.3    Champine, J.E.4    Phillips, E.J.5
  • 4
    • 67650590854 scopus 로고    scopus 로고
    • The genome sequence of Geobacter metallireducens: features of metabolism, physiology and regulation common and dissimilar to Geobacter sulfurreducens
    • Aklujkar M, Krushkal J, DiBartolo G, Lapidus A, Land ML, et al. (2009) The genome sequence of Geobacter metallireducens: features of metabolism, physiology and regulation common and dissimilar to Geobacter sulfurreducens. BMC microbiology 9: 109.
    • (2009) BMC Microbiology , vol.9 , pp. 109
    • Aklujkar, M.1    Krushkal, J.2    DiBartolo, G.3    Lapidus, A.4    Land, M.L.5
  • 5
    • 75549086595 scopus 로고    scopus 로고
    • REBASE-a database for DNA restriction and modification: enzymes, genes and genomes
    • Roberts RJ, Vincze T, Posfai J, Macelis D, (2010) REBASE-a database for DNA restriction and modification: enzymes, genes and genomes. Nucleic Acids Res 38: D234-236.
    • (2010) Nucleic Acids Res , vol.38
    • Roberts, R.J.1    Vincze, T.2    Posfai, J.3    Macelis, D.4
  • 7
    • 77956187416 scopus 로고    scopus 로고
    • The high-throughput protein sample production platform of the Northeast Structural Genomics Consortium
    • Xiao R, Anderson S, Aramini J, Belote R, Buchwald WA, et al. (2010) The high-throughput protein sample production platform of the Northeast Structural Genomics Consortium. Journal of structural biology 172: 21-33.
    • (2010) Journal of Structural Biology , vol.172 , pp. 21-33
    • Xiao, R.1    Anderson, S.2    Aramini, J.3    Belote, R.4    Buchwald, W.A.5
  • 8
    • 0030095165 scopus 로고    scopus 로고
    • High-level production of uniformly (1)(5)N- and (1)(3)C-enriched fusion proteins in Escherichia coli
    • Jansson M, Li YC, Jendeberg L, Anderson S, Montelione GT, et al. (1996) High-level production of uniformly (1)(5)N- and (1)(3)C-enriched fusion proteins in Escherichia coli. Journal of biomolecular NMR 7: 131-141.
    • (1996) Journal of Biomolecular NMR , vol.7 , pp. 131-141
    • Jansson, M.1    Li, Y.C.2    Jendeberg, L.3    Anderson, S.4    Montelione, G.T.5
  • 9
    • 0029916726 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of the 9 kDa protein of the mouse signal recognition particle and the selenomethionyl-SRP9
    • Doublie S, Kapp U, Aberg A, Brown K, Strub K, et al. (1996) Crystallization and preliminary X-ray analysis of the 9 kDa protein of the mouse signal recognition particle and the selenomethionyl-SRP9. FEBS letters 384: 219-221.
    • (1996) FEBS Letters , vol.384 , pp. 219-221
    • Doublie, S.1    Kapp, U.2    Aberg, A.3    Brown, K.4    Strub, K.5
  • 10
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray Diffraction Data Collected in Oscillation Mode
    • CW Carter, Jr & R M Sweet, Eds Academic Press (New York)
    • Otwinowski Z, Minor W, (1997) Processing of X-ray Diffraction Data Collected in Oscillation Mode. Methods in Enzymology, Macromolecular Crystallography, part A, CW Carter, Jr & R M Sweet, Eds Academic Press (New York) 276: 307-326.
    • (1997) Methods in Enzymology, Macromolecular Crystallography, Part A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 15
    • 0026754035 scopus 로고
    • A novel, sensitive, and specific assay for abasic sites, the most commonly produced DNA lesion
    • Kubo K, Ide H, Wallace SS, Kow YW, (1992) A novel, sensitive, and specific assay for abasic sites, the most commonly produced DNA lesion. Biochemistry 31: 3703-3708.
    • (1992) Biochemistry , vol.31 , pp. 3703-3708
    • Kubo, K.1    Ide, H.2    Wallace, S.S.3    Kow, Y.W.4
  • 16
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: a tool for multiple protein sequence and structure alignments
    • Pei J, Kim BH, Grishin NV, (2008) PROMALS3D: a tool for multiple protein sequence and structure alignments. Nucleic acids research 36: 2295-2300.
    • (2008) Nucleic Acids Research , vol.36 , pp. 2295-2300
    • Pei, J.1    Kim, B.H.2    Grishin, N.V.3
  • 18
    • 67649888360 scopus 로고    scopus 로고
    • Crystal structure of the beta beta alpha-Me type II restriction endonuclease Hpy99I with target DNA
    • Sokolowska M, Czapinska H, Bochtler M, (2009) Crystal structure of the beta beta alpha-Me type II restriction endonuclease Hpy99I with target DNA. Nucleic Acids Res 37: 3799-3810.
    • (2009) Nucleic Acids Res , vol.37 , pp. 3799-3810
    • Sokolowska, M.1    Czapinska, H.2    Bochtler, M.3
  • 19
    • 34948885722 scopus 로고    scopus 로고
    • Crystal structure of T4 endonuclease VII resolving a Holliday junction
    • Biertumpfel C, Yang W, Suck D, (2007) Crystal structure of T4 endonuclease VII resolving a Holliday junction. Nature 449: 616-620.
    • (2007) Nature , vol.449 , pp. 616-620
    • Biertumpfel, C.1    Yang, W.2    Suck, D.3
  • 20
    • 0042525860 scopus 로고    scopus 로고
    • DNA binding and cleavage by the periplasmic nuclease Vvn: a novel structure with a known active site
    • Li CL, Hor LI, Chang ZF, Tsai LC, Yang WZ, et al. (2003) DNA binding and cleavage by the periplasmic nuclease Vvn: a novel structure with a known active site. The EMBO journal 22: 4014-4025.
    • (2003) The EMBO Journal , vol.22 , pp. 4014-4025
    • Li, C.L.1    Hor, L.I.2    Chang, Z.F.3    Tsai, L.C.4    Yang, W.Z.5
  • 22
    • 77953604755 scopus 로고    scopus 로고
    • Unusual target site disruption by the rare-cutting HNH restriction endonuclease PacI
    • Shen BW, Heiter DF, Chan SH, Wang H, Xu SY, et al. (2010) Unusual target site disruption by the rare-cutting HNH restriction endonuclease PacI. Structure 18: 734-743.
    • (2010) Structure , vol.18 , pp. 734-743
    • Shen, B.W.1    Heiter, D.F.2    Chan, S.H.3    Wang, H.4    Xu, S.Y.5
  • 23
    • 84883613659 scopus 로고    scopus 로고
    • Natural zinc ribbon HNH endonucleases and engineered zinc finger nicking endonuclease
    • Xu SY, Gupta YK (2012) Natural zinc ribbon HNH endonucleases and engineered zinc finger nicking endonuclease. Nucleic acids research.
    • (2012) Nucleic acids research
    • Xu, S.Y.1    Gupta, Y.K.2
  • 24
    • 78650694154 scopus 로고    scopus 로고
    • Cleavage of phosphorothioated DNA and methylated DNA by the type IV restriction endonuclease ScoMcrA
    • Liu G, Ou HY, Wang T, Li L, Tan H, et al. (2010) Cleavage of phosphorothioated DNA and methylated DNA by the type IV restriction endonuclease ScoMcrA. PLoS Genetics 6: e1001253.
    • (2010) PLoS Genetics , vol.6
    • Liu, G.1    Ou, H.Y.2    Wang, T.3    Li, L.4    Tan, H.5
  • 25
    • 4344643339 scopus 로고    scopus 로고
    • Transposon-mediated linker insertion scanning mutagenesis of the Escherichia coli McrA endonuclease
    • Anton BP, Raleigh EA, (2004) Transposon-mediated linker insertion scanning mutagenesis of the Escherichia coli McrA endonuclease. Journal of bacteriology 186: 5699-5707.
    • (2004) Journal of Bacteriology , vol.186 , pp. 5699-5707
    • Anton, B.P.1    Raleigh, E.A.2
  • 26
    • 52949085449 scopus 로고    scopus 로고
    • Cloning, purification and initial characterization of E. coli McrA, a putative 5-methylcytosine-specific nuclease
    • Mulligan EA, Dunn JJ, (2008) Cloning, purification and initial characterization of E. coli McrA, a putative 5-methylcytosine-specific nuclease. Protein expression and purification 62: 98-103.
    • (2008) Protein Expression and Purification , vol.62 , pp. 98-103
    • Mulligan, E.A.1    Dunn, J.J.2
  • 27
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley LA, Sternberg MJ, (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nature protocols 4: 363-371.
    • (2009) Nature Protocols , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 30
    • 84869116787 scopus 로고    scopus 로고
    • Bacillus subtilis hlpB encodes a conserved stand-alone HNH nuclease-like protein that is essential for viability unless the hlpB deletion is accompanied by the deletion of genes encoding the AddAB DNA repair complex
    • Pediaditakis M, Kaufenstein M, Graumann PL, (2012) Bacillus subtilis hlpB encodes a conserved stand-alone HNH nuclease-like protein that is essential for viability unless the hlpB deletion is accompanied by the deletion of genes encoding the AddAB DNA repair complex. Journal of bacteriology 194: 6184-6194.
    • (2012) Journal of Bacteriology , vol.194 , pp. 6184-6194
    • Pediaditakis, M.1    Kaufenstein, M.2    Graumann, P.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.