메뉴 건너뛰기




Volumn 42, Issue 3, 2014, Pages 1831-1844

Erratum: Efficient DNA ligation in DNA-RNA hybrid helices by Chlorella virus DNA ligase(Nucleic Acids Research (2014) 42: 3 (1831-44) dOI: 10.1093/nar/gkt1032);Efficient DNA ligation in DNA-RNA hybrid helices by Chlorella virus DNA ligase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYTOSINE; GUANINE; MANGANESE; MESSENGER RNA; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; PROTEIN PBCV 1; SINGLE STRANDED DNA; SODIUM CHLORIDE; UNCLASSIFIED DRUG; VIRUS DNA; VIRUS ENZYME; VIRUS RNA;

EID: 84896737012     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku792     Document Type: Erratum
Times cited : (79)

References (53)
  • 1
    • 9944230069 scopus 로고    scopus 로고
    • The polynucleotide ligase and RNA capping enzyme superfamily of covalent nucleotidyltransferases
    • Shuman, S. and Lima, C.D. (2004) The polynucleotide ligase and RNA capping enzyme superfamily of covalent nucleotidyltransferases. Curr. Opin. Struct. Biol., 14, 757-764.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 757-764
    • Shuman, S.1    Lima, C.D.2
  • 3
    • 39149142191 scopus 로고    scopus 로고
    • DNA and RNA ligases: Structural variations and shared mechanisms
    • Pascal, J.M. (2008) DNA and RNA ligases: structural variations and shared mechanisms. Curr. Opin. Struct. Biol., 18, 96-105.
    • (2008) Curr. Opin. Struct. Biol , vol.18 , pp. 96-105
    • Pascal, J.M.1
  • 4
    • 67650538051 scopus 로고    scopus 로고
    • DNA ligases: Progress and prospects
    • Shuman, S. (2009) DNA ligases: progress and prospects. J. Biol. Chem., 284, 17365-17369.
    • (2009) J. Biol. Chem , vol.284 , pp. 17365-17369
    • Shuman, S.1
  • 5
    • 0017903878 scopus 로고
    • T4 polynucleotide ligase catalyzed joining of short synthetic DNA duplexes at basepaired ends
    • Deugau, K.V. and van de Sande, J.H. (1978) T4 polynucleotide ligase catalyzed joining of short synthetic DNA duplexes at basepaired ends. Biochemistry, 17, 723-729.
    • (1978) Biochemistry , vol.17 , pp. 723-729
    • Deugau, K.V.1    Van De Sande, J.H.2
  • 6
    • 0017822995 scopus 로고
    • Use of the T4 polynucleotide ligase in the joining of flush-ended DNA segments generated by restriction endonucleases
    • Sgaramella, V. and Ehrlich, S.D. (1978) Use of the T4 polynucleotide ligase in the joining of flush-ended DNA segments generated by restriction endonucleases. Eur. J. Biochem., 86, 531-537.
    • (1978) Eur. J. Biochem , vol.86 , pp. 531-537
    • Sgaramella, V.1    Ehrlich, S.D.2
  • 7
    • 0020480166 scopus 로고
    • Sealing of gaps in duplex DNA by T4 DNA ligase
    • Nilsson, S.V. and Magnusson, G. (1982) Sealing of gaps in duplex DNA by T4 DNA ligase. Nucleic Acids Res., 10, 1425-1437.
    • (1982) Nucleic Acids Res , vol.10 , pp. 1425-1437
    • Nilsson, S.V.1    Magnusson, G.2
  • 8
    • 0023651476 scopus 로고
    • Nicks 30 or 50 to AP sites or to mispaired bases, and one-nucleotide gaps can be sealed by T4 DNA ligase
    • Goffin, C., Bailly, V. and Verly, W.G. (1987) Nicks 30 or 50 to AP sites or to mispaired bases, and one-nucleotide gaps can be sealed by T4 DNA ligase. Nucleic Acids Res., 15, 8755-8771.
    • (1987) Nucleic Acids Res , vol.15 , pp. 8755-8771
    • Goffin, C.1    Bailly, V.2    Verly, W.G.3
  • 9
    • 0024559478 scopus 로고
    • Specificity of the nick-closing activity of bacteriophage T4 DNA ligase
    • Wu, D.Y. and Wallace, R.B. (1989) Specificity of the nick-closing activity of bacteriophage T4 DNA ligase. Gene, 76, 245-254.
    • (1989) Gene , vol.76 , pp. 245-254
    • Wu, D.Y.1    Wallace, R.B.2
  • 10
    • 0030873236 scopus 로고    scopus 로고
    • Functional characterization of the T4 DNA ligase: A new insight into the mechanism of action
    • Rossi, R., Montecucco, A., Ciarrocchi, G. and Biamonti, G. (1997) Functional characterization of the T4 DNA ligase: a new insight into the mechanism of action. Nucleic Acids Res., 25, 2106-2113.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2106-2113
    • Rossi, R.1    Montecucco, A.2    Ciarrocchi, G.3    Biamonti, G.4
  • 11
    • 0035125009 scopus 로고    scopus 로고
    • Joining of short DNA oligonucleotides with base pair mismatches by T4 DNA ligase
    • Cherepanov, A., Yildirim, E. and de Vries, S. (2001) Joining of short DNA oligonucleotides with base pair mismatches by T4 DNA ligase. J. Biochem., 129, 61-68.
    • (2001) J. Biochem , vol.129 , pp. 61-68
    • Cherepanov, A.1    Yildirim, E.2    De Vries, S.3
  • 12
    • 14744272204 scopus 로고
    • The ligase chain reaction in a PCR world
    • Barany, F. (1991) The ligase chain reaction in a PCR world. PCR Methods Appl., 1, 5-16.
    • (1991) PCR Methods Appl , vol.1 , pp. 5-16
    • Barany, F.1
  • 15
    • 0346158534 scopus 로고    scopus 로고
    • Recent developments in ligase-mediated amplification and detection
    • Cao, W. (2004) Recent developments in ligase-mediated amplification and detection. Trends Biotechnol., 22, 38-44.
    • (2004) Trends Biotechnol , vol.22 , pp. 38-44
    • Cao, W.1
  • 17
    • 0345434243 scopus 로고    scopus 로고
    • Detection of hepatitis C virus RNA using ligationdependent polymerase chain reaction in formalin-fixed paraffinembedded liver tissues
    • Park, Y.N., Abe, K., Li, H., Hsuih, T., Thung, S.N. and Zhang, D.Y. (1996) Detection of hepatitis C virus RNA using ligationdependent polymerase chain reaction in formalin-fixed, paraffinembedded liver tissues. Am. J. Pathol., 149, 1485-1491.
    • (1996) Am. J. Pathol , vol.149 , pp. 1485-1491
    • Park, Y.N.1    Abe, K.2    Li, H.3    Hsuih, T.4    Thung, S.N.5    Zhang, D.Y.6
  • 19
    • 0031810934 scopus 로고    scopus 로고
    • Further study of hepatitis C virus RNA detection in formalinfixed paraffin-embedded liver tissues by ligation-dependent polymerase chain reaction
    • Miyauchi, I., Moriyama, M., Zhang, D.Y. and Abe, K. (1998) Further study of hepatitis C virus RNA detection in formalinfixed, paraffin-embedded liver tissues by ligation-dependent polymerase chain reaction. Pathol. Int., 48, 428-432.
    • (1998) Pathol. Int , vol.48 , pp. 428-432
    • Miyauchi, I.1    Moriyama, M.2    Zhang, D.Y.3    Abe, K.4
  • 20
    • 0034131335 scopus 로고    scopus 로고
    • Joining of RNAs by splinted ligation
    • Moore, M.J. and Query, C.C. (2000) Joining of RNAs by splinted ligation. Methods Enzymol., 317, 109-123.
    • (2000) Methods Enzymol , vol.317 , pp. 109-123
    • Moore, M.J.1    Query, C.C.2
  • 21
    • 0033910579 scopus 로고    scopus 로고
    • Enhanced detection and distinction of RNA by enzymatic probe ligation
    • Nilsson, M., Barbany, G., Antson, D.O., Gertow, K. and Landegren, U. (2000) Enhanced detection and distinction of RNA by enzymatic probe ligation. Nat. Biotechnol., 18, 791-793.
    • (2000) Nat. Biotechnol , vol.18 , pp. 791-793
    • Nilsson, M.1    Barbany, G.2    Antson, D.O.3    Gertow, K.4    Landegren, U.5
  • 24
    • 84864087907 scopus 로고    scopus 로고
    • RASL-seq for massively parallel and quantitative analysis of gene expression
    • Chapter 4, Unit 4.13
    • Li, H., Qiu, J. and Fu, X.D. (2012) RASL-seq for massively parallel and quantitative analysis of gene expression. Curr. Protoc. Mol. Biol., Chapter 4, Unit 4.13 11-19.
    • (2012) Curr Protoc. Mol. Biol , pp. 11-19
    • Li, H.1    Qiu, J.2    Fu, X.D.3
  • 25
    • 33748163981 scopus 로고    scopus 로고
    • A microRNA detection system based on padlock probes and rolling circle amplification
    • Jonstrup, S.P., Koch, J. and Kjems, J. (2006) A microRNA detection system based on padlock probes and rolling circle amplification. RNA, 12, 1747-1752.
    • (2006) RNA , vol.12 , pp. 1747-1752
    • Jonstrup, S.P.1    Koch, J.2    Kjems, J.3
  • 27
    • 33751088560 scopus 로고    scopus 로고
    • A systematic, ligation-based approach to study RNA modifications
    • Saikia, M., Dai, Q., Decatur, W.A., Fournier, M.J., Piccirilli, J.A. and Pan, T. (2006) A systematic, ligation-based approach to study RNA modifications. RNA, 12, 2025-2033.
    • (2006) RNA , vol.12 , pp. 2025-2033
    • Saikia, M.1    Dai, Q.2    Decatur, W.A.3    Fournier, M.J.4    Piccirilli, J.A.5    Pan, T.6
  • 29
    • 43049167529 scopus 로고    scopus 로고
    • RNA-templated single-base mutation detection based on T4 DNA ligase and reverse molecular beacon
    • Tang, H., Yang, X., Wang, K., Tan, W., Li, H., He, L. and Liu, B. (2008) RNA-templated single-base mutation detection based on T4 DNA ligase and reverse molecular beacon. Talanta, 75, 1388-1393.
    • (2008) Talanta , vol.75 , pp. 1388-1393
    • Tang, H.1    Yang, X.2    Wang, K.3    Tan, W.4    Li, H.5    He, L.6    Liu, B.7
  • 30
    • 0014850334 scopus 로고
    • Polynucleotide ligase-catalyzed joining of deoxyribooligonucleotides on ribopolynucleotide templates and of ribo-oligonucleotides on deoxyribopolynucleotide templates
    • Kleppe, K., Van de Sande, J.H. and Khorana, H.G. (1970) Polynucleotide ligase-catalyzed joining of deoxyribooligonucleotides on ribopolynucleotide templates and of ribo-oligonucleotides on deoxyribopolynucleotide templates. Proc. Natl Acad. Sci. USA, 67, 68-73.
    • (1970) Proc. Natl Acad. Sci. USA , vol.67 , pp. 68-73
    • Kleppe, K.1    Van De Sande, J.H.2    Khorana, H.G.3
  • 31
    • 0015239170 scopus 로고
    • Enzymatic breakage and joining of deoxyribonucleic acid 8. Hybrids of ribo-And deoxyribonucleotide homopolymers as substrates for polynucleotide ligase of bacteriophage T4
    • Fareed, G.C., Wilt, E.M. and Richardson, C.C. (1971) Enzymatic breakage and joining of deoxyribonucleic acid. 8. Hybrids of ribo-And deoxyribonucleotide homopolymers as substrates for polynucleotide ligase of bacteriophage T4. J. Biol. Chem., 246, 925-932.
    • (1971) J. Biol. Chem , vol.246 , pp. 925-932
    • Fareed, G.C.1    Wilt, E.M.2    Richardson, C.C.3
  • 32
    • 0030767872 scopus 로고    scopus 로고
    • Ligation of RNA-containing duplexes by vaccinia DNA ligase
    • Sekiguchi, J. and Shuman, S. (1997) Ligation of RNA-containing duplexes by vaccinia DNA ligase. Biochemistry, 36, 9073-9079.
    • (1997) Biochemistry , vol.36 , pp. 9073-9079
    • Sekiguchi, J.1    Shuman, S.2
  • 33
    • 0032145356 scopus 로고    scopus 로고
    • Specificity and fidelity of strand joining by Chlorella virus DNA ligase
    • Sriskanda, V. and Shuman, S. (1998) Specificity and fidelity of strand joining by Chlorella virus DNA ligase. Nucleic Acids Res., 26, 3536-3541.
    • (1998) Nucleic Acids Res , vol.26 , pp. 3536-3541
    • Sriskanda, V.1    Shuman, S.2
  • 34
    • 3843051369 scopus 로고    scopus 로고
    • RNA substrate specificity and structure-guided mutational analysis of bacteriophage T4 RNA ligase 2
    • Nandakumar, J., Ho, C.K., Lima, C.D. and Shuman, S. (2004) RNA substrate specificity and structure-guided mutational analysis of bacteriophage T4 RNA ligase 2. J. Biol. Chem., 279, 31337-31347.
    • (2004) J. Biol. Chem , vol.279 , pp. 31337-31347
    • Nandakumar, J.1    Ho, C.K.2    Lima, C.D.3    Shuman, S.4
  • 35
    • 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, C.L., Rock, D.L., Barany, F. and Cao, W. (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    Rock, D.L.6    Barany, F.7    Cao, W.8
  • 36
    • 33747177904 scopus 로고    scopus 로고
    • Direct comparison of nickjoining activity of the nucleic acid ligases from bacteriophage T4
    • Bullard, D.R. and Bowater, R.P. (2006) Direct comparison of nickjoining activity of the nucleic acid ligases from bacteriophage T4. Biochem. J., 398, 135-144.
    • (2006) Biochem. J , vol.398 , pp. 135-144
    • Bullard, D.R.1    Bowater, R.P.2
  • 37
    • 0015239823 scopus 로고
    • Enzymatic breakage and joining of deoxyribonucleic acid. IX. Synthesis and properties of the deoxyribonucleic acid adenylate in the phage T4 ligase reaction
    • Harvey, C.L., Gabriel, T.F., Wilt, E.M. and Richardson, C.C. (1971) Enzymatic breakage and joining of deoxyribonucleic acid. IX. Synthesis and properties of the deoxyribonucleic acid adenylate in the phage T4 ligase reaction. J. Biol. Chem., 246, 4523-4530.
    • (1971) J. Biol. Chem , vol.246 , pp. 4523-4530
    • Harvey, C.L.1    Gabriel, T.F.2    Wilt, E.M.3    Richardson, C.C.4
  • 38
    • 83755171561 scopus 로고    scopus 로고
    • Kinetic characterization of single strand break ligation in duplex DNA by T4 DNA ligase
    • Lohman, G.J., Chen, L. and Evans, T.C. Jr (2011) Kinetic characterization of single strand break ligation in duplex DNA by T4 DNA ligase. J. Biol. Chem., 286, 44187-44196.
    • (2011) J. Biol. Chem , vol.286 , pp. 44187-44196
    • Lohman, G.J.1    Chen, L.2    Evans Jr., T.C.3
  • 39
    • 9644289536 scopus 로고    scopus 로고
    • Human DNA ligase i completely encircles and partially unwinds nicked DNA
    • Pascal, J.M., OBrien, P.J., Tomkinson, A.E. and Ellenberger, T. (2004) Human DNA ligase I completely encircles and partially unwinds nicked DNA. Nature, 432, 473-478.
    • (2004) Nature , vol.432 , pp. 473-478
    • Pascal, J.M.1    Obrien, P.J.2    Tomkinson, A.E.3    Ellenberger, T.4
  • 41
    • 34247279304 scopus 로고    scopus 로고
    • Last stop on the road to repair: Structure of E coli DNA ligase bound to nicked DNA-Adenylate
    • Nandakumar, J., Nair, P.A. and Shuman, S. (2007) Last stop on the road to repair: structure of E. coli DNA ligase bound to nicked DNA-Adenylate. Mol. Cell, 26, 257-271.
    • (2007) Mol. Cell , vol.26 , pp. 257-271
    • Nandakumar, J.1    Nair, P.A.2    Shuman, S.3
  • 42
    • 0032518177 scopus 로고    scopus 로고
    • Chlorella virus DNA ligase: Nick recognition and mutational analysis
    • Sriskanda, V. and Shuman, S. (1998) Chlorella virus DNA ligase: nick recognition and mutational analysis. Nucleic Acids Res., 26, 525-531.
    • (1998) Nucleic Acids Res , vol.26 , pp. 525-531
    • Sriskanda, V.1    Shuman, S.2
  • 43
    • 0031054449 scopus 로고    scopus 로고
    • Characterization of an ATP-dependent DNA ligase encoded by Chlorella virus PBCV-1
    • Ho, C.K., Van Etten, J.L. and Shuman, S. (1997) Characterization of an ATP-dependent DNA ligase encoded by Chlorella virus PBCV-1. J. Virol., 71, 1931-1937.
    • (1997) J. Virol , vol.71 , pp. 1931-1937
    • Ho, C.K.1    Van Etten, J.L.2    Shuman, S.3
  • 44
    • 0032531971 scopus 로고    scopus 로고
    • Mutational analysis of Chlorella virus DNA ligase: Catalytic roles of domain i and motif VI
    • Sriskanda, V. and Shuman, S. (1998) Mutational analysis of Chlorella virus DNA ligase: catalytic roles of domain I and motif VI. Nucleic Acids Res., 26, 4618-4625.
    • (1998) Nucleic Acids Res , vol.26 , pp. 4618-4625
    • Sriskanda, V.1    Shuman, S.2
  • 45
    • 0033553405 scopus 로고    scopus 로고
    • Footprinting of Chlorella virus DNA ligase bound at a nick in duplex DNA
    • Odell, M. and Shuman, S. (1999) Footprinting of Chlorella virus DNA ligase bound at a nick in duplex DNA. J. Biol. Chem., 274, 14032-14039.
    • (1999) J. Biol. Chem , vol.274 , pp. 14032-14039
    • Odell, M.1    Shuman, S.2
  • 46
    • 0037082434 scopus 로고    scopus 로고
    • Role of nucleotidyltransferase motifs I, III and IV in the catalysis of phosphodiester bond formation by Chlorella virus DNA ligase
    • Sriskanda, V. and Shuman, S. (2002) Role of nucleotidyltransferase motifs I, III and IV in the catalysis of phosphodiester bond formation by Chlorella virus DNA ligase. Nucleic Acids Res., 30, 903-911.
    • (2002) Nucleic Acids Res , vol.30 , pp. 903-911
    • Sriskanda, V.1    Shuman, S.2
  • 47
    • 0037155931 scopus 로고    scopus 로고
    • Role of nucleotidyl transferase motif v in strand joining by chlorella virus DNA ligase
    • Sriskanda, V. and Shuman, S. (2002) Role of nucleotidyl transferase motif V in strand joining by chlorella virus DNA ligase. J. Biol. Chem., 277, 9661-9667.
    • (2002) J. Biol. Chem , vol.277 , pp. 9661-9667
    • Sriskanda, V.1    Shuman, S.2
  • 48
    • 0345306347 scopus 로고    scopus 로고
    • Analysis of the DNA joining repertoire of Chlorella virus DNA ligase and a new crystal structure of the ligase-Adenylate intermediate
    • Odell, M., Malinina, L., Sriskanda, V., Teplova, M. and Shuman, S. (2003) Analysis of the DNA joining repertoire of Chlorella virus DNA ligase and a new crystal structure of the ligase-Adenylate intermediate. Nucleic Acids Res., 31, 5090-5100.
    • (2003) Nucleic Acids Res , vol.31 , pp. 5090-5100
    • Odell, M.1    Malinina, L.2    Sriskanda, V.3    Teplova, M.4    Shuman, S.5
  • 49
    • 73149118018 scopus 로고    scopus 로고
    • Solution NMR studies of Chlorella virus DNA ligase-Adenylate
    • Piserchio, A., Nair, P.A., Shuman, S. and Ghose, R. (2010) Solution NMR studies of Chlorella virus DNA ligase-Adenylate. J. Mol. Biol., 395, 291-308.
    • (2010) J. Mol. Biol , vol.395 , pp. 291-308
    • Piserchio, A.1    Nair, P.A.2    Shuman, S.3    Ghose, R.4
  • 50
    • 79959358971 scopus 로고    scopus 로고
    • Structure-function analysis of the OB and latch domains of Chlorella virus DNA ligase
    • Samai, P. and Shuman, S. (2011) Structure-function analysis of the OB and latch domains of Chlorella virus DNA ligase. J. Biol. Chem., 286, 22642-22652.
    • (2011) J. Biol. Chem , vol.286 , pp. 22642-22652
    • Samai, P.1    Shuman, S.2
  • 51
    • 79953879420 scopus 로고    scopus 로고
    • Functional dissection of the DNA interface of the nucleotidyltransferase domain of Chlorella virus DNA ligase
    • Samai, P. and Shuman, S. (2011) Functional dissection of the DNA interface of the nucleotidyltransferase domain of Chlorella virus DNA ligase. J. Biol. Chem., 286, 13314-13326.
    • (2011) J. Biol. Chem , vol.286 , pp. 13314-13326
    • Samai, P.1    Shuman, S.2
  • 52
    • 84865208997 scopus 로고    scopus 로고
    • Kinetic analysis of DNA strand joining by Chlorella virus DNA ligase and the role of nucleotidyltransferase motif VI in ligase adenylylation
    • Samai, P. and Shuman, S. (2012) Kinetic analysis of DNA strand joining by Chlorella virus DNA ligase and the role of nucleotidyltransferase motif VI in ligase adenylylation. J. Biol. Chem., 287, 28609-28618.
    • (2012) J. Biol. Chem , vol.287 , pp. 28609-28618
    • Samai, P.1    Shuman, S.2
  • 53
    • 0014413975 scopus 로고
    • Enzymic joining of polynucleotides 3 the polydeoxyadenylate- polydeoxythymidylate homopolymer pair
    • Olivera, B.M. and Lehman, I.R. (1968) Enzymic joining of polynucleotides. 3. The polydeoxyadenylate-polydeoxythymidylate homopolymer pair. J. Mol. Biol., 36, 261-274.
    • (1968) J. Mol. Biol , vol.36 , pp. 261-274
    • Olivera, B.M.1    Lehman, I.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.