메뉴 건너뛰기




Volumn 69, Issue 2, 2010, Pages 226-234

Engineering BspQI nicking enzymes and application of N.BspQI in DNA labeling and production of single-strand DNA

Author keywords

Alanine scanning; CatHI; DNA labeling; Nicking endonuclease; Optical mapping of DNA

Indexed keywords

RESTRICTION ENDONUCLEASE; SINGLE STRANDED DNA;

EID: 70449705894     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2009.09.003     Document Type: Article
Times cited : (27)

References (49)
  • 1
    • 33846078626 scopus 로고    scopus 로고
    • REBASE - enzymes and genes for DNA restriction and modification
    • Roberts R., Vincze T., Posfai J., and Macelis D. REBASE - enzymes and genes for DNA restriction and modification. Nucleic Acids Res. 35 (2007) 269-270
    • (2007) Nucleic Acids Res. , vol.35 , pp. 269-270
    • Roberts, R.1    Vincze, T.2    Posfai, J.3    Macelis, D.4
  • 2
    • 0024297192 scopus 로고
    • A site-specific single strand endonuclease activity induced by NYs-1 virus infection of a Chlorella-like green alga
    • Xia Y., Morgan R., Schildkraut I., and Van Etten J.L. A site-specific single strand endonuclease activity induced by NYs-1 virus infection of a Chlorella-like green alga. Nucleic Acids Res. 16 (1988) 9477-9487
    • (1988) Nucleic Acids Res. , vol.16 , pp. 9477-9487
    • Xia, Y.1    Morgan, R.2    Schildkraut, I.3    Van Etten, J.L.4
  • 3
    • 0032518484 scopus 로고    scopus 로고
    • Chlorella virus NY-2A encodes at least 12 DNA endonuclease/methyltransferase genes
    • Zhang Y., Nelson M., Nietfeldt J., Xia Y., Burbank D., Ropp S., and Van Etten J.L. Chlorella virus NY-2A encodes at least 12 DNA endonuclease/methyltransferase genes. Virology 240 (1998) 366-375
    • (1998) Virology , vol.240 , pp. 366-375
    • Zhang, Y.1    Nelson, M.2    Nietfeldt, J.3    Xia, Y.4    Burbank, D.5    Ropp, S.6    Van Etten, J.L.7
  • 4
    • 0034529393 scopus 로고    scopus 로고
    • Characterization of the specific DNA nicking activity of restriction endonuclease N.BstNBI
    • Morgan R.D., Calvet C., Demeter M., Agra R., and Kong H. Characterization of the specific DNA nicking activity of restriction endonuclease N.BstNBI. Biol. Chem. 381 (2000) 1123-1125
    • (2000) Biol. Chem. , vol.381 , pp. 1123-1125
    • Morgan, R.D.1    Calvet, C.2    Demeter, M.3    Agra, R.4    Kong, H.5
  • 5
    • 34547888748 scopus 로고    scopus 로고
    • Discovery of natural nicking endonucleases Nb.BsrDI and Nb.BtsI and engineering of top-strand nicking variants from BsrDI and BtsI
    • Xu S.-Y., Zhu Z., Zhang P., Chan S.-H., Samuelson J.C., Xiao J., Ingalls D., and Wilson G.G. Discovery of natural nicking endonucleases Nb.BsrDI and Nb.BtsI and engineering of top-strand nicking variants from BsrDI and BtsI. Nucleic Acids Res. 35 (2007) 4608-4618
    • (2007) Nucleic Acids Res. , vol.35 , pp. 4608-4618
    • Xu, S.-Y.1    Zhu, Z.2    Zhang, P.3    Chan, S.-H.4    Samuelson, J.C.5    Xiao, J.6    Ingalls, D.7    Wilson, G.G.8
  • 6
    • 33746224342 scopus 로고    scopus 로고
    • Nickase and a protein encoded by an open reading frame downstream from the nickase BspD6I gene form a restriction endonuclease complex
    • Yunusova A., Rogulin E., Artyukh R., Zheleznaya L., and Matvienko N. Nickase and a protein encoded by an open reading frame downstream from the nickase BspD6I gene form a restriction endonuclease complex. Biochemistry (Mosc) 71 (2007) 815-820
    • (2007) Biochemistry (Mosc) , vol.71 , pp. 815-820
    • Yunusova, A.1    Rogulin, E.2    Artyukh, R.3    Zheleznaya, L.4    Matvienko, N.5
  • 7
    • 33644821134 scopus 로고    scopus 로고
    • Determination and analysis of the primary structure of NM.BstSEI operone from Bacillus stearothermophilus SE-589 which produces N.BstSEI site-specific nickase
    • Golobova N.S., Okhapkina S.S., Abdurashitov M.A., and Degtiarev S. Determination and analysis of the primary structure of NM.BstSEI operone from Bacillus stearothermophilus SE-589 which produces N.BstSEI site-specific nickase. Mol. Biol. (Mosk) 39 (2005) 960-964
    • (2005) Mol. Biol. (Mosk) , vol.39 , pp. 960-964
    • Golobova, N.S.1    Okhapkina, S.S.2    Abdurashitov, M.A.3    Degtiarev, S.4
  • 8
    • 17144415297 scopus 로고    scopus 로고
    • Site-specific DNA-nicking mutants of the heterodimeric restriction endonuclease R.BbvCI
    • Heiter D.F., Lunnen K.D., and Wilson G.G. Site-specific DNA-nicking mutants of the heterodimeric restriction endonuclease R.BbvCI. J. Mol. Biol. 348 (2005) 631-640
    • (2005) J. Mol. Biol. , vol.348 , pp. 631-640
    • Heiter, D.F.1    Lunnen, K.D.2    Wilson, G.G.3
  • 9
    • 0035818527 scopus 로고    scopus 로고
    • Engineering a nicking endonuclease N.AlwI by domain swapping
    • Xu Y., Lunnen K.D., and Kong H. Engineering a nicking endonuclease N.AlwI by domain swapping. Proc. Natl. Acad. Sci. USA 98 (2001) 12990-12995
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12990-12995
    • Xu, Y.1    Lunnen, K.D.2    Kong, H.3
  • 10
    • 0034769233 scopus 로고    scopus 로고
    • Converting MlyI endonuclease into a nicking enzyme by changing its oligomerization state
    • Besnier C.E., and Kong H. Converting MlyI endonuclease into a nicking enzyme by changing its oligomerization state. EMBO Rep. 2 (2001) 782-786
    • (2001) EMBO Rep. , vol.2 , pp. 782-786
    • Besnier, C.E.1    Kong, H.2
  • 11
    • 1542268955 scopus 로고    scopus 로고
    • Engineering strand-specific DNA nicking enzymes from the type IIS restriction endonucleases BsaI, BsmBI, and BsmAI
    • Zhu Z., Samuelson J.C., Zhou J., Dore A., and Xu S.-Y. Engineering strand-specific DNA nicking enzymes from the type IIS restriction endonucleases BsaI, BsmBI, and BsmAI. J. Mol. Biol. 337 (2004) 573-583
    • (2004) J. Mol. Biol. , vol.337 , pp. 573-583
    • Zhu, Z.1    Samuelson, J.C.2    Zhou, J.3    Dore, A.4    Xu, S.-Y.5
  • 12
    • 65549139378 scopus 로고    scopus 로고
    • Targeting individual subunits of the FokI restriction endonuclease to specific DNA strands
    • Sanders K.L., Catto L.E., Bellamy S.R., and Halford S.E. Targeting individual subunits of the FokI restriction endonuclease to specific DNA strands. Nucleic Acids Res. 37 (2009) 2105-2115
    • (2009) Nucleic Acids Res. , vol.37 , pp. 2105-2115
    • Sanders, K.L.1    Catto, L.E.2    Bellamy, S.R.3    Halford, S.E.4
  • 13
    • 3142773244 scopus 로고    scopus 로고
    • The isolation of strand-specific nicking endonucleases from a randomized SapI expression library
    • Samuelson J.C., Zhu Z., and Xu S.-Y. The isolation of strand-specific nicking endonucleases from a randomized SapI expression library. Nucleic Acids Res. 32 (2004) 3661-3671
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3661-3671
    • Samuelson, J.C.1    Zhu, Z.2    Xu, S.-Y.3
  • 14
    • 49349086561 scopus 로고    scopus 로고
    • Engineering variants of the I-SceI homing endonuclease with strand-specific and site-specific DNA-nicking activity
    • Niu Y., Tenney K., Li H., and Gimble F.S. Engineering variants of the I-SceI homing endonuclease with strand-specific and site-specific DNA-nicking activity. J. Mol. Biol. 382 (2008) 188-202
    • (2008) J. Mol. Biol. , vol.382 , pp. 188-202
    • Niu, Y.1    Tenney, K.2    Li, H.3    Gimble, F.S.4
  • 16
    • 0037135556 scopus 로고    scopus 로고
    • Mismatch repair in human nuclear extracts. Quantitative analyses of excision of nicked circular mismatched DNA substrates, constructed by a new technique employing synthetic oligonucleotides
    • Wang H., and Hays J.B. Mismatch repair in human nuclear extracts. Quantitative analyses of excision of nicked circular mismatched DNA substrates, constructed by a new technique employing synthetic oligonucleotides. J. Biol. Chem. 277 (2002) 26136-26142
    • (2002) J. Biol. Chem. , vol.277 , pp. 26136-26142
    • Wang, H.1    Hays, J.B.2
  • 17
    • 0037446841 scopus 로고    scopus 로고
    • Isothermal reactions for the amplification of oligonucleotides
    • Van Ness J., Van Ness L.K., and Galas D.J. Isothermal reactions for the amplification of oligonucleotides. Proc. Natl. Acad. Sci. USA 100 (2003) 4504-4509
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4504-4509
    • Van Ness, J.1    Van Ness, L.K.2    Galas, D.J.3
  • 18
    • 52249124502 scopus 로고    scopus 로고
    • Specific versus nonspecific isothermal DNA amplification through thermophilic polymerase and nicking enzyme activities
    • Tan E., Erwin B., Dames S., Ferguson T., Buechel M., Irvine B., Voelkerding K., and Niemz A. Specific versus nonspecific isothermal DNA amplification through thermophilic polymerase and nicking enzyme activities. Biochemistry 47 (2008) 9987-9999
    • (2008) Biochemistry , vol.47 , pp. 9987-9999
    • Tan, E.1    Erwin, B.2    Dames, S.3    Ferguson, T.4    Buechel, M.5    Irvine, B.6    Voelkerding, K.7    Niemz, A.8
  • 19
    • 13444305311 scopus 로고    scopus 로고
    • Cloning of CviPII nicking and modification system from chlorella virus NYs-1 and application of Nt.CviPII in random DNA amplification
    • Chan S.-H., Zhu Z., Van Etten J.L., and Xu S.-Y. Cloning of CviPII nicking and modification system from chlorella virus NYs-1 and application of Nt.CviPII in random DNA amplification. Nucleic Acids Res. 32 (2004) 6187-6199
    • (2004) Nucleic Acids Res. , vol.32 , pp. 6187-6199
    • Chan, S.-H.1    Zhu, Z.2    Van Etten, J.L.3    Xu, S.-Y.4
  • 23
    • 0025865885 scopus 로고
    • Isolation of BamHI variants with reduced cleavage activities
    • Xu S.-Y., and Schildkraut I. Isolation of BamHI variants with reduced cleavage activities. J. Biol. Chem. 266 (1991) 4425-4429
    • (1991) J. Biol. Chem. , vol.266 , pp. 4425-4429
    • Xu, S.-Y.1    Schildkraut, I.2
  • 24
    • 53649100100 scopus 로고    scopus 로고
    • The development and impact of 454 sequencing
    • Rothberg J.M., and Leamon J.H. The development and impact of 454 sequencing. Nat. Biotechnol. 26 (2008) 1117-1124
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1117-1124
    • Rothberg, J.M.1    Leamon, J.H.2
  • 26
    • 0037368961 scopus 로고    scopus 로고
    • Croceibacter atlanticus gen. nov., sp. nov., a novel marine bacterium in the family Flavobacteriaceae
    • Cho J.C., and Giovannoni S.J. Croceibacter atlanticus gen. nov., sp. nov., a novel marine bacterium in the family Flavobacteriaceae. Syst. Appl. Microbiol. 26 (2003) 76-83
    • (2003) Syst. Appl. Microbiol. , vol.26 , pp. 76-83
    • Cho, J.C.1    Giovannoni, S.J.2
  • 27
    • 0018966254 scopus 로고
    • Cloning the modification methylase gene of Bacillus sphaericus R in Escherichia coli
    • Szomolanyi I., Kiss A., and Venetianer P. Cloning the modification methylase gene of Bacillus sphaericus R in Escherichia coli. Gene 10 (1980) 219-225
    • (1980) Gene , vol.10 , pp. 219-225
    • Szomolanyi, I.1    Kiss, A.2    Venetianer, P.3
  • 28
    • 0028240186 scopus 로고
    • The 'endo-blue method' for direct cloning of restriction endonuclease genes in E. coli
    • Fomenkov A., Xiao J.-P., Dila D., Raleigh E., and Xu S.-Y. The 'endo-blue method' for direct cloning of restriction endonuclease genes in E. coli. Nucleic Acids Res. 22 (1994) 2399-2403
    • (1994) Nucleic Acids Res. , vol.22 , pp. 2399-2403
    • Fomenkov, A.1    Xiao, J.-P.2    Dila, D.3    Raleigh, E.4    Xu, S.-Y.5
  • 29
    • 0025830670 scopus 로고
    • SOS induction as an in vivo assay of enzyme-DNA interactions
    • Heitman J., and Model P. SOS induction as an in vivo assay of enzyme-DNA interactions. Gene 103 (1991) 1-9
    • (1991) Gene , vol.103 , pp. 1-9
    • Heitman, J.1    Model, P.2
  • 30
    • 0039577881 scopus 로고
    • DNA-damaging agents stimulate gene expression at specific loci in Escherichia coli
    • Kenyon C.J., and Walker G.C. DNA-damaging agents stimulate gene expression at specific loci in Escherichia coli. Proc. Natl. Acad. Sci. USA 77 (1980) 2819-2823
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2819-2823
    • Kenyon, C.J.1    Walker, G.C.2
  • 32
    • 28844494799 scopus 로고    scopus 로고
    • Crystal structure of the restriction-modification system control element C.Bcll and mapping of its binding site
    • Sawaya M.R., Zhu Z., Mersha F., Chan S.-H., Dabur R., Xu S.-Y., and Balendiran G.K. Crystal structure of the restriction-modification system control element C.Bcll and mapping of its binding site. Structure 13 (2005) 1837-1847
    • (2005) Structure , vol.13 , pp. 1837-1847
    • Sawaya, M.R.1    Zhu, Z.2    Mersha, F.3    Chan, S.-H.4    Dabur, R.5    Xu, S.-Y.6    Balendiran, G.K.7
  • 33
    • 0023425411 scopus 로고
    • Missing contact probing of DNA-protein interactions
    • Brunelle A., and Schleif R.F. Missing contact probing of DNA-protein interactions. Proc. Natl. Acad. Sci. USA 84 (1987) 6673-6676
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6673-6676
    • Brunelle, A.1    Schleif, R.F.2
  • 34
    • 0024359479 scopus 로고
    • The negative charge of Glu-111 is required to activate the cleavage center of EcoRI endonuclease
    • Wright D.J., King K., and Modrich P. The negative charge of Glu-111 is required to activate the cleavage center of EcoRI endonuclease. J. Biol. Chem. 264 (1989) 11816-11821
    • (1989) J. Biol. Chem. , vol.264 , pp. 11816-11821
    • Wright, D.J.1    King, K.2    Modrich, P.3
  • 35
    • 0026650908 scopus 로고
    • On the catalytic mechanism of EcoRI and EcoRV. A detailed proposal based on biochemical results, structural data and molecular modelling
    • Jeltsch A., Alves J., Maass G., and Pingoud A. On the catalytic mechanism of EcoRI and EcoRV. A detailed proposal based on biochemical results, structural data and molecular modelling. FEBS Lett. 304 (1992) 4-8
    • (1992) FEBS Lett. , vol.304 , pp. 4-8
    • Jeltsch, A.1    Alves, J.2    Maass, G.3    Pingoud, A.4
  • 36
    • 0028932881 scopus 로고
    • Structure and function of restriction endonucleases
    • Aggarwal A.K. Structure and function of restriction endonucleases. Curr. Opin. Struct. Biol. 5 (1995) 11-19
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 11-19
    • Aggarwal, A.K.1
  • 37
    • 0035096078 scopus 로고    scopus 로고
    • Restriction enzyme BsoBI-DNA complex: a tunnel for recognition of degenerate DNA sequences and potential histidine catalysis
    • Vander Woerd M., Pelletier J., Xu S.-Y., and Friedman A. Restriction enzyme BsoBI-DNA complex: a tunnel for recognition of degenerate DNA sequences and potential histidine catalysis. Structure 9 (2001) 133-144
    • (2001) Structure , vol.9 , pp. 133-144
    • Vander Woerd, M.1    Pelletier, J.2    Xu, S.-Y.3    Friedman, A.4
  • 40
    • 4143108003 scopus 로고    scopus 로고
    • DNA binding and cleavage by the HNH homing endonuclease I-HmuI
    • Shen B.W., Landthaler M., Shub D.A., and Stoddard B.L. DNA binding and cleavage by the HNH homing endonuclease I-HmuI. J. Mol. Biol. 342 (2004) 43-56
    • (2004) J. Mol. Biol. , vol.342 , pp. 43-56
    • Shen, B.W.1    Landthaler, M.2    Shub, D.A.3    Stoddard, B.L.4
  • 41
    • 0030472767 scopus 로고    scopus 로고
    • T4 endonuclease VII. Importance of a histidine-aspartate cluster within the zinc-binding domain
    • Giraud-Panis M.J., and Lilley D.M. T4 endonuclease VII. Importance of a histidine-aspartate cluster within the zinc-binding domain. J. Biol. Chem. 271 (1996) 33148-33155
    • (1996) J. Biol. Chem. , vol.271 , pp. 33148-33155
    • Giraud-Panis, M.J.1    Lilley, D.M.2
  • 42
    • 46349101158 scopus 로고    scopus 로고
    • Structural and evolutionary classification of Type II restriction enzymes based on theoretical and experimental analyses
    • Orlowski J., and Bujnicki J.M. Structural and evolutionary classification of Type II restriction enzymes based on theoretical and experimental analyses. Nucleic Acids Res. 36 (2008) 3552-3569
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3552-3569
    • Orlowski, J.1    Bujnicki, J.M.2
  • 43
    • 11344267268 scopus 로고    scopus 로고
    • Type II restriction endonuclease R.KpnI is a member of the HNH nuclease superfamily
    • Saravanan M., Bujnicki J.M., Cymerman I.A., Rao D.N., and Nagaraja V. Type II restriction endonuclease R.KpnI is a member of the HNH nuclease superfamily. Nucleic Acids Res. 32 (2004) 6129-6135
    • (2004) Nucleic Acids Res. , vol.32 , pp. 6129-6135
    • Saravanan, M.1    Bujnicki, J.M.2    Cymerman, I.A.3    Rao, D.N.4    Nagaraja, V.5
  • 44
    • 23444453714 scopus 로고    scopus 로고
    • MnlI - the member of H-N-H subtype of Type IIS restriction endonucleases
    • Kriukiene E., Lubiene J., Lagunavicius A., and Lubys A. MnlI - the member of H-N-H subtype of Type IIS restriction endonucleases. Biochim. Biophys. Acta 1751 (2005) 194-204
    • (2005) Biochim. Biophys. Acta , vol.1751 , pp. 194-204
    • Kriukiene, E.1    Lubiene, J.2    Lagunavicius, A.3    Lubys, A.4
  • 45
    • 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., and Bochtler M. Crystal structure of the beta beta alpha-Me type II restriction endonuclease Hpy99I with target DNA. Nucleic Acids Res. 37 (2009) 3799-3810
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3799-3810
    • Sokolowska, M.1    Czapinska, H.2    Bochtler, M.3
  • 46
    • 0035150384 scopus 로고    scopus 로고
    • Polyphyletic evolution of type II restriction enzymes revisited: two independent sources of second-hand folds revealed
    • Bujnicki J.M., Radlinska M., and Rychlewski L. Polyphyletic evolution of type II restriction enzymes revisited: two independent sources of second-hand folds revealed. Trends Biochem. Sci. 26 (2001) 9-11
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 9-11
    • Bujnicki, J.M.1    Radlinska, M.2    Rychlewski, L.3
  • 48
    • 36148984593 scopus 로고    scopus 로고
    • 2+ in maintaining structural integrity and inducing DNA sequence specificity in a promiscuous endonuclease
    • 2+ in maintaining structural integrity and inducing DNA sequence specificity in a promiscuous endonuclease. J. Biol. Chem. 282 (2007) 32320-32326
    • (2007) J. Biol. Chem. , vol.282 , pp. 32320-32326
    • Saravanan, M.1    Vasu, K.2    Ghosh, S.3    Nagaraja, V.4
  • 49
    • 41449117713 scopus 로고    scopus 로고
    • Structures of the rare-cutting restriction endonuclease NotI reveal a unique metal binding fold involved in DNA binding
    • Lambert A.R., Sussman D., Shen B., Maunus R., Nix J., Samuelson J., Xu S.-Y., and Stoddard B.L. Structures of the rare-cutting restriction endonuclease NotI reveal a unique metal binding fold involved in DNA binding. Structure 16 (2008) 558-569
    • (2008) Structure , vol.16 , pp. 558-569
    • Lambert, A.R.1    Sussman, D.2    Shen, B.3    Maunus, R.4    Nix, J.5    Samuelson, J.6    Xu, S.-Y.7    Stoddard, B.L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.