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Volumn 54, Issue 2, 2013, Pages 685-691

Prokaryotic expression and purification of soluble maize Ac transposase

Author keywords

AcTPase; E. coli; Expression; His Tag; LC MS MS; Maize; Purification

Indexed keywords

ACTPASE; E. COLI; EXPRESSION; HIS-TAG; LC-MS/MS; MAIZE;

EID: 84882901149     PISSN: 10736085     EISSN: 15590305     Source Type: Journal    
DOI: 10.1007/s12033-012-9610-z     Document Type: Article
Times cited : (6)

References (30)
  • 1
    • 42349096534 scopus 로고    scopus 로고
    • Plant transposable elements: Where genetics meets genomics
    • 10.1038/nrg2337 1:CAS:528:DC%2BD1cXkvVOhs7k%3D
    • Feschotte, C. (2008). Plant transposable elements: where genetics meets genomics. Nature Reviews Genetics, 9, 397-405.
    • (2008) Nature Reviews Genetics , vol.9 , pp. 397-405
    • Feschotte, C.1
  • 2
    • 0037301560 scopus 로고    scopus 로고
    • Origin of a substantial fraction of human regulatory sequences from transposable elements
    • 10.1016/S0168-9525(02)00006-9 1:CAS:528:DC%2BD3sXkvVyitg%3D%3D
    • Jordan, I. K., Rogozin, I. B., Glazko, G. V., & Koonin, E. V. (2003). Origin of a substantial fraction of human regulatory sequences from transposable elements. Trends in Genetics, 19, 68-72.
    • (2003) Trends in Genetics , vol.19 , pp. 68-72
    • Jordan, I.K.1    Rogozin, I.B.2    Glazko, G.V.3    Koonin, E.V.4
  • 3
    • 84863388033 scopus 로고    scopus 로고
    • Mutagenesis of barley malting quality QTLs with Ds transposons
    • 10.1007/s10142-011-0258-8 1:CAS:528:DC%2BC38XjvVSktbY%3D
    • Singh, S., Tan, H.-Q., & Singh, J. (2012). Mutagenesis of barley malting quality QTLs with Ds transposons. Functional and Integrative Genomics, 12, 131-141.
    • (2012) Functional and Integrative Genomics , vol.12 , pp. 131-141
    • Singh, S.1    Tan, H.-Q.2    Singh, J.3
  • 4
    • 33750916343 scopus 로고    scopus 로고
    • High-frequency Ds remobilization over multiple generations in barley facilitates gene tagging in large genomes
    • 10.1007/s11103-006-9067-1 1:CAS:528:DC%2BD28XhtFyltL3L
    • Singh, J., Zhang, S., Chen, C., Cooper, L., Bregitzer, P., Sturbaum, A., et al. (2006). High-frequency Ds remobilization over multiple generations in barley facilitates gene tagging in large genomes. Plant Molecular Biology, 62, 937-950.
    • (2006) Plant Molecular Biology , vol.62 , pp. 937-950
    • Singh, J.1    Zhang, S.2    Chen, C.3    Cooper, L.4    Bregitzer, P.5    Sturbaum, A.6    Hayes, P.M.7    Lemaux, P.G.8
  • 5
    • 40749128495 scopus 로고    scopus 로고
    • A versatile transposon-based activation tag vector system for functional genomics in cereals and other monocot plants
    • 10.1104/pp.107.111427 1:CAS:528:DC%2BD1cXjtFCmsLg%3D
    • Qu, S., Desai, A., Wing, R., & Sundaresan, V. (2008). A versatile transposon-based activation tag vector system for functional genomics in cereals and other monocot plants. Plant Physiology, 146, 189-199.
    • (2008) Plant Physiology , vol.146 , pp. 189-199
    • Qu, S.1    Desai, A.2    Wing, R.3    Sundaresan, V.4
  • 6
  • 7
    • 78650675586 scopus 로고    scopus 로고
    • DNA transposon Hermes inserts into DNA in nucleosome-free regions in vivo
    • 10.1073/pnas.1016382107 1:CAS:528:DC%2BC3MXntVKg
    • Gangadharan, S., Mularononi, L., Fain-Thornton, J., Wheelan, S. J., & Craig, N. L. (2010). DNA transposon Hermes inserts into DNA in nucleosome-free regions in vivo. PNAS, 107(51), 21966-21972.
    • (2010) PNAS , vol.107 , Issue.51 , pp. 21966-21972
    • Gangadharan, S.1    Mularononi, L.2    Fain-Thornton, J.3    Wheelan, S.J.4    Craig, N.L.5
  • 8
    • 33751318230 scopus 로고    scopus 로고
    • Trans-kingdom transposition of the maize dissociation element
    • 10.1534/genetics.106.061184 1:CAS:528:DC%2BD2sXktlChsQ%3D%3D
    • Emelyanov, A., Gao, Y., Naqvi, N. I., & Parinov, S. (2006). Trans-kingdom transposition of the maize dissociation element. Genetics, 174, 1095-1104.
    • (2006) Genetics , vol.174 , pp. 1095-1104
    • Emelyanov, A.1    Gao, Y.2    Naqvi, N.I.3    Parinov, S.4
  • 10
    • 0033780451 scopus 로고    scopus 로고
    • Transposition of maize Ac/Ds transposable elements in yeast Saccharomyces cerevisiae
    • 10.1038/82827 1:CAS:528:DC%2BD3cXntlGms7o%3D
    • Weil, C. F., & Kunze, R. (2000). Transposition of maize Ac/Ds transposable elements in yeast Saccharomyces cerevisiae. Nature Genetics, 26, 187-190.
    • (2000) Nature Genetics , vol.26 , pp. 187-190
    • Weil, C.F.1    Kunze, R.2
  • 11
    • 0041695830 scopus 로고    scopus 로고
    • Maize activator transposase expressed in Saccharomyces cerevisiae from a genetic clone: Detection via ELISA, and proposed use in complementation studies
    • 10.1159/000069977 1:CAS:528:DC%2BD3sXjs1Giu70%3D
    • MacRae, A. F. (2003). Maize activator transposase expressed in Saccharomyces cerevisiae from a genetic clone: detection via ELISA, and proposed use in complementation studies. Journal of Molecular Microbiology and Biotechnology, 5, 78-81.
    • (2003) Journal of Molecular Microbiology and Biotechnology , vol.5 , pp. 78-81
    • Macrae, A.F.1
  • 12
    • 0034143320 scopus 로고    scopus 로고
    • A highly conserved domain of the maize activator transposase is involved in dimerization
    • 1:CAS:528:DC%2BD3cXktFagt7Y%3D
    • Essers, L., Adolphs, R. H., & Kunze, R. (2000). A highly conserved domain of the maize activator transposase is involved in dimerization. Plant Cell, 12, 211-223.
    • (2000) Plant Cell , vol.12 , pp. 211-223
    • Essers, L.1    Adolphs, R.H.2    Kunze, R.3
  • 13
    • 1642458360 scopus 로고    scopus 로고
    • Microhomology-dependent end joining and repair of transposon-induced DNA hairpins by host factors in Saccharomyces cerevisiae
    • 10.1128/MCB.24.3.1351-1364.2004 1:CAS:528:DC%2BD2cXmsFWmug%3D%3D
    • Yu, J., Marshall, K., Yamaguchi, M., Haber, J. E., & Weil, C. F. (2004). Microhomology-dependent end joining and repair of transposon-induced DNA hairpins by host factors in Saccharomyces cerevisiae. Molecular and Cellular Biology, 24(3), 1351-1364.
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.3 , pp. 1351-1364
    • Yu, J.1    Marshall, K.2    Yamaguchi, M.3    Haber, J.E.4    Weil, C.F.5
  • 14
    • 78649326287 scopus 로고    scopus 로고
    • DDE transposases: Structural similarity and diversity
    • 10.1016/j.addr.2010.06.006 1:CAS:528:DC%2BC3cXhsVGitb%2FL
    • Nesmelova, I. V., & Hackett, P. B. (2010). DDE transposases: structural similarity and diversity. Advanced Drug Delivery Reviews, 62, 1187-1195.
    • (2010) Advanced Drug Delivery Reviews , vol.62 , pp. 1187-1195
    • Nesmelova, I.V.1    Hackett, P.B.2
  • 15
    • 0034913514 scopus 로고    scopus 로고
    • Structure and evolution of the hAT transposon family
    • 1:CAS:528:DC%2BD3MXmtVKru7Y%3D
    • Rubin, E., Lithwick, G., & Levy, A. (2001). Structure and evolution of the hAT transposon family. Genetics, 158, 949-957.
    • (2001) Genetics , vol.158 , pp. 949-957
    • Rubin, E.1    Lithwick, G.2    Levy, A.3
  • 16
    • 0025931131 scopus 로고
    • The ORFa protein, the putative transposase of maize transposable element Ac, has a basic DNA binding domain
    • 1:CAS:528:DyaK38Xht1ertLk%3D
    • Feldmar, S., & Kunze, R. (1991). The ORFa protein, the putative transposase of maize transposable element Ac, has a basic DNA binding domain. EMBO Journal, 10(13), 4003-4010.
    • (1991) EMBO Journal , vol.10 , Issue.13 , pp. 4003-4010
    • Feldmar, S.1    Kunze, R.2
  • 17
    • 0029257424 scopus 로고
    • One of three nuclear localization signals of maize activator transposase overlaps the DNA-binding domain
    • 10.1046/j.1365-313X.1995.7030441.x 1:CAS:528:DyaK2MXltFCgsbo%3D
    • Boehm, U., Heinlein, M., Behrens, U., & Kunze, R. (1995). One of three nuclear localization signals of maize activator transposase overlaps the DNA-binding domain. Plant Journal, 7(3), 441-451.
    • (1995) Plant Journal , vol.7 , Issue.3 , pp. 441-451
    • Boehm, U.1    Heinlein, M.2    Behrens, U.3    Kunze, R.4
  • 18
    • 0030892130 scopus 로고    scopus 로고
    • Maize activator transposase has a bipartite DNA binding domain that recognizes subterminal sequences and the terminal inverted repeats
    • 10.1007/s004380050410 1:CAS:528:DyaK2sXjsFKkur8%3D
    • Becker, H. A., & Kunze, R. (1997). Maize activator transposase has a bipartite DNA binding domain that recognizes subterminal sequences and the terminal inverted repeats. Molecular and General Genetics, 254, 219-230.
    • (1997) Molecular and General Genetics , vol.254 , pp. 219-230
    • Becker, H.A.1    Kunze, R.2
  • 21
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high-density shaking cultures
    • 10.1016/j.pep.2005.01.016 1:CAS:528:DC%2BD2MXjsFCktLw%3D
    • Studier, F. W. (2005). Protein production by auto-induction in high-density shaking cultures. Protein Expression and Purification, 41(1), 207-234.
    • (2005) Protein Expression and Purification , vol.41 , Issue.1 , pp. 207-234
    • Studier, F.W.1
  • 22
    • 84858396324 scopus 로고    scopus 로고
    • High-efficiency thermal asymmetric interlaced (HE-TAIL) PCR for amplification of Ds transposon insertion sites in barley
    • Tan, H-Q., & Singh, J. (2011). High-efficiency thermal asymmetric interlaced (HE-TAIL) PCR for amplification of Ds transposon insertion sites in barley. Journal of Plant Molecular Biology and Biotechnology, 2, 9-14.
    • (2011) Journal of Plant Molecular Biology and Biotechnology , vol.2 , pp. 9-14
    • Tan, H.-Q.1    Singh, J.2
  • 23
    • 84892625581 scopus 로고    scopus 로고
    • Seed development-related expression of ARGONAUTE4-9 class of genes in barley: Possible role in seed dormancy
    • Singh, M., and Singh, J. (2012) Seed development-related expression of ARGONAUTE4-9 class of genes in barley: possible role in seed dormancy. Euphytica. OnlineFirst, 1-7.
    • (2012) Euphytica. OnlineFirst , pp. 1-7
    • Singh, M.1    Singh, J.2
  • 24
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • 10.1002/elps.1150090603 1:CAS:528:DyaL1cXksFWisro%3D
    • Neuhoff, V., Arold, A., Taube, D., & Ehrhardrt, W. (1988). Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis, 9(6), 255-262.
    • (1988) Electrophoresis , vol.9 , Issue.6 , pp. 255-262
    • Neuhoff, V.1    Arold, A.2    Taube, D.3    Ehrhardrt, W.4
  • 25
    • 0034895653 scopus 로고    scopus 로고
    • Albumin and globulin proteins of wheat: Immunological and N-terminal sequence characterization
    • 10.1006/jcrs.2001.0380 1:CAS:528:DC%2BD3MXkvFOqtL4%3D
    • Singh, J., Blundell, M., Tanner, G., & Skerritt, J. H. (2001). Albumin and globulin proteins of wheat: immunological and N-terminal sequence characterization. Journal of Cereal Science, 34, 85-103.
    • (2001) Journal of Cereal Science , vol.34 , pp. 85-103
    • Singh, J.1    Blundell, M.2    Tanner, G.3    Skerritt, J.H.4
  • 26
    • 0026073798 scopus 로고
    • Detection and abundance of mRNA and protein encoded by transposable element activator (Ac) in maize
    • 10.1007/BF00269846 1:CAS:528:DyaK3MXhsl2ms7c%3D
    • Fusswinkel, H., Schein, S., Courage, U., Starlinger, P., & Kunze, R. (1991). Detection and abundance of mRNA and protein encoded by transposable element activator (Ac) in maize. Molecular and General Genetics, 225, 186-192.
    • (1991) Molecular and General Genetics , vol.225 , pp. 186-192
    • Fusswinkel, H.1    Schein, S.2    Courage, U.3    Starlinger, P.4    Kunze, R.5
  • 27
    • 3543149006 scopus 로고    scopus 로고
    • The toxicity of recombinant proteins in Escherichia coli: A comparison of overexpression in BL21(DE3), C41(DE3), and C43(DE3)
    • 10.1016/j.pep.2004.04.025 1:CAS:528:DC%2BD2cXmt1Cls7Y%3D
    • Dumon-Seignovert, L., Cariot, G., & Vuillard, L. (2004). The toxicity of recombinant proteins in Escherichia coli: a comparison of overexpression in BL21(DE3), C41(DE3), and C43(DE3). Protein Expression and Purification, 37, 203-206.
    • (2004) Protein Expression and Purification , vol.37 , pp. 203-206
    • Dumon-Seignovert, L.1    Cariot, G.2    Vuillard, L.3
  • 28
    • 0000671329 scopus 로고
    • Low temperatures stabilize interferon α-2 against proteolysis in Methylophilus methylotrophus and Escherichia coli
    • 10.1007/BF00262455 1:CAS:528:DyaL1MXkvFGmsrc%3D
    • Chesshyre, J. A., & Hipkiss, A. R. (1989). Low temperatures stabilize interferon α-2 against proteolysis in Methylophilus methylotrophus and Escherichia coli. Applied Microbiology and Biotechnology, 31, 158-162.
    • (1989) Applied Microbiology and Biotechnology , vol.31 , pp. 158-162
    • Chesshyre, J.A.1    Hipkiss, A.R.2
  • 29
    • 13644262805 scopus 로고    scopus 로고
    • Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli
    • 10.1186/1475-2859-4-1
    • Sorensen, H. P., & Mortensen, K. K. (2005). Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microbial Cell Factories, 4, 1.
    • (2005) Microbial Cell Factories , vol.4 , pp. 1
    • Sorensen, H.P.1    Mortensen, K.K.2
  • 30
    • 0031105876 scopus 로고    scopus 로고
    • Expression of aggregation-prone recombinant proteins at low temperatures: A comparative study of the Escherichia coli cspA and tac promoter systems
    • 10.1006/prep.1996.0678 1:CAS:528:DyaK2sXhs12msLw%3D
    • Vasina, J. A., & Baneyx, F. (1997). Expression of aggregation-prone recombinant proteins at low temperatures: a comparative study of the Escherichia coli cspA and tac promoter systems. Protein Expression and Purification, 9(2), 211-218.
    • (1997) Protein Expression and Purification , vol.9 , Issue.2 , pp. 211-218
    • Vasina, J.A.1    Baneyx, F.2


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