메뉴 건너뛰기




Volumn 19, Issue 6, 2010, Pages 1243-1252

Purification of Escherichia coli RNA polymerase using a self-cleaving elastin-like polypeptide tag

Author keywords

ELP; Intein; Multisubunit enzyme; Purification; RNA polymerase

Indexed keywords

CASPASE RECRUITMENT DOMAIN PROTEIN 4; ELASTIN; POLYETHYLENE; POLYETHYLENEIMINE; POLYNUCLEOTIDE; POLYPEPTIDE; RECOMBINANT ENZYME; RNA POLYMERASE;

EID: 77952736311     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.403     Document Type: Article
Times cited : (19)

References (26)
  • 1
    • 0021447319 scopus 로고
    • Purification and subunit structure of RNA polymerase II from different stages of Artemia development
    • Cruces J, Diaz V, Quintanilla M, Renart J, Sebastian J (1984) Purification and subunit structure of RNA polymerase II from different stages of Artemia development. Eur J Biochem 141:279-282.
    • (1984) Eur J Biochem , vol.141 , pp. 279-282
    • Cruces, J.1    Diaz, V.2    Quintanilla, M.3    Renart, J.4    Sebastian, J.5
  • 2
    • 0028232348 scopus 로고
    • Calf thymus DNA helicase F, a replication protein a copurifying enzyme
    • Georgaki A, Tuteja N, Sturzenegger B, Hubscher U (1994) Calf thymus DNA helicase F, a replication protein A copurifying enzyme. Nucleic Acids Res 22: 1128-1134. (Pubitemid 24162113)
    • (1994) Nucleic Acids Research , vol.22 , Issue.7 , pp. 1128-1134
    • Georgaki, A.1    Tuteja, N.2    Sturzenegger, B.3    Hubscher, U.4
  • 3
    • 0015618514 scopus 로고
    • A procedure for the rapid purification of Escherichia coli deoxyribonucleic acid-dependent ribonucleic acid polymerase
    • Humphries P, McConnell DJ, Gordon RL (1973) A procedure for the rapid purification of Escherichia coli deoxyribonucleic acid-dependent ribonucleic acid polymerase. Biochem J 133:201-203.
    • (1973) Biochem J , vol.133 , pp. 201-203
    • Humphries, P.1    McConnell, D.J.2    Gordon, R.L.3
  • 4
    • 0015911237 scopus 로고
    • Separation of RNA polymerase holoenzyme from core enzyme on DNA-cellulose column
    • Mukai R, Iida Y (1973) Separation of RNA polymerase holoenzyme from core enzyme on DNA-cellulose column. Biochem Biophys Res Commun 54:134-139.
    • (1973) Biochem Biophys Res Commun , vol.54 , pp. 134-139
    • Mukai, R.1    Iida, Y.2
  • 5
    • 0015505665 scopus 로고
    • Chromatography of RNA polymerase from Escherichia coli on single stranded DNA-agarose columns
    • Nusslein C, Heyden B (1972) Chromatography of RNA polymerase from Escherichia coli on single stranded DNA-agarose columns. Biochem Biophys Res Commun 47:282-289.
    • (1972) Biochem Biophys Res Commun , vol.47 , pp. 282-289
    • Nusslein, C.1    Heyden, B.2
  • 6
    • 0021099627 scopus 로고
    • Purification and characterization of a multisubunit phosphatase from turkey gizzard smooth muscle the effect of calmodulin binding to myosin light chain kinase on dephosphorylation
    • Pato MD, Adelstein RS (1983) Purification and characterization of a multisubunit phosphatase from turkey gizzard smooth muscle. The effect of calmodulin binding to myosin light chain kinase on dephosphorylation. J Biol Chem 258:7047-7054.
    • (1983) J Biol Chem , vol.258 , pp. 7047-7054
    • Pato, M.D.1    Adelstein, R.S.2
  • 7
    • 0016284663 scopus 로고
    • The reversible denaturation of deoxyribonucleic acid-dependent ribonucleic acid polymerase of Escherichia coli
    • Yarbrough LR, Hurwitz J (1974) The reversible denaturation of deoxyribonucleic acid-dependent ribonucleic acid polymerase of Escherichia coli. J Biol Chem 249: 5394-5399.
    • (1974) J Biol Chem , vol.249 , pp. 5394-5399
    • Yarbrough, L.R.1    Hurwitz, J.2
  • 8
    • 0027744758 scopus 로고
    • Recombinant Escherichia coli RNA polymerase - Purification of individually overexpressed subunits and in vitro assembly
    • DOI 10.1006/prep.1993.1066
    • Borukhov S, Goldfarb A (1993) Recombinant Escherichia coli RNA polymerase: purification of individually overexpressed subunits and in vitro assembly. Protein Expr Purif 4:503-511. (Pubitemid 2007168)
    • (1993) Protein Expression and Purification , vol.4 , Issue.6 , pp. 503-511
    • Borukhov, S.1    Goldfarb, A.2
  • 9
    • 1542650914 scopus 로고    scopus 로고
    • Purification of G protein subunits from Sf9 insect cells using hexahistidine-tagged alpha and beta gamma subunits
    • Kozasa T (2004) Purification of G protein subunits from Sf9 insect cells using hexahistidine-tagged alpha and beta gamma subunits. Methods Mol Biol 237: 21-38.
    • (2004) Methods Mol Biol , vol.237 , pp. 21-38
    • Kozasa, T.1
  • 10
    • 1542441272 scopus 로고    scopus 로고
    • Assay for G protein-dependent activation of phospholipase C beta using purified protein components
    • Ghosh M, Smrcka AV (2004) Assay for G protein-dependent activation of phospholipase C beta using purified protein components. Methods Mol Biol 237:67-75.
    • (2004) Methods Mol Biol , vol.237 , pp. 67-75
    • Ghosh, M.1    Smrcka, A.V.2
  • 11
    • 0036669677 scopus 로고    scopus 로고
    • Advances in gentle immunoaffinity chromatography
    • Burgess RR, Thompson NE (2002) Advances in gentle immunoaffinity chromatography. Curr Opin Biotechnol 13:304-308.
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 304-308
    • Burgess, R.R.1    Thompson, N.E.2
  • 12
    • 33847368588 scopus 로고    scopus 로고
    • A system for heterologous expression and isolation of Escherichia coli RNA polymerase and its components
    • Khodak YA, Koroleva ON, Drutsa VL (2007) A system for heterologous expression and isolation of Escherichia coli RNA polymerase and its components. Biochemistry 72:178-187.
    • (2007) Biochemistry , vol.72 , pp. 178-187
    • Khodak, Y.A.1    Koroleva, O.N.2    Drutsa, V.L.3
  • 13
    • 0038823636 scopus 로고    scopus 로고
    • Co-overexpression of Escherichia coli RNA polymerase subunits allows isolation and analysis of mutant enzymes lacking lineage-specific sequence insertions
    • DOI 10.1074/jbc.M211214200
    • Artsimovitch I, Svetlov V, Murakami KS, Landick R (2003) Co-overexpression of Escherichia coli RNA polymerase subunits allows isolation and analysis of mutant enzymes lacking lineage-specific sequence insertions. J Biol Chem 278:12344-12355. (Pubitemid 36800218)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 12344-12355
    • Artsimovitch, I.1    Svetlov, V.2    Murakami, K.S.3    Landick, R.4
  • 14
    • 24044491571 scopus 로고    scopus 로고
    • Simple bioseparations using self-cleaving elastin-like polypeptide tags
    • DOI 10.1038/nmeth787
    • Banki MR, Feng L, Wood DW (2005) Simple bioseparations using self-cleaving elastin-like polypeptide tags. Nat Methods 2:659-661. (Pubitemid 41223091)
    • (2005) Nature Methods , vol.2 , Issue.9 , pp. 659-661
    • Banki, M.R.1    Feng, L.2    Wood, D.W.3
  • 16
    • 0032739304 scopus 로고    scopus 로고
    • Purification of recombinant proteins by fusion with thermally-responsive polypeptides
    • DOI 10.1038/15100
    • Meyer DE, Chilkoti A (1999) Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat Biotechnol 17:1112-1115. (Pubitemid 29533553)
    • (1999) Nature Biotechnology , vol.17 , Issue.11 , pp. 1112-1115
    • Meyer, D.E.1    Chilkoti, A.2
  • 17
    • 34548841392 scopus 로고    scopus 로고
    • Recombinant protein purification by self-cleaving aggregation tag
    • Wu W-Y, Mee C, Califano F, Banki R, Wood DW (2006) Recombinant protein purification by self-cleaving aggregation tag. Nat Protoc 1:2257-2262.
    • (2006) Nat Protoc , vol.1 , pp. 2257-2262
    • Wu, W.-Y.1    Mee, C.2    Califano, F.3    Banki, R.4    Wood, D.W.5
  • 18
    • 0023918675 scopus 로고
    • Structure and function of bacterial sigma factors
    • Helmann JD, Chamberlin MJ (1988) Structure and function of bacterial sigma factors. Annu Rev Biochem 57:839-872.
    • (1988) Annu Rev Biochem , vol.57 , pp. 839-872
    • Helmann, J.D.1    Chamberlin, M.J.2
  • 19
  • 20
    • 0016748261 scopus 로고
    • A procedure for the rapid, large-scall purification of Escherichia coli DNA-dependent RNA polymerase involving Polymin P precipitation and DNA-cellulose chromatography
    • Burgess RR, Jendrisak JJ (1975) A procedure for the rapid, large-scall purification of Escherichia coli DNA-dependent RNA polymerase involving Polymin P precipitation and DNA-cellulose chromatography. Biochemistry 14:4634-4638.
    • (1975) Biochemistry , vol.14 , pp. 4634-4638
    • Burgess, R.R.1    Jendrisak, J.J.2
  • 21
    • 0017146440 scopus 로고
    • Rapid micromethod for the purification of Escherichia coli ribonucleic acid polymerase and the preparation of bacterial extracts active in ribonucleic acid synthesis
    • Gross C, Engbaek F, Flammang T, Burgess R (1976) Rapid micromethod for the purification of Escherichia coli ribonucleic acid polymerase and the preparation of bacterial extracts active in ribonucleic acid synthesis. J Bacteriol 128:382-389.
    • (1976) J Bacteriol , vol.128 , pp. 382-389
    • Gross, C.1    Engbaek, F.2    Flammang, T.3    Burgess, R.4
  • 22
    • 0015949863 scopus 로고
    • Multiple forms of deoxyribonucleic acid-dependent ribonucleic acid polymerase in Xenopus laevis Isolation and partial characterization
    • Roeder RG (1974) Multiple forms of deoxyribonucleic acid-dependent ribonucleic acid polymerase in Xenopus laevis. Isolation and partial characterization. J Biol Chem 249:241-248.
    • (1974) J Biol Chem , vol.249 , pp. 241-248
    • Roeder, R.G.1
  • 24
    • 0025886298 scopus 로고
    • The omega subunit of Escherichia coli K-12 RNA polymerase is not required for stringent RNA control in vivo
    • Gentry D, Xiao H, Burgess R, Cashel M (1991) The omega subunit of Escherichia coli K-12 RNA polymerase is not required for stringent RNA control in vivo. J Bacteriol 173:3901-3903.
    • (1991) J Bacteriol , vol.173 , pp. 3901-3903
    • Gentry, D.1    Xiao, H.2    Burgess, R.3    Cashel, M.4
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 0022753749 scopus 로고
    • Accurate in vitro transcription of Xenopus laevis mitochondrial DNA from two bidirectional promoters
    • Bogenhagen DF, Yoza BK (1986) Accurate in vitro transcription of Xenopus laevis mitochondrial DNA from two bidirectional promoters. Mol Cell Biol 6: 2543-2550.
    • (1986) Mol Cell Biol , vol.6 , pp. 2543-2550
    • Bogenhagen, D.F.1    Yoza, B.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.