메뉴 건너뛰기




Volumn 11, Issue , 2011, Pages

Expression of tung tree diacylglycerol acyltransferase 1 in E. coli

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY TAGS; BACTERIAL EXPRESSION SYSTEMS; CARBOXYL TERMINUS; DATABASE SEARCHES; DIACYLGLYCEROL ACYLTRANSFERASES; E. COLI; EUKARYOTIC ORGANISMS; FULL-LENGTH PROTEINS; FUSION PROTEINS; IMMUNOBLOTTING; INTEGRAL MEMBRANE PROTEINS; MALTOSE BINDING PROTEINS; OPEN READING FRAME; PROTEASE DIGESTION; RATE-LIMITING STEPS; SOLUBLE FRACTION; TRIACYLGLYCEROLS; TRITON X-100; VERNICIA FORDII;

EID: 79960032578     PISSN: None     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/1472-6750-11-73     Document Type: Article
Times cited : (18)

References (35)
  • 1
    • 0037376557 scopus 로고    scopus 로고
    • Expression and purification of recombinant tristetraprolin that can bind to tumor necrosis factor-alpha mRNA and serve as a substrate for mitogen-activated protein kinases
    • 10.1016/S0003-9861(03)00012-2, 1351391, 12646273
    • Cao H, Dzineku F, Blackshear PJ. Expression and purification of recombinant tristetraprolin that can bind to tumor necrosis factor-alpha mRNA and serve as a substrate for mitogen-activated protein kinases. Arch Biochem Biophys 2003, 412:106-120. 10.1016/S0003-9861(03)00012-2, 1351391, 12646273.
    • (2003) Arch Biochem Biophys , vol.412 , pp. 106-120
    • Cao, H.1    Dzineku, F.2    Blackshear, P.J.3
  • 2
    • 7244252846 scopus 로고    scopus 로고
    • Expression, purification, and biochemical characterization of the antiinflammatory tristetraprolin: a zinc-dependent mRNA binding protein affected by posttranslational modifications
    • 10.1021/bi049014y, 1351390, 15504035
    • Cao H. Expression, purification, and biochemical characterization of the antiinflammatory tristetraprolin: a zinc-dependent mRNA binding protein affected by posttranslational modifications. Biochemistry 2004, 43:13724-13738. 10.1021/bi049014y, 1351390, 15504035.
    • (2004) Biochemistry , vol.43 , pp. 13724-13738
    • Cao, H.1
  • 3
    • 2442656756 scopus 로고    scopus 로고
    • Immunological characterization of tristetraprolin as a low abundance, inducible, stable cytosolic protein
    • 10.1074/jbc.M400900200, 1351392, 15010466
    • Cao H, Tuttle JS, Blackshear PJ. Immunological characterization of tristetraprolin as a low abundance, inducible, stable cytosolic protein. J Biol Chem 2004, 279:21489-21499. 10.1074/jbc.M400900200, 1351392, 15010466.
    • (2004) J Biol Chem , vol.279 , pp. 21489-21499
    • Cao, H.1    Tuttle, J.S.2    Blackshear, P.J.3
  • 4
    • 42049109899 scopus 로고    scopus 로고
    • Production and characterization of ZFP36L1 antiserum against recombinant protein from Escherichia coli
    • 10.1021/bp070269n, 2674335, 18302406
    • Cao H, Lin R, Ghosh S, Anderson RA, Urban JF. Production and characterization of ZFP36L1 antiserum against recombinant protein from Escherichia coli. Biotechnol Prog 2008, 24:326-333. 10.1021/bp070269n, 2674335, 18302406.
    • (2008) Biotechnol Prog , vol.24 , pp. 326-333
    • Cao, H.1    Lin, R.2    Ghosh, S.3    Anderson, R.A.4    Urban, J.F.5
  • 5
    • 79960892915 scopus 로고    scopus 로고
    • Recombinant protein production technology
    • Cao H. Recombinant protein production technology. J Jiangxi Agric Univ 2010, 32:1018-1031.
    • (2010) J Jiangxi Agric Univ , vol.32 , pp. 1018-1031
    • Cao, H.1
  • 6
    • 79960891444 scopus 로고    scopus 로고
    • Bioengineering recombinant diacylglycerol acyltransferases
    • Rijeka, Croatia: InTech, Carpi A
    • Cao H. Bioengineering recombinant diacylglycerol acyltransferases. Bioengineering 2011, 1-16. Rijeka, Croatia: InTech, Carpi A.
    • (2011) Bioengineering , pp. 1-16
    • Cao, H.1
  • 8
    • 0035914356 scopus 로고    scopus 로고
    • Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members
    • 10.1074/jbc.M106219200, 11481335
    • Cases S, Stone SJ, Zhou P, Yen E, Tow B, Lardizabal KD, Voelker T, Farese RV. Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members. J Biol Chem 2001, 276:38870-38876. 10.1074/jbc.M106219200, 11481335.
    • (2001) J Biol Chem , vol.276 , pp. 38870-38876
    • Cases, S.1    Stone, S.J.2    Zhou, P.3    Yen, E.4    Tow, B.5    Lardizabal, K.D.6    Voelker, T.7    Farese, R.V.8
  • 9
    • 0035914412 scopus 로고    scopus 로고
    • DGAT2 is a new diacylglycerol acyltransferase gene family: purification, cloning, and expression in insect cells of two polypeptides from Mortierella ramanniana with diacylglycerol acyltransferase activity
    • 10.1074/jbc.M106168200, 11481333
    • Lardizabal KD, Mai JT, Wagner NW, Wyrick A, Voelker T, Hawkins DJ. DGAT2 is a new diacylglycerol acyltransferase gene family: purification, cloning, and expression in insect cells of two polypeptides from Mortierella ramanniana with diacylglycerol acyltransferase activity. J Biol Chem 2001, 276:38862-38869. 10.1074/jbc.M106168200, 11481333.
    • (2001) J Biol Chem , vol.276 , pp. 38862-38869
    • Lardizabal, K.D.1    Mai, J.T.2    Wagner, N.W.3    Wyrick, A.4    Voelker, T.5    Hawkins, D.J.6
  • 10
    • 33749263895 scopus 로고    scopus 로고
    • Tung tree DGAT1 and DGAT2 have nonredundant functions in triacylglycerol biosynthesis and are localized to different subdomains of the endoplasmic reticulum
    • 10.1105/tpc.106.043695, 1560902, 16920778
    • Shockey JM, Gidda SK, Chapital DC, Kuan JC, Dhanoa PK, Bland JM, Rothstein SJ, Mullen RT, Dyer JM. Tung tree DGAT1 and DGAT2 have nonredundant functions in triacylglycerol biosynthesis and are localized to different subdomains of the endoplasmic reticulum. Plant Cell 2006, 18:2294-2313. 10.1105/tpc.106.043695, 1560902, 16920778.
    • (2006) Plant Cell , vol.18 , pp. 2294-2313
    • Shockey, J.M.1    Gidda, S.K.2    Chapital, D.C.3    Kuan, J.C.4    Dhanoa, P.K.5    Bland, J.M.6    Rothstein, S.J.7    Mullen, R.T.8    Dyer, J.M.9
  • 11
    • 77952715010 scopus 로고    scopus 로고
    • A distinct DGAT with sn-3 acetyltransferase activity that synthesizes unusual, reduced-viscosity oils in Euonymus and transgenic seeds
    • 10.1073/pnas.1001707107, 2889089, 20439724
    • Durrett TP, McClosky DD, Tumaney AW, Elzinga DA, Ohlrogge J, Pollard M. A distinct DGAT with sn-3 acetyltransferase activity that synthesizes unusual, reduced-viscosity oils in Euonymus and transgenic seeds. Proc Natl Acad Sci USA 2010, 107:9464-9469. 10.1073/pnas.1001707107, 2889089, 20439724.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 9464-9469
    • Durrett, T.P.1    McClosky, D.D.2    Tumaney, A.W.3    Elzinga, D.A.4    Ohlrogge, J.5    Pollard, M.6
  • 12
    • 33747123328 scopus 로고    scopus 로고
    • Cytosolic triacylglycerol biosynthetic pathway in oilseeds. Molecular cloning and expression of peanut cytosolic diacylglycerol acyltransferase
    • 10.1104/pp.106.082198, 1533943, 16798944
    • Saha S, Enugutti B, Rajakumari S, Rajasekharan R. Cytosolic triacylglycerol biosynthetic pathway in oilseeds. Molecular cloning and expression of peanut cytosolic diacylglycerol acyltransferase. Plant Physiol 2006, 141:1533-1543. 10.1104/pp.106.082198, 1533943, 16798944.
    • (2006) Plant Physiol , vol.141 , pp. 1533-1543
    • Saha, S.1    Enugutti, B.2    Rajakumari, S.3    Rajasekharan, R.4
  • 16
    • 33845977414 scopus 로고    scopus 로고
    • Membrane topology and identification of key functional amino acid residues of murine acyl-CoA:diacylglycerol acyltransferase-2
    • 10.1074/jbc.M607986200, 17035227
    • Stone SJ, Levin MC, Farese RV. Membrane topology and identification of key functional amino acid residues of murine acyl-CoA:diacylglycerol acyltransferase-2. J Biol Chem 2006, 281:40273-40282. 10.1074/jbc.M607986200, 17035227.
    • (2006) J Biol Chem , vol.281 , pp. 40273-40282
    • Stone, S.J.1    Levin, M.C.2    Farese, R.V.3
  • 17
    • 0035503969 scopus 로고    scopus 로고
    • Human acyl-CoA:diacylglycerol acyltransferase is a tetrameric protein
    • 10.1042/0264-6021:3590707, 1222193, 11672446
    • Cheng D, Meegalla RL, He B, Cromley DA, Billheimer JT, Young PR. Human acyl-CoA:diacylglycerol acyltransferase is a tetrameric protein. Biochem J 2001, 359:707-714. 10.1042/0264-6021:3590707, 1222193, 11672446.
    • (2001) Biochem J , vol.359 , pp. 707-714
    • Cheng, D.1    Meegalla, R.L.2    He, B.3    Cromley, D.A.4    Billheimer, J.T.5    Young, P.R.6
  • 20
    • 0032965889 scopus 로고    scopus 로고
    • Cloning of a cDNA encoding diacylglycerol acyltransferase from Arabidopsis thaliana and its functional expression
    • 10.1016/S0014-5793(99)00646-8, 10386579
    • Hobbs DH, Lu C, Hills MJ. Cloning of a cDNA encoding diacylglycerol acyltransferase from Arabidopsis thaliana and its functional expression. FEBS Lett 1999, 452:145-149. 10.1016/S0014-5793(99)00646-8, 10386579.
    • (1999) FEBS Lett , vol.452 , pp. 145-149
    • Hobbs, D.H.1    Lu, C.2    Hills, M.J.3
  • 21
    • 78549270833 scopus 로고    scopus 로고
    • Topological orientation of acyl-CoA:diacylglycerol acyltransferase-1 (DGAT1) and identification of a putative active site histidine and the role of the n terminus in dimer/tetramer formation
    • 10.1074/jbc.M110.163691, 20876538
    • McFie PJ, Stone SL, Banman SL, Stone SJ. Topological orientation of acyl-CoA:diacylglycerol acyltransferase-1 (DGAT1) and identification of a putative active site histidine and the role of the n terminus in dimer/tetramer formation. J Biol Chem 2010, 285:37377-37387. 10.1074/jbc.M110.163691, 20876538.
    • (2010) J Biol Chem , vol.285 , pp. 37377-37387
    • McFie, P.J.1    Stone, S.L.2    Banman, S.L.3    Stone, S.J.4
  • 22
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • 10.1110/ps.8.8.1668, 2144417, 10452611
    • Kapust RB, Waugh DS. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci 1999, 8:1668-1674. 10.1110/ps.8.8.1668, 2144417, 10452611.
    • (1999) Protein Sci , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 23
    • 32944473015 scopus 로고    scopus 로고
    • Identification of the anti-inflammatory protein tristetraprolin as a hyperphosphorylated protein by mass spectrometry and site-directed mutagenesis
    • 10.1042/BJ20051316, 1386027, 16262601
    • Cao H, Deterding LJ, Venable JD, Kennington EA, Yates JR, Tomer KB, Blackshear PJ. Identification of the anti-inflammatory protein tristetraprolin as a hyperphosphorylated protein by mass spectrometry and site-directed mutagenesis. Biochem J 2006, 394:285-297. 10.1042/BJ20051316, 1386027, 16262601.
    • (2006) Biochem J , vol.394 , pp. 285-297
    • Cao, H.1    Deterding, L.J.2    Venable, J.D.3    Kennington, E.A.4    Yates, J.R.5    Tomer, K.B.6    Blackshear, P.J.7
  • 24
    • 37149054919 scopus 로고    scopus 로고
    • Phosphorylation of recombinant tristetraprolin in vitro
    • 10.1007/s10930-007-9119-7, 2674330, 18071886
    • Cao H, Lin R. Phosphorylation of recombinant tristetraprolin in vitro. Protein J 2008, 27:163-169. 10.1007/s10930-007-9119-7, 2674330, 18071886.
    • (2008) Protein J , vol.27 , pp. 163-169
    • Cao, H.1    Lin, R.2
  • 25
    • 66149168939 scopus 로고    scopus 로고
    • Quantitative evaluation of His-tag purification and immunoprecipitation of tristetraprolin and its mutant proteins from transfected human cells
    • 10.1002/btpr.121, 2680604, 19330843
    • Cao H, Lin R. Quantitative evaluation of His-tag purification and immunoprecipitation of tristetraprolin and its mutant proteins from transfected human cells. Biotechnol Prog 2009, 25:461-467. 10.1002/btpr.121, 2680604, 19330843.
    • (2009) Biotechnol Prog , vol.25 , pp. 461-467
    • Cao, H.1    Lin, R.2
  • 26
    • 0033971564 scopus 로고    scopus 로고
    • Expression in yeast and tobacco of plant cDNAs encoding acyl CoA:diacylglycerol acyltransferase
    • 10.1046/j.1432-1327.2000.00961.x, 10601854
    • Bouvier-Nave P, Benveniste P, Oelkers P, Sturley SL, Schaller H. Expression in yeast and tobacco of plant cDNAs encoding acyl CoA:diacylglycerol acyltransferase. Eur J Biochem 2000, 267:85-96. 10.1046/j.1432-1327.2000.00961.x, 10601854.
    • (2000) Eur J Biochem , vol.267 , pp. 85-96
    • Bouvier-Nave, P.1    Benveniste, P.2    Oelkers, P.3    Sturley, S.L.4    Schaller, H.5
  • 27
    • 0017899242 scopus 로고
    • Triacylglycerol synthesis in lipid particles from baker's yeast (Saccharomyces cerevisiae)
    • Christiansen K. Triacylglycerol synthesis in lipid particles from baker's yeast (Saccharomyces cerevisiae). Biochim Biophys Acta 1978, 530:78-90.
    • (1978) Biochim Biophys Acta , vol.530 , pp. 78-90
    • Christiansen, K.1
  • 28
    • 0030859990 scopus 로고    scopus 로고
    • Purification and characterization of diacylglycerol acyltransferase from the lipid body fraction of an oleaginous fungus
    • Kamisaka Y, Mishra S, Nakahara T. Purification and characterization of diacylglycerol acyltransferase from the lipid body fraction of an oleaginous fungus. J Biochem 1997, 121:1107-1114.
    • (1997) J Biochem , vol.121 , pp. 1107-1114
    • Kamisaka, Y.1    Mishra, S.2    Nakahara, T.3
  • 29
    • 38849096602 scopus 로고    scopus 로고
    • Imaging of lipid biosynthesis: how a neutral lipid enters lipid droplets
    • 10.1111/j.1600-0854.2007.00689.x, 18088320
    • Kuerschner L, Moessinger C, Thiele C. Imaging of lipid biosynthesis: how a neutral lipid enters lipid droplets. Traffic 2008, 9:338-352. 10.1111/j.1600-0854.2007.00689.x, 18088320.
    • (2008) Traffic , vol.9 , pp. 338-352
    • Kuerschner, L.1    Moessinger, C.2    Thiele, C.3
  • 30
    • 0034662156 scopus 로고    scopus 로고
    • Recovery of active medium-chain-length-poly-3-hydroxyalkanoate polymerase from inactive inclusion bodies using ion-exchange resin
    • 10.1042/0264-6021:3490599, 1221183, 10880359
    • Ren Q, De RG, Kessler B, Witholt B. Recovery of active medium-chain-length-poly-3-hydroxyalkanoate polymerase from inactive inclusion bodies using ion-exchange resin. Biochem J 2000, 349:599-604. 10.1042/0264-6021:3490599, 1221183, 10880359.
    • (2000) Biochem J , vol.349 , pp. 599-604
    • Ren, Q.1    De, R.G.2    Kessler, B.3    Witholt, B.4
  • 31
    • 0013838217 scopus 로고
    • Molecular weight of the DNA in the chromosomes of E. coli and B. subtilis
    • 10.1073/pnas.54.6.1636, 300526, 4956451
    • Massie HR, Zimm BH. Molecular weight of the DNA in the chromosomes of E. coli and B. subtilis. Proc Natl Acad Sci USA 1965, 54:1636-1641. 10.1073/pnas.54.6.1636, 300526, 4956451.
    • (1965) Proc Natl Acad Sci USA , vol.54 , pp. 1636-1641
    • Massie, H.R.1    Zimm, B.H.2
  • 32
    • 27744596418 scopus 로고    scopus 로고
    • A live cell hormone-binding assay on transgenic bacteria expressing a eukaryotic receptor protein
    • 10.1016/j.ab.2005.09.012, 16246292
    • Romanov GA, Spichal L, Lomin SN, Strnad M, Schmulling T. A live cell hormone-binding assay on transgenic bacteria expressing a eukaryotic receptor protein. Anal Biochem 2005, 347:129-134. 10.1016/j.ab.2005.09.012, 16246292.
    • (2005) Anal Biochem , vol.347 , pp. 129-134
    • Romanov, G.A.1    Spichal, L.2    Lomin, S.N.3    Strnad, M.4    Schmulling, T.5
  • 33
    • 0029186042 scopus 로고
    • Bt1, a structural gene for the major 39-44 kDa amyloplast membrane polypeptides
    • Cao H, Sullivan TD, Boyer CD, Shannon JC. Bt1, a structural gene for the major 39-44 kDa amyloplast membrane polypeptides. Physiol Plant 1995, 95:176-186.
    • (1995) Physiol Plant , vol.95 , pp. 176-186
    • Cao, H.1    Sullivan, T.D.2    Boyer, C.D.3    Shannon, J.C.4
  • 34
    • 79960894226 scopus 로고    scopus 로고
    • Purification of recombinant tung tree diacylglycerol acyltransferases from E. coli
    • 10.1096/fj.10-166595, 20959516
    • Cao H, Chapital DC, Howard OD, Jiang XN, Shockey JM, Klasson KT. Purification of recombinant tung tree diacylglycerol acyltransferases from E. coli. FASEB J 2011, 25:765-8. 10.1096/fj.10-166595, 20959516.
    • (2011) FASEB J , vol.25 , pp. 765-768
    • Cao, H.1    Chapital, D.C.2    Howard, O.D.3    Jiang, X.N.4    Shockey, J.M.5    Klasson, K.T.6
  • 35
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N, Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 1987, 4:406-425.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.