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Volumn 13, Issue 1, 2014, Pages

Antisense knockdown of pyruvate dehydrogenase kinase promotes the neutral lipid accumulation in the diatom Phaeodactylum tricornutum

Author keywords

Antisense; Biofuel; Lipid; Microalga; Pyruvate dehydrogenase kinase

Indexed keywords

ALGAL PROTEIN; COMPLEMENTARY DNA; PYRUVATE DEHYDROGENASE KINASE; COMPLEMENTARY RNA; PROTEIN SERINE THREONINE KINASE; PYRUVATE DEHYDROGENASE (ACETYL-TRANSFERRING) KINASE;

EID: 84905976378     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/s12934-014-0100-9     Document Type: Article
Times cited : (91)

References (29)
  • 3
    • 43549102657 scopus 로고    scopus 로고
    • Microalgal triacylglycerols as feedstocks for biofuel production: perspectives and advances
    • Hu Q, Sommerfeld M, Jarvis E, Ghirardi M, Posewitz M, Seibert M, Darzins A. Microalgal triacylglycerols as feedstocks for biofuel production: perspectives and advances. Plant J 2008, 54:621-639. 10.1111/j.1365-313X.2008.03492.x.
    • (2008) Plant J , vol.54 , pp. 621-639
    • Hu, Q.1    Sommerfeld, M.2    Jarvis, E.3    Ghirardi, M.4    Posewitz, M.5    Seibert, M.6    Darzins, A.7
  • 4
    • 33748934377 scopus 로고    scopus 로고
    • Molecular genetic manipulation of the diatom Thalassiosira pseudonana (Bacillariophyceae)
    • Poulsen N, Chesley PM, Kro¨ger N. Molecular genetic manipulation of the diatom Thalassiosira pseudonana (Bacillariophyceae). J Phycol 2006, 42:1059-1065. 10.1111/j.1529-8817.2006.00269.x.
    • (2006) J Phycol , vol.42 , pp. 1059-1065
    • Poulsen, N.1    Chesley, P.M.2    Kro¨ger, N.3
  • 5
    • 66149134086 scopus 로고    scopus 로고
    • Research note: high efficiency transformation of the diatom Phaeodactylum tricornutum with a promoter from the diatom Cylindrotheca fusiformis
    • Miyagawa A, Okami T, Kira N, Yamaguchi H, Ohnishi K, Adachi M. Research note: high efficiency transformation of the diatom Phaeodactylum tricornutum with a promoter from the diatom Cylindrotheca fusiformis Phycol Res 2009, 57:142-146. 9.12, 10.1111/j.1440-1835.2009.00531.x.
    • (2009) Phycol Res , vol.57 , pp. 142-146
    • Miyagawa, A.1    Okami, T.2    Kira, N.3    Yamaguchi, H.4    Ohnishi, K.5    Adachi, M.6
  • 6
    • 84914163912 scopus 로고    scopus 로고
    • Activity of the mitochondrial pyruvate dehydrogenase complex in plants is stimulated in the presence of malate
    • Igamberdiev AU, Lernmark U, Gardestro¨m P: Activity of the mitochondrial pyruvate dehydrogenase complex in plants is stimulated in the presence of malate. Mitochondrion 2014,. doi:10.1016/j.mito.2014.04.006..
    • (2014) Mitochondrion
    • Igamberdiev, A.U.1    Lernmark, U.2    Gardestro¨m, P.3
  • 7
    • 0034234737 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase kinase from Arabidopsis thaliana: a protein histidine kinase that phosphorylates serine residues
    • Thelen J, Miernyk J, Randall D. Pyruvate dehydrogenase kinase from Arabidopsis thaliana: a protein histidine kinase that phosphorylates serine residues. Biochem J 2000, 349:195-201. 14.25, 10.1042/0264-6021:3490195.
    • (2000) Biochem J , vol.349 , pp. 195-201
    • Thelen, J.1    Miernyk, J.2    Randall, D.3
  • 8
    • 0037404976 scopus 로고    scopus 로고
    • Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs
    • Sugden MC, Holness MJ. Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs. Amer J Physiol-Endocrinol Metab 2003, 284:E855-E862.
    • (2003) Amer J Physiol-Endocrinol Metab , vol.284 , pp. E855-E862
    • Sugden, M.C.1    Holness, M.J.2
  • 9
    • 84864648298 scopus 로고    scopus 로고
    • Comparative homology modeling of pyruvate dehydrogenase kinase isozymes from Xenopus tropicalis reveals structural basis for their subfunctionalization
    • Tokmakov AA. Comparative homology modeling of pyruvate dehydrogenase kinase isozymes from Xenopus tropicalis reveals structural basis for their subfunctionalization. J Mol Model 2012, 18:2567-2576. 10.1007/s00894-011-1281-3.
    • (2012) J Mol Model , vol.18 , pp. 2567-2576
    • Tokmakov, A.A.1
  • 10
    • 79960283039 scopus 로고    scopus 로고
    • Cloning and functions analysis of a pyruvate dehydrogenase kinase in Brassica napus
    • Li R-J, Hu Z-Y, Zhang H-S, Zhan G-M, Wang H-Z, Hua W. Cloning and functions analysis of a pyruvate dehydrogenase kinase in Brassica napus. Plant Cell Rep 2011, 30:1533-1540. 10.1007/s00299-011-1066-2.
    • (2011) Plant Cell Rep , vol.30 , pp. 1533-1540
    • Li, R.-J.1    Hu, Z.-Y.2    Zhang, H.-S.3    Zhan, G.-M.4    Wang, H.-Z.5    Hua, W.6
  • 11
    • 84871937976 scopus 로고    scopus 로고
    • Flow cytometry for the development of biotechnological processes with microalgae
    • Hyka P, Lickova S, Pribyl P, Melzoch K, Kovar K. Flow cytometry for the development of biotechnological processes with microalgae. Biotechnol Adv 2013, 31:2-16. 10.1016/j.biotechadv.2012.04.007.
    • (2013) Biotechnol Adv , vol.31 , pp. 2-16
    • Hyka, P.1    Lickova, S.2    Pribyl, P.3    Melzoch, K.4    Kovar, K.5
  • 13
    • 0028304882 scopus 로고
    • Characteristics of the gene that encodes acetyl-CoA carboxylase in the diatom Cyclotella cryptica
    • Roessler PG, Bleibaum JL, Thompson GA, Ohlrogge JB. Characteristics of the gene that encodes acetyl-CoA carboxylase in the diatom Cyclotella cryptica Ann N Y Acad Sci 1994, 721:250-256. 10.1111/j.1749-6632.1994.tb47398.x.
    • (1994) Ann N Y Acad Sci , vol.721 , pp. 250-256
    • Roessler, P.G.1    Bleibaum, J.L.2    Thompson, G.A.3    Ohlrogge, J.B.4
  • 15
    • 9644274305 scopus 로고    scopus 로고
    • Mechanisms responsible for regulation of pyruvate dehydrogenase kinase 4 gene expression
    • Kwon H-S, Harris RA. Mechanisms responsible for regulation of pyruvate dehydrogenase kinase 4 gene expression. Adv Enzyme Regul 2004, 44:109-122. 10.1016/j.advenzreg.2003.11.020.
    • (2004) Adv Enzyme Regul , vol.44 , pp. 109-122
    • Kwon, H.-S.1    Harris, R.A.2
  • 16
  • 17
    • 0016797754 scopus 로고
    • Regulation of pyruvate dehydrogenase kinase and phosphatase by acetyl-CoA/CoA and NADH/NAD ratios
    • Pettit FH, Pelley JW, Reed LJ. Regulation of pyruvate dehydrogenase kinase and phosphatase by acetyl-CoA/CoA and NADH/NAD ratios. Biochem Biophys Res Commun 1975, 65:575-582. 10.1016/S0006-291X(75)80185-9.
    • (1975) Biochem Biophys Res Commun , vol.65 , pp. 575-582
    • Pettit, F.H.1    Pelley, J.W.2    Reed, L.J.3
  • 18
    • 70350101435 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase kinase isoenzyme 4 (PDHK4) deficiency attenuates the long-term negative effects of a high-saturated fat diet
    • Hwang B, Jeoung N, Harris R. Pyruvate dehydrogenase kinase isoenzyme 4 (PDHK4) deficiency attenuates the long-term negative effects of a high-saturated fat diet. Biochem J 2009, 423:243-252. 10.1042/BJ20090390.
    • (2009) Biochem J , vol.423 , pp. 243-252
    • Hwang, B.1    Jeoung, N.2    Harris, R.3
  • 19
    • 33845928752 scopus 로고    scopus 로고
    • Mitochondrial metabolism in developing embryos of Brassica napus
    • Schwender J, Shachar-Hill Y, Ohlrogge JB. Mitochondrial metabolism in developing embryos of Brassica napus. J Biol Chem 2006, 281:34040-34047. 10.1074/jbc.M606266200.
    • (2006) J Biol Chem , vol.281 , pp. 34040-34047
    • Schwender, J.1    Shachar-Hill, Y.2    Ohlrogge, J.B.3
  • 20
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura K, Dudley J, Nei M, Kumar S. MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 2007, 24:1596-1599. 10.1093/molbev/msm092.
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 21
    • 84966282792 scopus 로고    scopus 로고
    • Transformation of diatom Phaeodactylum tricornutum by electroporation and establishment of inducible selection marker
    • Niu YF, Yang ZK, Zhang MH, Zhu CC, Yang WD, Liu JS, Li HY: Transformation of diatom Phaeodactylum tricornutum by electroporation and establishment of inducible selection marker. Biotechniques 2012,. doi:10.2144/000113881..
    • (2012) Biotechniques
    • Niu, Y.F.1    Yang, Z.K.2    Zhang, M.H.3    Zhu, C.C.4    Yang, W.D.5    Liu, J.S.6    Li, H.Y.7
  • 22
    • 34248663955 scopus 로고    scopus 로고
    • The single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction: twenty-something years on
    • Chomczynski P, Sacchi N. The single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction: twenty-something years on. Nat Protoc 2006, 1:581-585. 10.1038/nprot.2006.83.
    • (2006) Nat Protoc , vol.1 , pp. 581-585
    • Chomczynski, P.1    Sacchi, N.2
  • 23
    • 13544265408 scopus 로고    scopus 로고
    • The use of a fluorescent dye, Nile red, to evaluate the lipid content of single mammalian oocytes
    • Genicot G, Leroy J, Soom AV, Donnay I. The use of a fluorescent dye, Nile red, to evaluate the lipid content of single mammalian oocytes. Theriogenology 2005, 63:1181-1194. 10.1016/j.theriogenology.2004.06.006.
    • (2005) Theriogenology , vol.63 , pp. 1181-1194
    • Genicot, G.1    Leroy, J.2    Soom, A.V.3    Donnay, I.4
  • 25
    • 0021729906 scopus 로고
    • Improved recovery of fatty acid through direct transesterification without prior extraction or purification
    • Lepage G, Roy CC. Improved recovery of fatty acid through direct transesterification without prior extraction or purification. J Lipid Res 1984, 25:1391-1396.
    • (1984) J Lipid Res , vol.25 , pp. 1391-1396
    • Lepage, G.1    Roy, C.C.2
  • 26
    • 0033390795 scopus 로고    scopus 로고
    • Effects of antisense repression of an Arabidopsis thaliana pyruvate dehydrogenase kinase cDNA on plant development
    • Zou J, Qi Q, Katavic V, Marillia E-F, Taylor DC. Effects of antisense repression of an Arabidopsis thaliana pyruvate dehydrogenase kinase cDNA on plant development. Plant Mol Biol 1999, 41:837-849. 17, 10.1023/A:1006393726018.
    • (1999) Plant Mol Biol , vol.41 , pp. 837-849
    • Zou, J.1    Qi, Q.2    Katavic, V.3    Marillia, E.-F.4    Taylor, D.C.5
  • 27
    • 0022260442 scopus 로고
    • Flow cytometry: present and future
    • Muirhead K, Horan P, Poste G. Flow cytometry: present and future. Nat Biotechnol 1985, 3:337-356. 10.1038/nbt0485-337.
    • (1985) Nat Biotechnol , vol.3 , pp. 337-356
    • Muirhead, K.1    Horan, P.2    Poste, G.3
  • 28
    • 79955780615 scopus 로고    scopus 로고
    • Flow cytometry, amped up
    • Benoist C, Hacohen N. Flow cytometry, amped up. Science 2011, 332:677-678. 10.1126/science.1206351.
    • (2011) Science , vol.332 , pp. 677-678
    • Benoist, C.1    Hacohen, N.2
  • 29
    • 33645235536 scopus 로고    scopus 로고
    • Development of multispecies algal bioassays using flow cytometry
    • Franklin NM, Stauber JL, Lim RP. Development of multispecies algal bioassays using flow cytometry. Environ Toxicol Chem 2004, 23:1452-1462. 10.1897/03-250.
    • (2004) Environ Toxicol Chem , vol.23 , pp. 1452-1462
    • Franklin, N.M.1    Stauber, J.L.2    Lim, R.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.