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Volumn 11, Issue 2, 2013, Pages

Reciprocal Regulation of Protein Synthesis and Carbon Metabolism for Thylakoid Membrane Biogenesis

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; ACETYL COENZYME A; DIHYDROLIPOAMIDE ACETYLTRANSFERASE; MESSENGER RNA; PYRUVATE DEHYDROGENASE COMPLEX; RECOMBINANT PROTEIN;

EID: 84874677591     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1001482     Document Type: Article
Times cited : (43)

References (84)
  • 1
    • 78649692853 scopus 로고    scopus 로고
    • On getting there from here
    • McKnight SL, (2010) On getting there from here. Science 330: 1338-1339.
    • (2010) Science , vol.330 , pp. 1338-1339
    • McKnight, S.L.1
  • 2
    • 84858796367 scopus 로고    scopus 로고
    • A two-way street: reciprocal regulation of metabolism and signalling
    • Wellen KE, Thompson CB, (2012) A two-way street: reciprocal regulation of metabolism and signalling. Nat Rev Mol Cell Biol 13: 270-276.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 270-276
    • Wellen, K.E.1    Thompson, C.B.2
  • 3
    • 84862894494 scopus 로고    scopus 로고
    • The protein acetylome and the regulation of metabolism
    • Xing S, Poirier Y, (2012) The protein acetylome and the regulation of metabolism. Trends Plant Sci 17: 423-430.
    • (2012) Trends Plant Sci , vol.17 , pp. 423-430
    • Xing, S.1    Poirier, Y.2
  • 4
    • 18744396678 scopus 로고    scopus 로고
    • A metabolic enzyme doing double duty as a transcription factor
    • Bhardwaj A, Wilkinson MF, (2005) A metabolic enzyme doing double duty as a transcription factor. Bioessays 27: 467-471.
    • (2005) Bioessays , vol.27 , pp. 467-471
    • Bhardwaj, A.1    Wilkinson, M.F.2
  • 5
    • 33645220015 scopus 로고    scopus 로고
    • Metabolic enzymes that bind RNA: yet another level of cellular regulatory network?
    • Cieśla J, (2006) Metabolic enzymes that bind RNA: yet another level of cellular regulatory network? Acta Biochim Pol 53: 11-32.
    • (2006) Acta Biochim Pol , vol.53 , pp. 11-32
    • Cieśla, J.1
  • 6
    • 70350236482 scopus 로고    scopus 로고
    • Mechanisms of lipid transport involved in organelle biogenesis in plant cells
    • Benning C, (2009) Mechanisms of lipid transport involved in organelle biogenesis in plant cells. Annu Rev Cell Dev Biol 25: 71-91.
    • (2009) Annu Rev Cell Dev Biol , vol.25 , pp. 71-91
    • Benning, C.1
  • 7
    • 0036139124 scopus 로고    scopus 로고
    • Carbon flux and fatty acid synthesis in plants
    • Rawsthorne S, (2002) Carbon flux and fatty acid synthesis in plants. Prog Lipid Res 41: 182-196.
    • (2002) Prog Lipid Res , vol.41 , pp. 182-196
    • Rawsthorne, S.1
  • 8
    • 53749097392 scopus 로고    scopus 로고
    • The role of acetyl-coenzyme A synthetase in Arabidopsis
    • Lin M, Oliver DJ, (2008) The role of acetyl-coenzyme A synthetase in Arabidopsis. Plant Physiol 147: 1822-1829.
    • (2008) Plant Physiol , vol.147 , pp. 1822-1829
    • Lin, M.1    Oliver, D.J.2
  • 10
    • 77956926954 scopus 로고    scopus 로고
    • The CO2-concentrating mechanism and carbon assimilation. The Chlamydomonas Sourcebook: Organellar and Metabolic Processes
    • Spalding MH, (2009) The CO2-concentrating mechanism and carbon assimilation. The Chlamydomonas Sourcebook: Organellar and Metabolic Processes. D B Stern, Elsevier Inc 2: 257-301.
    • (2009) D B Stern, Elsevier Inc , vol.2 , pp. 257-301
    • Spalding, M.H.1
  • 11
    • 0345074089 scopus 로고    scopus 로고
    • Regulation of pyruvate dehydrogenase complex activity in plant cells
    • Tovar-Méndez A, Miernyk JA, Randall DD, (2003) Regulation of pyruvate dehydrogenase complex activity in plant cells. Eur J Biochem 270: 1043-1049.
    • (2003) Eur J Biochem , vol.270 , pp. 1043-1049
    • Tovar-Méndez, A.1    Miernyk, J.A.2    Randall, D.D.3
  • 12
    • 79953711431 scopus 로고    scopus 로고
    • Expression of plastid genes: organelle-specific elaborations on a prokaryotic scaffold
    • Barkan A, (2011) Expression of plastid genes: organelle-specific elaborations on a prokaryotic scaffold. Plant Physiol 155: 1520-1532.
    • (2011) Plant Physiol , vol.155 , pp. 1520-1532
    • Barkan, A.1
  • 14
    • 42449103989 scopus 로고    scopus 로고
    • Coordination of gene expression between organellar and nuclear genomes
    • Woodson JD, Chory J, (2008) Coordination of gene expression between organellar and nuclear genomes. Nat Rev Genet 9: 383-395.
    • (2008) Nat Rev Genet , vol.9 , pp. 383-395
    • Woodson, J.D.1    Chory, J.2
  • 15
    • 0000325720 scopus 로고    scopus 로고
    • Subcellular visualization of gene transcripts encoding key proteins of the chlorophyll accumulation process in developing chloroplasts
    • Marrison JL, Schünmann PHD, Ougham HJ, Leech RM, (1996) Subcellular visualization of gene transcripts encoding key proteins of the chlorophyll accumulation process in developing chloroplasts. Plant Physiol 110: 1089-1096.
    • (1996) Plant Physiol , vol.110 , pp. 1089-1096
    • Marrison, J.L.1    Schünmann, P.H.D.2    Ougham, H.J.3    Leech, R.M.4
  • 16
    • 60849108324 scopus 로고    scopus 로고
    • Chloroplast protein targeting involves localized translation in Chlamydomonas
    • Uniacke J, Zerges W, (2009) Chloroplast protein targeting involves localized translation in Chlamydomonas. Proc Natl Acad Sci USA 106: 1430-1444.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1430-1444
    • Uniacke, J.1    Zerges, W.2
  • 17
    • 0036037428 scopus 로고    scopus 로고
    • A chloroplast RNA binding protein from stromal thylakoid membranes specifically binds to the 5′ untranslated region of the psbA mRNA
    • Ossenbühl F, Hartmann K, Nickelsen J, (2002) A chloroplast RNA binding protein from stromal thylakoid membranes specifically binds to the 5′ untranslated region of the psbA mRNA. Eur J Biochem 269: 3912-3919.
    • (2002) Eur J Biochem , vol.269 , pp. 3912-3919
    • Ossenbühl, F.1    Hartmann, K.2    Nickelsen, J.3
  • 18
    • 84874753507 scopus 로고    scopus 로고
    • The Chlamydomonas Sourcebook: Organellar and metabolic processes
    • Oxford, Academic Press, Elsevier Inc
    • Harris EH, (2009) The Chlamydomonas Sourcebook: Organellar and metabolic processes. D B Stern. Oxford, Academic press, Elsevier Inc pp. 2.
    • (2009) D B Stern , pp. 2
    • Harris, E.H.1
  • 19
    • 0000287479 scopus 로고
    • Composition and function of pyrenoids: cytochemical and immunocytochemical approaches
    • Michael R, McKay L, Gibbs SP, (1991) Composition and function of pyrenoids: cytochemical and immunocytochemical approaches. Can J Bot 69: 1040-1052.
    • (1991) Can J Bot , vol.69 , pp. 1040-1052
    • Michael, R.1    McKay, L.2    Gibbs, S.P.3
  • 20
    • 37849013494 scopus 로고    scopus 로고
    • Photosystem II assembly and repair are differentially localized in Chlamydomonas
    • Uniacke J, Zerges W, (2007) Photosystem II assembly and repair are differentially localized in Chlamydomonas. Plant Cell 19: 3640-3654.
    • (2007) Plant Cell , vol.19 , pp. 3640-3654
    • Uniacke, J.1    Zerges, W.2
  • 21
    • 70350051346 scopus 로고    scopus 로고
    • Protein quality control in chloroplasts: a current model of D1 protein degradation in the photosystem II repair cycle
    • Kato Y, Sakamoto W, (2009) Protein quality control in chloroplasts: a current model of D1 protein degradation in the photosystem II repair cycle. J Biochem 146: 463-469.
    • (2009) J Biochem , vol.146 , pp. 463-469
    • Kato, Y.1    Sakamoto, W.2
  • 22
    • 0032583118 scopus 로고    scopus 로고
    • Processing of the psbA 5′ untranslated region in Chlamydomonas reinhardtii depends upon factors mediating ribosome association
    • Bruick RK, Mayfield SP, (1998) Processing of the psbA 5′ untranslated region in Chlamydomonas reinhardtii depends upon factors mediating ribosome association. J Cell Biol 143: 1145-1153.
    • (1998) J Cell Biol , vol.143 , pp. 1145-1153
    • Bruick, R.K.1    Mayfield, S.P.2
  • 23
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson O, Nielsen H, Brunak S, von Heijne G, (2000) Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J Mol Biol 300: 1005-1016.
    • (2000) J Mol Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    von Heijne, G.4
  • 24
    • 66749108480 scopus 로고    scopus 로고
    • A proteomic survey of Chlamydomonas reinhardtii mitochondria sheds new light on the metabolic plasticity of the organelle and on the nature of the {alpha}-proteobacterial mitochondrial ancestor
    • Atteia A, Adrait A, Brugiere S, Tardif M, van Lis R, et al. (2009) A proteomic survey of Chlamydomonas reinhardtii mitochondria sheds new light on the metabolic plasticity of the organelle and on the nature of the {alpha}-proteobacterial mitochondrial ancestor. Mol Biol Evol 26: 1533-1548.
    • (2009) Mol Biol Evol , vol.26 , pp. 1533-1548
    • Atteia, A.1    Adrait, A.2    Brugiere, S.3    Tardif, M.4    van Lis, R.5
  • 25
    • 77954569441 scopus 로고    scopus 로고
    • Proteomic and functional characterization of a Chlamydomonas reinhardtii mutant lacking the mitochondrial alternative oxidase 1
    • Mathy G, Cardol P, Dinant M, Blomme A, Gerin S, et al. (2010) Proteomic and functional characterization of a Chlamydomonas reinhardtii mutant lacking the mitochondrial alternative oxidase 1. J Proteome Res 9: 2825-2838.
    • (2010) J Proteome Res , vol.9 , pp. 2825-2838
    • Mathy, G.1    Cardol, P.2    Dinant, M.3    Blomme, A.4    Gerin, S.5
  • 26
    • 0022373235 scopus 로고
    • Genetic reconstruction and functional analysis of the repeating lipoyl domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli
    • Guest JR, Lewis HM, Graham LD, Packman LC, Perham RN, (1985) Genetic reconstruction and functional analysis of the repeating lipoyl domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. J Mol Biol 185: 743-754.
    • (1985) J Mol Biol , vol.185 , pp. 743-754
    • Guest, J.R.1    Lewis, H.M.2    Graham, L.D.3    Packman, L.C.4    Perham, R.N.5
  • 27
    • 0033150518 scopus 로고    scopus 로고
    • Cloning and characterization of the dihydrolipoamide S-acetyltransferase subunit of the plastid pyruvate dehydrogenase complex (E2) from Arabidopsis
    • Mooney BP, Miernyk JA, Randall DD, (1999) Cloning and characterization of the dihydrolipoamide S-acetyltransferase subunit of the plastid pyruvate dehydrogenase complex (E2) from Arabidopsis. Plant Physiol 120: 443-452.
    • (1999) Plant Physiol , vol.120 , pp. 443-452
    • Mooney, B.P.1    Miernyk, J.A.2    Randall, D.D.3
  • 28
    • 0033790516 scopus 로고    scopus 로고
    • Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions
    • Perham R, (2000) Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu Rev Biochem 69: 961-1004.
    • (2000) Annu Rev Biochem , vol.69 , pp. 961-1004
    • Perham, R.1
  • 29
    • 0025370816 scopus 로고
    • Structure-function relationships in dihydrolipoamide acyltransferases
    • Reed LJ, Hackert ML, (1990) Structure-function relationships in dihydrolipoamide acyltransferases. J Biol Chem 265: 8971-8974.
    • (1990) J Biol Chem , vol.265 , pp. 8971-8974
    • Reed, L.J.1    Hackert, M.L.2
  • 30
    • 0036190131 scopus 로고    scopus 로고
    • Evolution of the enzymes of the citric acid cycle and the glyoxylate cycle of higher plants
    • Schnarrenberger C, Martin W, (2002) Evolution of the enzymes of the citric acid cycle and the glyoxylate cycle of higher plants. Eur J Biochem 269: 868-883.
    • (2002) Eur J Biochem , vol.269 , pp. 868-883
    • Schnarrenberger, C.1    Martin, W.2
  • 31
    • 0001626320 scopus 로고
    • Partial purification of intact chloroplasts from Chlamydomonas reinhardtii
    • Belknap WR, (1983) Partial purification of intact chloroplasts from Chlamydomonas reinhardtii. Plant Physiol 72: 1130-1132.
    • (1983) Plant Physiol , vol.72 , pp. 1130-1132
    • Belknap, W.R.1
  • 32
    • 0029803309 scopus 로고    scopus 로고
    • Molecular and structural changes in Chlamydomonas under limiting CO2 (a possible mitochondrial role in adaptation)
    • Geraghty AM, Spalding MH, (1996) Molecular and structural changes in Chlamydomonas under limiting CO2 (a possible mitochondrial role in adaptation). Plant Physiol 111: 1339-1347.
    • (1996) Plant Physiol , vol.111 , pp. 1339-1347
    • Geraghty, A.M.1    Spalding, M.H.2
  • 33
    • 84868193881 scopus 로고    scopus 로고
    • Enrichment of native, high molecular weight ribonucleoprotein complexes from chloroplasts by consecutive gel filtration steps
    • Schwarz C, Nickelsen J, (2010) Enrichment of native, high molecular weight ribonucleoprotein complexes from chloroplasts by consecutive gel filtration steps. Endocyt Cell Res 20: 89-94.
    • (2010) Endocyt Cell Res , vol.20 , pp. 89-94
    • Schwarz, C.1    Nickelsen, J.2
  • 34
    • 0001608023 scopus 로고
    • Characterization of photosystem II mutants of Chlamydomonas reinhardtii lacking the psbA gene
    • Bennoun P, Spierer-Herz M, Erickson J, Girard-Bascou J, Pierre Y, et al. (1986) Characterization of photosystem II mutants of Chlamydomonas reinhardtii lacking the psbA gene. Plant Mol Biol 6: 151-160.
    • (1986) Plant Mol Biol , vol.6 , pp. 151-160
    • Bennoun, P.1    Spierer-Herz, M.2    Erickson, J.3    Girard-Bascou, J.4    Pierre, Y.5
  • 35
    • 0034601028 scopus 로고    scopus 로고
    • The Nac2 gene of Chlamydomonas encodes a chloroplast TPR-like protein involved in psbD mRNA stability
    • Boudreau E, Nickelsen J, Lemaire SD, Ossenbühl F, Rochaix JD, (2000) The Nac2 gene of Chlamydomonas encodes a chloroplast TPR-like protein involved in psbD mRNA stability. EMBO J 19: 3366-3376.
    • (2000) EMBO J , vol.19 , pp. 3366-3376
    • Boudreau, E.1    Nickelsen, J.2    Lemaire, S.D.3    Ossenbühl, F.4    Rochaix, J.D.5
  • 36
    • 0034687823 scopus 로고    scopus 로고
    • Characterization of Mbb1, a nucleus-encoded tetratricopeptide-like repeat protein required for expression of the chloroplast psbB/psbT/psbH gene cluster in Chlamydomonas reinhardtii
    • Vaistij FE, Boudreau E, Lemaire SD, Goldschmidt-Clermont M, Rochaix J-D, (2000) Characterization of Mbb1, a nucleus-encoded tetratricopeptide-like repeat protein required for expression of the chloroplast psbB/psbT/psbH gene cluster in Chlamydomonas reinhardtii. Proc Natl Acad Sci USA 97: 14813-14818.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14813-14818
    • Vaistij, F.E.1    Boudreau, E.2    Lemaire, S.D.3    Goldschmidt-Clermont, M.4    Rochaix, J.-D.5
  • 37
    • 37849006499 scopus 로고    scopus 로고
    • Synthesis of the D2 protein of photosystem II in Chlamydomonas is controlled by a high molecular mass complex containing the RNA stabilization factor Nac2 and the translational activator RBP40
    • Schwarz C, Elles I, Kortmann J, Piotrowski M, Nickelsen J, (2007) Synthesis of the D2 protein of photosystem II in Chlamydomonas is controlled by a high molecular mass complex containing the RNA stabilization factor Nac2 and the translational activator RBP40. Plant Cell 19: 3627-3639.
    • (2007) Plant Cell , vol.19 , pp. 3627-3639
    • Schwarz, C.1    Elles, I.2    Kortmann, J.3    Piotrowski, M.4    Nickelsen, J.5
  • 38
    • 26944458557 scopus 로고    scopus 로고
    • CRS1, a Chloroplast Group II Intron Splicing Factor, promotes intron folding through specific interactions with two intron domains
    • Ostersetzer O, Cooke AM, Watkins KP, Barkan A, (2005) CRS1, a Chloroplast Group II Intron Splicing Factor, promotes intron folding through specific interactions with two intron domains. Plant Cell 17: 241-255.
    • (2005) Plant Cell , vol.17 , pp. 241-255
    • Ostersetzer, O.1    Cooke, A.M.2    Watkins, K.P.3    Barkan, A.4
  • 39
    • 0037276124 scopus 로고    scopus 로고
    • A 100-kD complex of two RNA-binding proteins from mitochondria of Leishmania tarentolae catalyzes RNA annealing and interacts with several RNA editing components
    • Aphasizhev R, Aphasizheva I, Nelson RE, Simpson L, (2003) A 100-kD complex of two RNA-binding proteins from mitochondria of Leishmania tarentolae catalyzes RNA annealing and interacts with several RNA editing components. RNA 9: 62-76.
    • (2003) RNA , vol.9 , pp. 62-76
    • Aphasizhev, R.1    Aphasizheva, I.2    Nelson, R.E.3    Simpson, L.4
  • 41
    • 8444222059 scopus 로고    scopus 로고
    • Tandem inverted repeat system for selection of effective transgenic RNAi strains in Chlamydomonas
    • Rohr J, Sarkar N, Balenger S, Jeong B-R, Cerutti H, (2004) Tandem inverted repeat system for selection of effective transgenic RNAi strains in Chlamydomonas. Plant J 40: 611-621.
    • (2004) Plant J , vol.40 , pp. 611-621
    • Rohr, J.1    Sarkar, N.2    Balenger, S.3    Jeong, B.-R.4    Cerutti, H.5
  • 42
    • 0000240819 scopus 로고
    • Lack of the D2 protein in a Chlamydomonas reinhardtii psbD mutant affects photosystem II stability and D1 expression
    • Erickson J, Rahire M, Malnoë P, Girard-Bascou J, Pierre Y, et al. (1986) Lack of the D2 protein in a Chlamydomonas reinhardtii psbD mutant affects photosystem II stability and D1 expression. EMBO J 5: 1745-1754.
    • (1986) EMBO J , vol.5 , pp. 1745-1754
    • Erickson, J.1    Rahire, M.2    Malnoë, P.3    Girard-Bascou, J.4    Pierre, Y.5
  • 43
    • 0000324189 scopus 로고
    • Nuclear mutations specifically affect the synthesis and/or degradation of the chloroplast-encoded D2 polypeptide of photosystem II in Chlamydomonas reinhardtii
    • Kuchka MR, Mayfield SP, Rochaix J-D, (1988) Nuclear mutations specifically affect the synthesis and/or degradation of the chloroplast-encoded D2 polypeptide of photosystem II in Chlamydomonas reinhardtii. EMBO J 7: 319-324.
    • (1988) EMBO J , vol.7 , pp. 319-324
    • Kuchka, M.R.1    Mayfield, S.P.2    Rochaix, J.-D.3
  • 44
    • 0033133576 scopus 로고    scopus 로고
    • Identification of cis-acting RNA leader elements required for chloroplast psbD gene expression in Chlamydomonas
    • Nickelsen J, Fleischmann M, Boudreau E, Rahire M, Rochaix JD, (1999) Identification of cis-acting RNA leader elements required for chloroplast psbD gene expression in Chlamydomonas. Plant Cell 11: 957-970.
    • (1999) Plant Cell , vol.11 , pp. 957-970
    • Nickelsen, J.1    Fleischmann, M.2    Boudreau, E.3    Rahire, M.4    Rochaix, J.D.5
  • 47
    • 0035914303 scopus 로고    scopus 로고
    • A trail of research from lipoic acid to α-keto acid dehydrogenase complexes
    • Reed LJ, (2001) A trail of research from lipoic acid to α-keto acid dehydrogenase complexes. J Biol Chem 276: 38329-38336.
    • (2001) J Biol Chem , vol.276 , pp. 38329-38336
    • Reed, L.J.1
  • 48
    • 84859080796 scopus 로고    scopus 로고
    • Initial steps of photosystem II de novo assembly and preloading with manganese take place in biogenesis centers in synechocystis
    • Stengel A, Gügel IL, Hilger D, Rengstl B, Jung H, et al. (2012) Initial steps of photosystem II de novo assembly and preloading with manganese take place in biogenesis centers in synechocystis. The Plant Cell Online 24: 660-675.
    • (2012) The Plant Cell Online , vol.24 , pp. 660-675
    • Stengel, A.1    Gügel, I.L.2    Hilger, D.3    Rengstl, B.4    Jung, H.5
  • 49
    • 3142655271 scopus 로고    scopus 로고
    • Identification and characterization of a novel RNA binding protein that associates with the 5′-untranslated region of the chloroplast psbA mRNA
    • Barnes D, Cohen A, Bruick RK, Kantardjieff K, Fowler S, et al. (2004) Identification and characterization of a novel RNA binding protein that associates with the 5′-untranslated region of the chloroplast psbA mRNA. Biochemistry 43: 8541-8550.
    • (2004) Biochemistry , vol.43 , pp. 8541-8550
    • Barnes, D.1    Cohen, A.2    Bruick, R.K.3    Kantardjieff, K.4    Fowler, S.5
  • 50
    • 84868214112 scopus 로고    scopus 로고
    • An intermolecular disulfide-based light switch for chloroplast psbD gene expression in Chlamydomonas reinhardtii
    • Schwarz C, Bohne A-V, Wang F, Cejudo FJ, Nickelsen J, (2012) An intermolecular disulfide-based light switch for chloroplast psbD gene expression in Chlamydomonas reinhardtii. Plant J 72: 378-389.
    • (2012) Plant J , vol.72 , pp. 378-389
    • Schwarz, C.1    Bohne, A.-V.2    Wang, F.3    Cejudo, F.J.4    Nickelsen, J.5
  • 51
    • 0029037052 scopus 로고
    • Nucleic acid-binding metabolic enzymes: living fossils of stereochemical interactions
    • Kyrpides N, Ouzounis C, (1995) Nucleic acid-binding metabolic enzymes: living fossils of stereochemical interactions. J Mol Evol 40: 564-569.
    • (1995) J Mol Evol , vol.40 , pp. 564-569
    • Kyrpides, N.1    Ouzounis, C.2
  • 52
    • 77954711237 scopus 로고    scopus 로고
    • Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry and hierarchical clustering
    • Olinares PDB, Ponnola L, van Wijk KJ, (2010) Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry and hierarchical clustering. Mol Cell Proteomics 9: 1594-1615.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 1594-1615
    • Olinares, P.D.B.1    Ponnola, L.2    van Wijk, K.J.3
  • 53
    • 44749084800 scopus 로고    scopus 로고
    • Arabidopsis thaliana mutants reveal a role for CSP41a and CSP41b, two ribosome-associated endonucleases, in chloroplast ribosomal RNA metabolism
    • Beligni MV, Mayfield SP, (2008) Arabidopsis thaliana mutants reveal a role for CSP41a and CSP41b, two ribosome-associated endonucleases, in chloroplast ribosomal RNA metabolism. Plant Mol Biol 67: 389-401.
    • (2008) Plant Mol Biol , vol.67 , pp. 389-401
    • Beligni, M.V.1    Mayfield, S.P.2
  • 54
    • 60549092086 scopus 로고    scopus 로고
    • The RNA-binding proteins CSP41a and CSP41b may regulate transcription and translation of chloroplast-encoded RNAs in Arabidopsis
    • Bollenbach TJ, Sharwood RE, Gutierrez R, Lerbs-Mache S, Stern DB, (2009) The RNA-binding proteins CSP41a and CSP41b may regulate transcription and translation of chloroplast-encoded RNAs in Arabidopsis. Plant Mol Biol 69: 541-552.
    • (2009) Plant Mol Biol , vol.69 , pp. 541-552
    • Bollenbach, T.J.1    Sharwood, R.E.2    Gutierrez, R.3    Lerbs-Mache, S.4    Stern, D.B.5
  • 55
    • 84856865331 scopus 로고    scopus 로고
    • Arabidopsis CSP41 proteins form multimeric complexes that bind and stabilize distinct plastid transcripts
    • Qi Y, Armbruster U, Schmitz-Linneweber C, Delannoy E, de Longevialle AF, et al. (2011) Arabidopsis CSP41 proteins form multimeric complexes that bind and stabilize distinct plastid transcripts. J Exp Bot 63: 1251-1270.
    • (2011) J Exp Bot , vol.63 , pp. 1251-1270
    • Qi, Y.1    Armbruster, U.2    Schmitz-Linneweber, C.3    Delannoy, E.4    de Longevialle, A.F.5
  • 56
    • 77954276698 scopus 로고    scopus 로고
    • Disruption of ptLPD1 or ptLPD2, genes that encode isoforms of the plastidial lipoamide dehydrogenase, confers arsenate hypersensitivity in Arabidopsis
    • Chen W, Chi Y, Taylor NL, Lambers H, Finnegan PM, (2010) Disruption of ptLPD1 or ptLPD2, genes that encode isoforms of the plastidial lipoamide dehydrogenase, confers arsenate hypersensitivity in Arabidopsis. Plant Physiol 153: 1385-1397.
    • (2010) Plant Physiol , vol.153 , pp. 1385-1397
    • Chen, W.1    Chi, Y.2    Taylor, N.L.3    Lambers, H.4    Finnegan, P.M.5
  • 57
    • 0041693996 scopus 로고    scopus 로고
    • Disruption of plE2, the gene for the E2 subunit of the plastid pyruvate dehydrogenase complex, in Arabidopsis causes an early embryo lethal phenotype
    • Lin M, Behal R, Oliver DJ, (2003) Disruption of plE2, the gene for the E2 subunit of the plastid pyruvate dehydrogenase complex, in Arabidopsis causes an early embryo lethal phenotype. Plant Mol Biol 52: 865-872.
    • (2003) Plant Mol Biol , vol.52 , pp. 865-872
    • Lin, M.1    Behal, R.2    Oliver, D.J.3
  • 58
    • 70350217260 scopus 로고    scopus 로고
    • Integrating the genetic and physical maps of Arabidopsis thaliana: identification of mapped alleles of cloned essential (EMB) genes
    • doi:10.1371/journal.pone.0007386
    • Meinke D, Sweeney C, Muralla R, (2009) Integrating the genetic and physical maps of Arabidopsis thaliana: identification of mapped alleles of cloned essential (EMB) genes. PLoS ONE 4: e7386 doi:10.1371/journal.pone.0007386.
    • (2009) PLoS ONE , vol.4
    • Meinke, D.1    Sweeney, C.2    Muralla, R.3
  • 59
    • 82755187254 scopus 로고    scopus 로고
    • Strategies for psbA gene expression in cyanobacteria, green algae and higher plants: From transcription to PSII repair
    • Mulo P, Sakurai I, Aro E-M, (2012) Strategies for psbA gene expression in cyanobacteria, green algae and higher plants: From transcription to PSII repair. Biochimica et Biophysica Acta (BBA)-Bioenergetics 1817: 247-257.
    • (2012) Biochimica Et Biophysica Acta (BBA)-Bioenergetics , vol.1817 , pp. 247-257
    • Mulo, P.1    Sakurai, I.2    Aro, E.-M.3
  • 60
    • 0035909958 scopus 로고    scopus 로고
    • The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes
    • Zhou ZH, McCarthy DB, O'Connor CM, Reed LJ, Stoops JK, (2001) The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes. Proc Natl Acad Sci U S A 98: 14802-14807.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 14802-14807
    • Zhou, Z.H.1    McCarthy, D.B.2    O'Connor, C.M.3    Reed, L.J.4    Stoops, J.K.5
  • 61
    • 0001028416 scopus 로고
    • Purification and characterization of the pea chloroplast pyruvate dehydrogenase complex: a source of acetyl-CoA and NADH for fatty acid biosynthesis
    • Camp PJ, Randall DD, (1985) Purification and characterization of the pea chloroplast pyruvate dehydrogenase complex: a source of acetyl-CoA and NADH for fatty acid biosynthesis. Plant Physiol 77: 571-577.
    • (1985) Plant Physiol , vol.77 , pp. 571-577
    • Camp, P.J.1    Randall, D.D.2
  • 62
    • 0025148803 scopus 로고
    • Translational regulation of chloroplast gene expression during the light-dark cell cycle of Chlamydomonas: evidence for control by ATP/energy supply
    • Michaels A, Herrin DL, (1990) Translational regulation of chloroplast gene expression during the light-dark cell cycle of Chlamydomonas: evidence for control by ATP/energy supply. Biochem Biophys Res Commun 170: 1082-1088.
    • (1990) Biochem Biophys Res Commun , vol.170 , pp. 1082-1088
    • Michaels, A.1    Herrin, D.L.2
  • 63
    • 78649451048 scopus 로고    scopus 로고
    • Mitochondrial translocation of signal transducer and activator of transcription 5 (STAT5) in leukemic T cells and cytokine-stimulated cells
    • Chueh F-Y, Leong K-F, Yu C-L, (2010) Mitochondrial translocation of signal transducer and activator of transcription 5 (STAT5) in leukemic T cells and cytokine-stimulated cells. Biochem Biophys Res Commun 402: 778-783.
    • (2010) Biochem Biophys Res Commun , vol.402 , pp. 778-783
    • Chueh, F.-Y.1    Leong, K.-F.2    Yu, C.-L.3
  • 64
    • 79954414352 scopus 로고    scopus 로고
    • Nuclear localization of pyruvate dehydrogenase complex-E2 (PDC-E2), a mitochondrial enzyme, and its role in signal transducer and activator of transcription 5 (STAT5)-dependent gene transcription
    • Chueh F-Y, Leong K-F, Cronk RJ, Venkitachalam S, Pabich S, et al. (2011) Nuclear localization of pyruvate dehydrogenase complex-E2 (PDC-E2), a mitochondrial enzyme, and its role in signal transducer and activator of transcription 5 (STAT5)-dependent gene transcription. Cellular Signalling 23: 1170-1178.
    • (2011) Cellular Signalling , vol.23 , pp. 1170-1178
    • Chueh, F.-Y.1    Leong, K.-F.2    Cronk, R.J.3    Venkitachalam, S.4    Pabich, S.5
  • 65
    • 0015834475 scopus 로고
    • Comparison of super-secondary structures in proteins
    • Rao ST, Rossmann MG, (1973) Comparison of super-secondary structures in proteins. J Mol Biol 76: 241-256.
    • (1973) J Mol Biol , vol.76 , pp. 241-256
    • Rao, S.T.1    Rossmann, M.G.2
  • 67
    • 0034726714 scopus 로고    scopus 로고
    • Identification of the NAD+-binding fold of glyceraldehyde-3-phosphate dehydrogenase as a novel RNA-binding domain
    • Nagy E, Henics T, Eckert M, Miseta A, Lightowlers RN, et al. (2000) Identification of the NAD+-binding fold of glyceraldehyde-3-phosphate dehydrogenase as a novel RNA-binding domain. Biochem Biophys Res Commun 275: 253-260.
    • (2000) Biochem Biophys Res Commun , vol.275 , pp. 253-260
    • Nagy, E.1    Henics, T.2    Eckert, M.3    Miseta, A.4    Lightowlers, R.N.5
  • 68
    • 0028816615 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase selectively binds AU-rich RNA in the NAD-binding region (Rossmann Fold)
    • Nagy E, Rigby WFC, (1995) Glyceraldehyde-3-phosphate dehydrogenase selectively binds AU-rich RNA in the NAD-binding region (Rossmann Fold). J Biol Chem 270: 2755-2763.
    • (1995) J Biol Chem , vol.270 , pp. 2755-2763
    • Nagy, E.1    Rigby, W.F.C.2
  • 70
    • 62149107922 scopus 로고    scopus 로고
    • Generation of Chlamydomonas strains that efficiently express nuclear transgenes
    • Neupert J, Karcher D, Bock R, (2009) Generation of Chlamydomonas strains that efficiently express nuclear transgenes. Plant J 57: 1140-1150.
    • (2009) Plant J , vol.57 , pp. 1140-1150
    • Neupert, J.1    Karcher, D.2    Bock, R.3
  • 71
    • 0031953257 scopus 로고    scopus 로고
    • Low density membranes are associated with RNA-binding proteins and thylakoids in the chloroplast of Chlamydomonas reinhardtii
    • Zerges W, Rochaix J-D, (1998) Low density membranes are associated with RNA-binding proteins and thylakoids in the chloroplast of Chlamydomonas reinhardtii. J Cell Biol 140: 101-110.
    • (1998) J Cell Biol , vol.140 , pp. 101-110
    • Zerges, W.1    Rochaix, J.-D.2
  • 72
    • 33745189662 scopus 로고    scopus 로고
    • Cyanide metabolism in higher plants: Cyanoalanine hydratase is a NIT4 homolog
    • Piotrowski M, Volmer J, (2006) Cyanide metabolism in higher plants: Cyanoalanine hydratase is a NIT4 homolog. Plant Mol Biol 61: 111-122.
    • (2006) Plant Mol Biol , vol.61 , pp. 111-122
    • Piotrowski, M.1    Volmer, J.2
  • 73
    • 0029110550 scopus 로고
    • Isolation, purification, and characterization of mitochondria from Chlamydomonas reinhardtii
    • Eriksson M, Gardestrom P, Samuelsson G, (1995) Isolation, purification, and characterization of mitochondria from Chlamydomonas reinhardtii. Plant Physiol 107: 479-483.
    • (1995) Plant Physiol , vol.107 , pp. 479-483
    • Eriksson, M.1    Gardestrom, P.2    Samuelsson, G.3
  • 74
    • 0034888190 scopus 로고    scopus 로고
    • The flanking regions of PsaD drive efficient gene expression in the nucleus of the green alga Chlamydomonas reinhardtii
    • Fischer N, Rochaix JD, (2001) The flanking regions of PsaD drive efficient gene expression in the nucleus of the green alga Chlamydomonas reinhardtii. Mol Genet Genomics 265: 888-894.
    • (2001) Mol Genet Genomics , vol.265 , pp. 888-894
    • Fischer, N.1    Rochaix, J.D.2
  • 75
    • 0033179996 scopus 로고    scopus 로고
    • A synthetic gene coding for the green fluorescent protein (GFP) is a versatile reporter in Chlamydomonas reinhardtii
    • Fuhrmann M, Oertel W, Hegemann P, (1999) A synthetic gene coding for the green fluorescent protein (GFP) is a versatile reporter in Chlamydomonas reinhardtii. Plant J 19: 353-361.
    • (1999) Plant J , vol.19 , pp. 353-361
    • Fuhrmann, M.1    Oertel, W.2    Hegemann, P.3
  • 76
    • 0036690768 scopus 로고    scopus 로고
    • Sequence elements within an HSP70 promoter counteract transcriptional transgene silencing in Chlamydomonas
    • Schroda M, Beck CF, Vallon O, (2002) Sequence elements within an HSP70 promoter counteract transcriptional transgene silencing in Chlamydomonas. Plant J 31: 445-455.
    • (2002) Plant J , vol.31 , pp. 445-455
    • Schroda, M.1    Beck, C.F.2    Vallon, O.3
  • 77
    • 0342680049 scopus 로고    scopus 로고
    • The HSP70A promoter as a tool for the improved expression of transgenes in Chlamydomonas
    • Schroda M, Blöcker D, Beck CF, (2000) The HSP70A promoter as a tool for the improved expression of transgenes in Chlamydomonas. Plant J 21: 121-131.
    • (2000) Plant J , vol.21 , pp. 121-131
    • Schroda, M.1    Blöcker, D.2    Beck, C.F.3
  • 78
    • 79960073967 scopus 로고    scopus 로고
    • FISH and immunofluorescence staining in Chlamydomonas. RNA detection and visualization
    • Uniacke J, Colón-Ramos D, Zerges W, (2011) FISH and immunofluorescence staining in Chlamydomonas. RNA detection and visualization. J E Gerst, Humana Press 714: 15-29.
    • (2011) J E Gerst , vol.714 , pp. 15-29
    • Uniacke, J.1    Colón-Ramos, D.2    Zerges, W.3
  • 79
    • 0030479790 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase complex and acetyl-CoA carboxylase in pea root plastids: their characterization and role in modulating glycolytic carbon flow to fatty acid biosynthesis
    • Qi Q, Trimming BA, Kleppinger-Sparace KF, Emes MJ, Sparace SA, (1996) Pyruvate dehydrogenase complex and acetyl-CoA carboxylase in pea root plastids: their characterization and role in modulating glycolytic carbon flow to fatty acid biosynthesis. J Exp Bot 47: 1889-1896.
    • (1996) J Exp Bot , vol.47 , pp. 1889-1896
    • Qi, Q.1    Trimming, B.A.2    Kleppinger-Sparace, K.F.3    Emes, M.J.4    Sparace, S.A.5
  • 80
    • 0001457057 scopus 로고
    • Pyruvate dehydrogenase complex from higher plant mitochondria and proplastids
    • Reid EE, Thompson P, Lyttle CR, Dennis DT, (1977) Pyruvate dehydrogenase complex from higher plant mitochondria and proplastids. Plant Physiol 59: 842-848.
    • (1977) Plant Physiol , vol.59 , pp. 842-848
    • Reid, E.E.1    Thompson, P.2    Lyttle, C.R.3    Dennis, D.T.4
  • 82
  • 83
    • 79958732507 scopus 로고    scopus 로고
    • An intermediate membrane subfraction in cyanobacteria is involved in an assembly network for photosystem II biogenesis
    • Rengstl B, Oster U, Stengel A, Nickelsen J, (2011) An intermediate membrane subfraction in cyanobacteria is involved in an assembly network for photosystem II biogenesis. J Biol Chem 286: 21944-21951.
    • (2011) J Biol Chem , vol.286 , pp. 21944-21951
    • Rengstl, B.1    Oster, U.2    Stengel, A.3    Nickelsen, J.4


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