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Volumn 150, Issue 2, 2014, Pages 252-270

Phosphoproteomic analysis of chromoplasts from sweet orange during fruit ripening

Author keywords

[No Author keywords available]

Indexed keywords

CITRUS; CITRUS SINENSIS;

EID: 84892483182     PISSN: 00319317     EISSN: 13993054     Source Type: Journal    
DOI: 10.1111/ppl.12080     Document Type: Article
Times cited : (19)

References (66)
  • 1
    • 0035413606 scopus 로고    scopus 로고
    • Kinetic and catalytic mechanisms of protein kinases
    • Adams JA (2001) Kinetic and catalytic mechanisms of protein kinases. Chem Rev 101: 2271-2290
    • (2001) Chem Rev , vol.101 , pp. 2271-2290
    • Adams, J.A.1
  • 2
    • 85046915977 scopus 로고    scopus 로고
    • Modifications at the A-domain of the chloroplast import receptor Toc159
    • Agne B, Kessler F (2010) Modifications at the A-domain of the chloroplast import receptor Toc159. Plant Signal Behav 5: 1513-1516
    • (2010) Plant Signal Behav , vol.5 , pp. 1513-1516
    • Agne, B.1    Kessler, F.2
  • 6
    • 71249130462 scopus 로고    scopus 로고
    • The chloroplast kinase network: new insights from large-scale phosphoproteome profiling
    • Baginsky S, Gruissem W (2009) The chloroplast kinase network: new insights from large-scale phosphoproteome profiling. Mol Plant 2: 1141-1153
    • (2009) Mol Plant , vol.2 , pp. 1141-1153
    • Baginsky, S.1    Gruissem, W.2
  • 8
    • 84857949481 scopus 로고    scopus 로고
    • Chloroplast-localized protein kinases: a step forward towards a complete inventory
    • Bayer RG, Stael S, Rocha AG, Mair A, Vothknecht UC, Teige M (2012) Chloroplast-localized protein kinases: a step forward towards a complete inventory. J Exp Bot 63: 1713-1723
    • (2012) J Exp Bot , vol.63 , pp. 1713-1723
    • Bayer, R.G.1    Stael, S.2    Rocha, A.G.3    Mair, A.4    Vothknecht, U.C.5    Teige, M.6
  • 12
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
    • Blom N, Sicheritz-Pontén T, Gupta R, Gammeltoft S, Brunak S (2004) Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics 4: 1633-1649
    • (2004) Proteomics , vol.4 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Pontén, T.2    Gupta, R.3    Gammeltoft, S.4    Brunak, S.5
  • 13
    • 71249161231 scopus 로고    scopus 로고
    • Proteomic analysis of the proplastid envelope membrane provides novel insights into small molecule and protein transport across proplastid membranes
    • Brautigam A, Weber AP (2009) Proteomic analysis of the proplastid envelope membrane provides novel insights into small molecule and protein transport across proplastid membranes. Mol Plant 2: 1247-1261
    • (2009) Mol Plant , vol.2 , pp. 1247-1261
    • Brautigam, A.1    Weber, A.P.2
  • 15
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias JE, Gygi SP (2007) Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat Methods 4: 207-214
    • (2007) Nat Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 16
    • 84859164078 scopus 로고    scopus 로고
    • Nitrate and ammonium lead to distinct global dynamic phosphorylation patterns when resupplied to nitrogen-starved Arabidopsis seedlings
    • Engelsberger WR, Schulze WX (2012) Nitrate and ammonium lead to distinct global dynamic phosphorylation patterns when resupplied to nitrogen-starved Arabidopsis seedlings. Plant J 69: 978-995
    • (2012) Plant J , vol.69 , pp. 978-995
    • Engelsberger, W.R.1    Schulze, W.X.2
  • 18
    • 78650988662 scopus 로고    scopus 로고
    • Ascorbate and glutathione: the heart of the redox hub
    • Foyer CH, Noctor G (2011) Ascorbate and glutathione: the heart of the redox hub. Plant Physiol 155: 2-18
    • (2011) Plant Physiol , vol.155 , pp. 2-18
    • Foyer, C.H.1    Noctor, G.2
  • 19
    • 77949565231 scopus 로고    scopus 로고
    • Reconstruction of metabolic pathways, protein expression, and homeostasis machineries across maize bundle sheath and mesophyll chloroplasts: large-scale quantitative proteomics using the first maize genome assembly
    • Friso G, Majeran W, Huang M, Sun Q, van Wijk KJ (2010) Reconstruction of metabolic pathways, protein expression, and homeostasis machineries across maize bundle sheath and mesophyll chloroplasts: large-scale quantitative proteomics using the first maize genome assembly. Plant Physiol 152: 1219-1250
    • (2010) Plant Physiol , vol.152 , pp. 1219-1250
    • Friso, G.1    Majeran, W.2    Huang, M.3    Sun, Q.4    van Wijk, K.J.5
  • 20
    • 59349086947 scopus 로고    scopus 로고
    • Protein tyrosine phosphorylation in plants: more abundant than expected?
    • de la Fuente van Bentem S, Hirt H (2009) Protein tyrosine phosphorylation in plants: more abundant than expected? Trends Plant Sci 14: 71-76
    • (2009) Trends Plant Sci , vol.14 , pp. 71-76
    • de la Fuente van Bentem, S.1    Hirt, H.2
  • 21
    • 0037088638 scopus 로고    scopus 로고
    • The chloroplast protein import receptors Toc34 and Toc159 are phosphorylated by distinct protein kinases
    • Fulgosi H, Soll J (2002) The chloroplast protein import receptors Toc34 and Toc159 are phosphorylated by distinct protein kinases. J Biol Chem 277: 8934-8940
    • (2002) J Biol Chem , vol.277 , pp. 8934-8940
    • Fulgosi, H.1    Soll, J.2
  • 22
    • 45849140875 scopus 로고    scopus 로고
    • Structure and dynamics of photosystem II light-harvesting complex revealed by high-resolution FTICR mass spectrometric proteome analysis
    • Galetskiy D, Susnea I, Reiser V, Adamska I, Przybylski M (2008) Structure and dynamics of photosystem II light-harvesting complex revealed by high-resolution FTICR mass spectrometric proteome analysis. J Am Soc Mass Spectrom 19: 1004-1013
    • (2008) J Am Soc Mass Spectrom , vol.19 , pp. 1004-1013
    • Galetskiy, D.1    Susnea, I.2    Reiser, V.3    Adamska, I.4    Przybylski, M.5
  • 26
    • 1842546738 scopus 로고    scopus 로고
    • Identification of three previously unknown in vivo protein phosphorylation sites in thylakoid membranes of Arabidopsis thaliana
    • Hansson M, Vener AV (2003) Identification of three previously unknown in vivo protein phosphorylation sites in thylakoid membranes of Arabidopsis thaliana. Mol Cell Proteomics 2: 550-559
    • (2003) Mol Cell Proteomics , vol.2 , pp. 550-559
    • Hansson, M.1    Vener, A.V.2
  • 28
    • 47249152709 scopus 로고    scopus 로고
    • Targeting of nucleus-encoded proteins to chloroplasts in plants
    • Jarvis P (2008) Targeting of nucleus-encoded proteins to chloroplasts in plants. New Phytol 179: 257-285
    • (2008) New Phytol , vol.179 , pp. 257-285
    • Jarvis, P.1
  • 29
    • 33745800293 scopus 로고    scopus 로고
    • Interpreting the protein language using proteomics
    • Jensen ON (2006) Interpreting the protein language using proteomics. Nat Rev Mol Cell Biol 7: 391-403
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 391-403
    • Jensen, O.N.1
  • 30
    • 33750117539 scopus 로고    scopus 로고
    • Analysis of the defence phosphoproteome of Arabidopsis thaliana using differential mass tagging
    • Jones AME, Bennett MH, Mansfield JW, Grant M (2006) Analysis of the defence phosphoproteome of Arabidopsis thaliana using differential mass tagging. Proteomics 6: 4155-4165
    • (2006) Proteomics , vol.6 , pp. 4155-4165
    • Jones, A.M.E.1    Bennett, M.H.2    Mansfield, J.W.3    Grant, M.4
  • 33
    • 0028866903 scopus 로고
    • Crystal structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from Leishmania mexicana: implications for structure-based drug design and a new position for the inorganic phosphate binding site
    • Kim H, Feil IK, Verlinde CL, Petra PH, Hol WG (1995) Crystal structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from Leishmania mexicana: implications for structure-based drug design and a new position for the inorganic phosphate binding site. Biochemistry 34: 14975-14986
    • (1995) Biochemistry , vol.34 , pp. 14975-14986
    • Kim, H.1    Feil, I.K.2    Verlinde, C.L.3    Petra, P.H.4    Hol, W.G.5
  • 34
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen MR, Thingholm TE, Jensen ON, Roepstorff P, Jørgensen TJ (2005) Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol Cell Proteomics 4: 873-886
    • (2005) Mol Cell Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jørgensen, T.J.5
  • 36
    • 77949293684 scopus 로고    scopus 로고
    • Phosphopeptide enrichment using metal oxide affinity chromatography
    • Leitner A (2010) Phosphopeptide enrichment using metal oxide affinity chromatography. TrAC Trends Analyt Chem 29: 177-185
    • (2010) TrAC Trends Analyt Chem , vol.29 , pp. 177-185
    • Leitner, A.1
  • 37
    • 40049091938 scopus 로고    scopus 로고
    • A novel bud mutation that confers abnormal patterns of lycopene accumulation in sweet orange fruit (Citrus sinensis L. Osbeck)
    • Liu Q, Xu J, Liu Y, Zhao X, Deng X, Guo L, Gu J (2007) A novel bud mutation that confers abnormal patterns of lycopene accumulation in sweet orange fruit (Citrus sinensis L. Osbeck). J Exp Bot 58: 4161-4171
    • (2007) J Exp Bot , vol.58 , pp. 4161-4171
    • Liu, Q.1    Xu, J.2    Liu, Y.3    Zhao, X.4    Deng, X.5    Guo, L.6    Gu, J.7
  • 38
    • 63349112495 scopus 로고    scopus 로고
    • Phosphorylation site mapping of soluble proteins: bioinformatical filtering reveals potential plastidic phosphoproteins in Arabidopsis thaliana
    • Lohrig K, Muller B, Davydova J, Leister D, Wolters DA (2009) Phosphorylation site mapping of soluble proteins: bioinformatical filtering reveals potential plastidic phosphoproteins in Arabidopsis thaliana. Planta 229: 1123-1134
    • (2009) Planta , vol.229 , pp. 1123-1134
    • Lohrig, K.1    Muller, B.2    Davydova, J.3    Leister, D.4    Wolters, D.A.5
  • 39
    • 65249137629 scopus 로고    scopus 로고
    • Global and site-specific quantitative phosphoproteomics: principles and applications
    • Macek B, Mann M, Olsen JV (2009) Global and site-specific quantitative phosphoproteomics: principles and applications. Annu Rev Pharmacol 49: 199-221
    • (2009) Annu Rev Pharmacol , vol.49 , pp. 199-221
    • Macek, B.1    Mann, M.2    Olsen, J.V.3
  • 40
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann M, Jensen ON (2003) Proteomic analysis of post-translational modifications. Nat Biotechnol 21: 255-261
    • (2003) Nat Biotechnol , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 41
    • 84860549883 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of seed maturation in Arabidopsis, rapeseed, and soybean
    • Meyer LJ, Gao J, Xu D, Thelen JJ (2012) Phosphoproteomic analysis of seed maturation in Arabidopsis, rapeseed, and soybean. Plant Physiol 159: 517-528
    • (2012) Plant Physiol , vol.159 , pp. 517-528
    • Meyer, L.J.1    Gao, J.2    Xu, D.3    Thelen, J.J.4
  • 45
    • 35648996970 scopus 로고    scopus 로고
    • Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis
    • Niittyla T, Fuglsang AT, Palmgren MG, Frommer WB, Schulze WX (2007) Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis. Mol Cell Proteomics 6: 1711-1726
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1711-1726
    • Niittyla, T.1    Fuglsang, A.T.2    Palmgren, M.G.3    Frommer, W.B.4    Schulze, W.X.5
  • 46
    • 11444263845 scopus 로고    scopus 로고
    • Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry
    • Nuhse TS, Stensballe A, Jensen ON, Peck SC (2003) Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry. Mol Cell Proteomics 2: 1234-1243
    • (2003) Mol Cell Proteomics , vol.2 , pp. 1234-1243
    • Nuhse, T.S.1    Stensballe, A.2    Jensen, O.N.3    Peck, S.C.4
  • 47
    • 4544291080 scopus 로고    scopus 로고
    • Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database
    • Nuhse TS, Stensballe A, Jensen ON, Peck SC (2004) Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database. Plant Cell 16: 2394-2405
    • (2004) Plant Cell , vol.16 , pp. 2394-2405
    • Nuhse, T.S.1    Stensballe, A.2    Jensen, O.N.3    Peck, S.C.4
  • 48
    • 48649104944 scopus 로고    scopus 로고
    • Phosphorylation regulates the assembly of chloroplast import machinery
    • Oreb M, Höfle A, Mirus O, Schleiff E (2008) Phosphorylation regulates the assembly of chloroplast import machinery. J Exp Bot 59: 2309-2316
    • (2008) J Exp Bot , vol.59 , pp. 2309-2316
    • Oreb, M.1    Höfle, A.2    Mirus, O.3    Schleiff, E.4
  • 49
    • 79960145005 scopus 로고    scopus 로고
    • Nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase is phosphorylated in wheat endosperm at serine-404 by an SNF1-related protein kinase allosterically inhibited by ribose-5-phosphate
    • Piattoni CV, Bustos DM, Guerrero SA, Iglesias AÁ (2011) Nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase is phosphorylated in wheat endosperm at serine-404 by an SNF1-related protein kinase allosterically inhibited by ribose-5-phosphate. Plant Physiol 156: 1337-1350
    • (2011) Plant Physiol , vol.156 , pp. 1337-1350
    • Piattoni, C.V.1    Bustos, D.M.2    Guerrero, S.A.3    Iglesias, A.A.4
  • 50
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns
    • Pinkse MWH, Uitto PM, Hilhorst MJ, Ooms B, Heck AJR (2004) Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns. Anal Chem 76: 3935-3943
    • (2004) Anal Chem , vol.76 , pp. 3935-3943
    • Pinkse, M.W.H.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.R.5
  • 53
    • 33645779695 scopus 로고    scopus 로고
    • Novel protein phosphorylation site identification in spinach stroma membranes by titanium dioxide microcolumns and tandem mass spectrometry
    • Rinalducci S, Larsen MR, Mohammed S, Zolla L (2006) Novel protein phosphorylation site identification in spinach stroma membranes by titanium dioxide microcolumns and tandem mass spectrometry. J Proteome Res 5: 973-982
    • (2006) J Proteome Res , vol.5 , pp. 973-982
    • Rinalducci, S.1    Larsen, M.R.2    Mohammed, S.3    Zolla, L.4
  • 54
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • Schwartz D, Gygi SP (2005) An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nat Biotechnol 23: 1391-1398
    • (2005) Nat Biotechnol , vol.23 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 56
    • 79961026999 scopus 로고    scopus 로고
    • Fibrillin protein function: the tip of the iceberg?
    • Singh DK, McNellis TW (2011) Fibrillin protein function: the tip of the iceberg? Trends Plant Sci 16: 432-441
    • (2011) Trends Plant Sci , vol.16 , pp. 432-441
    • Singh, D.K.1    McNellis, T.W.2
  • 58
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28: 2731-2739
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 59
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 60
    • 0036479109 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Cι/λ and plays a role in microtubule dynamics in the early secretory pathway
    • Tisdale EJ (2002) Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Cι/λ and plays a role in microtubule dynamics in the early secretory pathway. J Biol Chem 277: 3334-3341
    • (2002) J Biol Chem , vol.277 , pp. 3334-3341
    • Tisdale, E.J.1
  • 61
    • 0035831456 scopus 로고    scopus 로고
    • Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana
    • Vener AV, Harms A, Sussman MR, Vierstra RD (2001) Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana. J Biol Chem 276: 6959-6966
    • (2001) J Biol Chem , vol.276 , pp. 6959-6966
    • Vener, A.V.1    Harms, A.2    Sussman, M.R.3    Vierstra, R.D.4
  • 63
    • 52649124306 scopus 로고    scopus 로고
    • A proteomic and phosphoproteomic analysis of Oryza sativa plasma membrane and vacuolar membrane
    • Whiteman SA, Nühse TS, Ashford DA, Sanders D, Maathuis FJM (2008a) A proteomic and phosphoproteomic analysis of Oryza sativa plasma membrane and vacuolar membrane. Plant J 56: 146-156
    • (2008) Plant J , vol.56 , pp. 146-156
    • Whiteman, S.A.1    Nühse, T.S.2    Ashford, D.A.3    Sanders, D.4    Maathuis, F.J.M.5
  • 64
    • 52649180552 scopus 로고    scopus 로고
    • Identification of novel proteins and phosphorylation sites in a tonoplast enriched membrane fraction of Arabidopsis thaliana
    • Whiteman SA, Serazetdinova L, Jones AME, Sanders D, Rathjen J, Peck SC, Maathuis FJM (2008b) Identification of novel proteins and phosphorylation sites in a tonoplast enriched membrane fraction of Arabidopsis thaliana. Proteomics 8: 3536-3547
    • (2008) Proteomics , vol.8 , pp. 3536-3547
    • Whiteman, S.A.1    Serazetdinova, L.2    Jones, A.M.E.3    Sanders, D.4    Rathjen, J.5    Peck, S.C.6    Maathuis, F.J.M.7
  • 65
    • 71049118230 scopus 로고    scopus 로고
    • Comparative transcripts profiling reveals new insight into molecular processes regulating lycopene accumulation in a sweet orange (Citrus sinensis) red-flesh mutant
    • Xu Q, Yu K, Zhu A, Ye J, Liu Q, Zhang J, Deng X (2009) Comparative transcripts profiling reveals new insight into molecular processes regulating lycopene accumulation in a sweet orange (Citrus sinensis) red-flesh mutant. BMC Genomics 10: 540
    • (2009) BMC Genomics , vol.10 , pp. 540
    • Xu, Q.1    Yu, K.2    Zhu, A.3    Ye, J.4    Liu, Q.5    Zhang, J.6    Deng, X.7
  • 66
    • 82255186279 scopus 로고    scopus 로고
    • A proteomic analysis of the chromoplasts isolated from sweet orange fruits [Citrus sinensis (L.) Osbeck]
    • Zeng Y, Pan Z, Ding Y, Zhu A, Cao H, Xu Q, Deng X (2011) A proteomic analysis of the chromoplasts isolated from sweet orange fruits [Citrus sinensis (L.) Osbeck]. J Exp Bot 62: 5297-5309
    • (2011) J Exp Bot , vol.62 , pp. 5297-5309
    • Zeng, Y.1    Pan, Z.2    Ding, Y.3    Zhu, A.4    Cao, H.5    Xu, Q.6    Deng, X.7


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