메뉴 건너뛰기




Volumn 229, Issue 5, 2009, Pages 1123-1134

Phosphorylation site mapping of soluble proteins: Bioinformatical filtering reveals potential plastidic phosphoproteins in Arabidopsis thaliana

Author keywords

Arabidopsis; Chloroplast; Immobilized metal ion affinity chromatography (IMAC); Multidimensional protein identification technology (MudPIT); Phosphorylation; TiO2

Indexed keywords

ARABIDOPSIS PROTEIN; PHOSPHOPROTEIN;

EID: 63349112495     PISSN: 00320935     EISSN: 14322048     Source Type: Journal    
DOI: 10.1007/s00425-009-0901-y     Document Type: Article
Times cited : (41)

References (66)
  • 1
    • 0034957327 scopus 로고    scopus 로고
    • Dependence of photosynthesis and energy dissipation activity upon growth form and light environment during the winter
    • WW Adams 3rd B Demmig-Adams TN Rosenstiel V Ebbert 2001 Dependence of photosynthesis and energy dissipation activity upon growth form and light environment during the winter Photosyn Res 67 51 62
    • (2001) Photosyn Res , vol.67 , pp. 51-62
    • Adams III, W.W.1    Demmig-Adams, B.2    Rosenstiel, T.N.3    Ebbert, V.4
  • 2
    • 0026513229 scopus 로고
    • How does protein phosphorylation regulate photosynthesis?
    • JF Allen 1992 How does protein phosphorylation regulate photosynthesis? Trends Biochem Sci 17 12 17
    • (1992) Trends Biochem Sci , vol.17 , pp. 12-17
    • Allen, J.F.1
  • 3
    • 0031148893 scopus 로고    scopus 로고
    • Transcription factor phosphorylation by a protein kinase associated with chloroplast RNA polymerase from mustard (Sinapis alba)
    • S Baginsky K Tiller G Link 1997 Transcription factor phosphorylation by a protein kinase associated with chloroplast RNA polymerase from mustard (Sinapis alba) Plant Mol Biol 34 181 189
    • (1997) Plant Mol Biol , vol.34 , pp. 181-189
    • Baginsky, S.1    Tiller, K.2    Link, G.3
  • 5
    • 14544282417 scopus 로고    scopus 로고
    • State transitions and light adaptation require chloroplast thylakoid protein kinase STN7
    • S Bellafiore F Barneche G Peltier JD Rochaix 2005 State transitions and light adaptation require chloroplast thylakoid protein kinase STN7 Nature 433 892 895
    • (2005) Nature , vol.433 , pp. 892-895
    • Bellafiore, S.1    Barneche, F.2    Peltier, G.3    Rochaix, J.D.4
  • 6
    • 0017411320 scopus 로고
    • Phosphorylation of chloroplast membrane polypeptides
    • J Bennett 1977 Phosphorylation of chloroplast membrane polypeptides Nature 269 344 346
    • (1977) Nature , vol.269 , pp. 344-346
    • Bennett, J.1
  • 8
    • 0023276611 scopus 로고
    • Chloroplast phosphoproteins: Phosphorylation of a 12-kDa stromal protein by the redox-controlled kinase of thylakoid membranes
    • P Bhalla J Bennett 1987 Chloroplast phosphoproteins: phosphorylation of a 12-kDa stromal protein by the redox-controlled kinase of thylakoid membranes Arch Biochem Biophys 252 97 104
    • (1987) Arch Biochem Biophys , vol.252 , pp. 97-104
    • Bhalla, P.1    Bennett, J.2
  • 9
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • N Blom S Gammeltoft S Brunak 1999 Sequence and structure-based prediction of eukaryotic protein phosphorylation sites J Mol Biol 294 1351 1362
    • (1999) J Mol Biol , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 14
    • 84989738512 scopus 로고
    • Stress induced degradation of the photosynthetic apparatus is accompanied by changes in thylakoid protein turnover and phosphorylation
    • H Dannehl A Alexandra Herbik D Godde 1995 Stress induced degradation of the photosynthetic apparatus is accompanied by changes in thylakoid protein turnover and phosphorylation Physiol Plant 93 179 186
    • (1995) Physiol Plant , vol.93 , pp. 179-186
    • Dannehl, H.1    Alexandra Herbik, A.2    Godde, D.3
  • 16
    • 0034962132 scopus 로고    scopus 로고
    • Correlation between persistent forms of zeaxanthin-dependent energy dissipation and thylakoid protein phosphorylation
    • V Ebbert B Demmig-Adams WW Adams 3rd KE Mueh LA Staehelin 2001 Correlation between persistent forms of zeaxanthin-dependent energy dissipation and thylakoid protein phosphorylation Photosyn Res 67 63 78
    • (2001) Photosyn Res , vol.67 , pp. 63-78
    • Ebbert, V.1    Demmig-Adams, B.2    Adams III, W.W.3    Mueh, K.E.4    Staehelin, L.A.5
  • 17
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • O Emanuelsson H Nielsen S Brunak G von Heijne 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
  • 18
    • 0022137502 scopus 로고
    • Stromal protein phosphorylation in spinach (Spinacia oleracea) chloroplasts
    • CH Foyer 1985 Stromal protein phosphorylation in spinach (Spinacia oleracea) chloroplasts Biochem J 231 97 103
    • (1985) Biochem J , vol.231 , pp. 97-103
    • Foyer, C.H.1
  • 19
    • 0035356565 scopus 로고    scopus 로고
    • Phosphoprotein isotope-coded affinity tag approach for isolating and quantitating phosphopeptides in proteome-wide analyzes
    • MB Goshe TP Conrads EA Panisko NH Angell TD Veenstra RD Smith 2001 Phosphoprotein isotope-coded affinity tag approach for isolating and quantitating phosphopeptides in proteome-wide analyzes Anal Chem 73 2578 2586
    • (2001) Anal Chem , vol.73 , pp. 2578-2586
    • Goshe, M.B.1    Conrads, T.P.2    Panisko, E.A.3    Angell, N.H.4    Veenstra, T.D.5    Smith, R.D.6
  • 20
    • 0023368807 scopus 로고
    • Phosphorylation in vitro of the large subunit of the ribulose-1, 5-bisphosphate carboxylase and of the glyceraldehyde-3-phosphate dehydrogenase
    • C Guitton R Mache 1987 Phosphorylation in vitro of the large subunit of the ribulose-1, 5-bisphosphate carboxylase and of the glyceraldehyde-3-phosphate dehydrogenase Eur J Biochem 166 249 254
    • (1987) Eur J Biochem , vol.166 , pp. 249-254
    • Guitton, C.1    MacHe, R.2
  • 22
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • T Hunter 1995 Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling Cell 80 225 236
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 23
    • 38049061188 scopus 로고    scopus 로고
    • Impaired photosystem i oxidation induces STN7-dependent phosphorylation of the light-harvesting complex i protein Lhca4 in Arabidopsis thaliana
    • A Ihnatowicz P Pesaresi K Lohrig D Wolters B Muller D Leister 2008 Impaired photosystem I oxidation induces STN7-dependent phosphorylation of the light-harvesting complex I protein Lhca4 in Arabidopsis thaliana Planta 227 717 722
    • (2008) Planta , vol.227 , pp. 717-722
    • Ihnatowicz, A.1    Pesaresi, P.2    Lohrig, K.3    Wolters, D.4    Muller, B.5    Leister, D.6
  • 24
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • TAG Initiative 2000 Analysis of the genome sequence of the flowering plant Arabidopsis thaliana Nature 408 796 815
    • (2000) Nature , vol.408 , pp. 796-815
    • Initiative, T.A.G.1
  • 25
    • 36248934589 scopus 로고    scopus 로고
    • Evaluation of the impact of some experimental procedures on different phosphopeptide enrichment techniques
    • SS Jensen MR Larsen 2007 Evaluation of the impact of some experimental procedures on different phosphopeptide enrichment techniques Rapid Commun Mass Spectrom 21 3635 3645
    • (2007) Rapid Commun Mass Spectrom , vol.21 , pp. 3635-3645
    • Jensen, S.S.1    Larsen, M.R.2
  • 26
    • 0037005989 scopus 로고    scopus 로고
    • Protein kinases and protein phosphatases in prokaryotes: A genomic perspective
    • PJ Kennelly 2002 Protein kinases and protein phosphatases in prokaryotes: a genomic perspective FEMS Microbiol Lett 206 1 8
    • (2002) FEMS Microbiol Lett , vol.206 , pp. 1-8
    • Kennelly, P.J.1
  • 27
    • 33645669336 scopus 로고    scopus 로고
    • A chloroplast-localized dual-specificity protein phosphatase in Arabidopsis contains a phylogenetically dispersed and ancient carbohydrate-binding domain, which binds the polysaccharide starch
    • D Kerk TR Conley FA Rodriguez HT Tran M Nimick DG Muench GB Moorhead 2006 A chloroplast-localized dual-specificity protein phosphatase in Arabidopsis contains a phylogenetically dispersed and ancient carbohydrate-binding domain, which binds the polysaccharide starch Plant J 46 400 413
    • (2006) Plant J , vol.46 , pp. 400-413
    • Kerk, D.1    Conley, T.R.2    Rodriguez, F.A.3    Tran, H.T.4    Nimick, M.5    Muench, D.G.6    Moorhead, G.B.7
  • 28
    • 36549010017 scopus 로고    scopus 로고
    • Isolation of the Arabidopsis phosphoproteome using a biotin-tagging approach
    • SJ Kwon EY Choi JB Seo OK Park 2007 Isolation of the Arabidopsis phosphoproteome using a biotin-tagging approach Mol Cells 24 268 275
    • (2007) Mol Cells , vol.24 , pp. 268-275
    • Kwon, S.J.1    Choi, E.Y.2    Seo, J.B.3    Park, O.K.4
  • 29
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • MR Larsen TE Thingholm ON Jensen P Roepstorff TJ Jorgensen 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    Jorgensen, T.J.5
  • 30
    • 0035669594 scopus 로고    scopus 로고
    • The role of protein kinases in the regulation of plant growth and development
    • S Laurie NG Halford 2001 The role of protein kinases in the regulation of plant growth and development Plant Growth Regul 34 253 265
    • (2001) Plant Growth Regul , vol.34 , pp. 253-265
    • Laurie, S.1    Halford, N.G.2
  • 31
    • 0037213560 scopus 로고    scopus 로고
    • Chloroplast research in the genomic age
    • D Leister 2003 Chloroplast research in the genomic age Trends Genet 19 47 56
    • (2003) Trends Genet , vol.19 , pp. 47-56
    • Leister, D.1
  • 33
    • 0037296184 scopus 로고    scopus 로고
    • Redox regulation of chloroplast transcription
    • G Link 2003 Redox regulation of chloroplast transcription Antioxid Redox Signal 5 79 87
    • (2003) Antioxid Redox Signal , vol.5 , pp. 79-87
    • Link, G.1
  • 34
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • H Liu RG Sadygov JR Yates 3rd 2004 A model for random sampling and estimation of relative protein abundance in shotgun proteomics Anal Chem 76 4193 4201
    • (2004) Anal Chem , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates III, J.R.3
  • 36
    • 4544291080 scopus 로고    scopus 로고
    • Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database
    • TS Nuhse A Stensballe ON Jensen SC Peck 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
  • 37
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Y Oda T Nagasu BT Chait 2001 Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome Nat Biotechnol 19 379 382
    • (2001) Nat Biotechnol , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 38
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • JV Olsen B Blagoev F Gnad B Macek C Kumar P Mortensen M Mann 2006 Global, in vivo, and site-specific phosphorylation dynamics in signaling networks Cell 127 635 648
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    MacEk, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 39
    • 10344242448 scopus 로고    scopus 로고
    • New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy
    • JB Peltier AJ Ytterberg Q Sun KJ van Wijk 2004 New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy J Biol Chem 279 49367 49383
    • (2004) J Biol Chem , vol.279 , pp. 49367-49383
    • Peltier, J.B.1    Ytterberg, A.J.2    Sun, Q.3    Van Wijk, K.J.4
  • 40
    • 63349088956 scopus 로고    scopus 로고
    • Thylakoid protein phosphorylation and its impact on short- and long-term acclimation of photosynthesis
    • Buchner TB, Ewingen NH (eds) Nova Science Publishers, Hauppauge (in press). ISBN: 978-1-60692-719-9
    • Pesaresi P, Kleine T, Leister D (2009) Thylakoid protein phosphorylation and its impact on short- and long-term acclimation of photosynthesis. In: Buchner TB, Ewingen NH (eds) Theory and applications in energy, biotechnology and nanotechnology. Nova Science Publishers, Hauppauge (in press). ISBN: 978-1-60692-719-9
    • (2009) Theory and Applications in Energy, Biotechnology and Nanotechnology
    • Pesaresi, P.1    Kleine, T.2    Leister, D.3
  • 41
    • 1642276286 scopus 로고    scopus 로고
    • An improved prediction of chloroplast proteins reveals diversities and commonalities in the chloroplast proteomes of Arabidopsis and rice
    • E Richly D Leister 2004 An improved prediction of chloroplast proteins reveals diversities and commonalities in the chloroplast proteomes of Arabidopsis and rice Gene 329 11 16
    • (2004) Gene , vol.329 , pp. 11-16
    • Richly, E.1    Leister, D.2
  • 42
    • 0033849072 scopus 로고    scopus 로고
    • Dephosphorylation of photosystem II reaction center proteins in plant photosynthetic membranes as an immediate response to abrupt elevation of temperature
    • A Rokka EM Aro RG Herrmann B Andersson AV Vener 2000 Dephosphorylation of photosystem II reaction center proteins in plant photosynthetic membranes as an immediate response to abrupt elevation of temperature Plant Physiol 123 1525 1536
    • (2000) Plant Physiol , vol.123 , pp. 1525-1536
    • Rokka, A.1    Aro, E.M.2    Herrmann, R.G.3    Andersson, B.4    Vener, A.V.5
  • 43
    • 0035886699 scopus 로고    scopus 로고
    • Calcium-dependent protein kinases play an essential role in a plant defence response
    • T Romeis AA Ludwig R Martin JD Jones 2001 Calcium-dependent protein kinases play an essential role in a plant defence response EMBO J 20 5556 5567
    • (2001) EMBO J , vol.20 , pp. 5556-5567
    • Romeis, T.1    Ludwig, A.A.2    Martin, R.3    Jones, J.D.4
  • 44
    • 0034031727 scopus 로고    scopus 로고
    • 12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis
    • F Schaller C Biesgen C Mussig T Altmann EW Weiler 2000 12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis Planta 210 979 984
    • (2000) Planta , vol.210 , pp. 979-984
    • Schaller, F.1    Biesgen, C.2    Mussig, C.3    Altmann, T.4    Weiler, E.W.5
  • 45
    • 46049104182 scopus 로고    scopus 로고
    • A survey of chloroplast protein kinases and phosphatases in Arabidopsis thaliana
    • I Schliebner M Pribil J Zühlke A Dietzmann D Leister 2008 A survey of chloroplast protein kinases and phosphatases in Arabidopsis thaliana Curr Genom 9 184 190
    • (2008) Curr Genom , vol.9 , pp. 184-190
    • Schliebner, I.1    Pribil, M.2    Zühlke, J.3    Dietzmann, A.4    Leister, D.5
  • 47
    • 2942589051 scopus 로고    scopus 로고
    • Predotar: A tool for rapidly screening proteomes for N-terminal targeting sequences
    • I Small N Peeters F Legeai C Lurin 2004 Predotar: a tool for rapidly screening proteomes for N-terminal targeting sequences Proteomics 4 1581 1590
    • (2004) Proteomics , vol.4 , pp. 1581-1590
    • Small, I.1    Peeters, N.2    Legeai, F.3    Lurin, C.4
  • 48
    • 0033515448 scopus 로고    scopus 로고
    • TAKs, thylakoid membrane protein kinases associated with energy transduction
    • S Snyders BD Kohorn 1999 TAKs, thylakoid membrane protein kinases associated with energy transduction J Biol Chem 274 9137 9140
    • (1999) J Biol Chem , vol.274 , pp. 9137-9140
    • Snyders, S.1    Kohorn, B.D.2
  • 49
    • 0024060685 scopus 로고
    • Localization of a 64-kDa phosphoprotein in the lumen between the outer and inner envelopes of pea chloroplasts
    • J Soll J Bennett 1988 Localization of a 64-kDa phosphoprotein in the lumen between the outer and inner envelopes of pea chloroplasts Eur J Biochem 175 301 307
    • (1988) Eur J Biochem , vol.175 , pp. 301-307
    • Soll, J.1    Bennett, J.2
  • 52
    • 0031592468 scopus 로고    scopus 로고
    • The structure of the complex between rubisco and its natural substrate ribulose 1, 5-bisphosphate
    • TC Taylor I Andersson 1997 The structure of the complex between rubisco and its natural substrate ribulose 1, 5-bisphosphate J Mol Biol 265 432 444
    • (1997) J Mol Biol , vol.265 , pp. 432-444
    • Taylor, T.C.1    Andersson, I.2
  • 55
    • 0031177703 scopus 로고    scopus 로고
    • Protein phosphorylation as a mechanism for osmotic-stress activation of sucrose-phosphate synthase in spinach leaves
    • D Toroser SC Huber 1997 Protein phosphorylation as a mechanism for osmotic-stress activation of sucrose-phosphate synthase in spinach leaves Plant Physiol 114 947 955
    • (1997) Plant Physiol , vol.114 , pp. 947-955
    • Toroser, D.1    Huber, S.C.2
  • 56
    • 0033082670 scopus 로고    scopus 로고
    • Site-directed mutagenesis of serine 158 demonstrates its role in spinach leaf sucrose-phosphate synthase modulation
    • D Toroser R McMichael Jr KP Krause J Kurreck U Sonnewald M Stitt SC Huber 1999 Site-directed mutagenesis of serine 158 demonstrates its role in spinach leaf sucrose-phosphate synthase modulation Plant J 17 407 413
    • (1999) Plant J , vol.17 , pp. 407-413
    • Toroser, D.1    McMichael Jr., R.2    Krause, K.P.3    Kurreck, J.4    Sonnewald, U.5    Stitt, M.6    Huber, S.C.7
  • 58
    • 34249816795 scopus 로고    scopus 로고
    • Environmentally modulated phosphorylation and dynamics of proteins in photosynthetic membranes
    • AV Vener 2007 Environmentally modulated phosphorylation and dynamics of proteins in photosynthetic membranes Biochim Biophys Acta 1767 449 457
    • (2007) Biochim Biophys Acta , vol.1767 , pp. 449-457
    • Vener, A.V.1
  • 59
    • 0032083023 scopus 로고    scopus 로고
    • Protein phosphorylation and redox sensing in chloroplast thylakoids
    • AV Vener I Ohad B Andersson 1998 Protein phosphorylation and redox sensing in chloroplast thylakoids Curr Opin Plant Biol 1 217 223
    • (1998) Curr Opin Plant Biol , vol.1 , pp. 217-223
    • Vener, A.V.1    Ohad, I.2    Andersson, B.3
  • 61
    • 0029868470 scopus 로고    scopus 로고
    • Phosphorylation of the transit sequence of chloroplast precursor proteins
    • K Waegemann J Soll 1996 Phosphorylation of the transit sequence of chloroplast precursor proteins J Biol Chem 271 6545 6554
    • (1996) J Biol Chem , vol.271 , pp. 6545-6554
    • Waegemann, K.1    Soll, J.2
  • 62
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • MP Washburn D Wolters JR Yates 3rd 2001 Large-scale analysis of the yeast proteome by multidimensional protein identification technology Nat Biotechnol 19 242 247
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 63
    • 0030765070 scopus 로고    scopus 로고
    • Octadecanoid-mediated signal transduction in higher plants
    • EW Weiler 1997 Octadecanoid-mediated signal transduction in higher plants Naturwissenschaften 84 340 349
    • (1997) Naturwissenschaften , vol.84 , pp. 340-349
    • Weiler, E.W.1
  • 65
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • H Zhou JD Watts R Aebersold 2001 A systematic approach to the analysis of protein phosphorylation Nat Biotechnol 19 375 378
    • (2001) Nat Biotechnol , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.