메뉴 건너뛰기




Volumn 167, Issue 12, 2010, Pages 939-950

In vitro characterization of Arabidopsis CP12 isoforms reveals common biochemical and molecular properties

Author keywords

Calvin cycle; Disulfide bridge; Protein family; Redox; Supramolecular complex

Indexed keywords

ARABIDOPSIS PROTEIN; CARRIER PROTEIN; CP12 1 PROTEIN, ARABIDOPSIS; CP12 2 PROTEIN, ARABIDOPSIS; CP12 3 PROTEIN, ARABIDOPSIS; CP12-1 PROTEIN, ARABIDOPSIS; CP12-2 PROTEIN, ARABIDOPSIS; CP12-3 PROTEIN, ARABIDOPSIS; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; ISOPROTEIN; MULTIPROTEIN COMPLEX; PHOSPHORIBULOKINASE; PHOSPHOTRANSFERASE;

EID: 77953712801     PISSN: 01761617     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jplph.2010.02.008     Document Type: Article
Times cited : (38)

References (31)
  • 2
    • 36849050657 scopus 로고    scopus 로고
    • Regulation of phosphoribulokinase and glyceraldehydes-3-phosphate dehydrogenase in a freshwater diatom, Asterionella formosa
    • Boggetto N., Gontero B., and Maberly S.C. Regulation of phosphoribulokinase and glyceraldehydes-3-phosphate dehydrogenase in a freshwater diatom, Asterionella formosa. J Phycol 43 (2007) 1227-1235
    • (2007) J Phycol , vol.43 , pp. 1227-1235
    • Boggetto, N.1    Gontero, B.2    Maberly, S.C.3
  • 4
    • 0034796437 scopus 로고    scopus 로고
    • Hydrophobic residues within the predicted N-terminal amphiphilic alpha-helix of a plant mitochondrial targeting presequence play a major role in in vivo import
    • Duby G., Oufattole M., and Boutry M. Hydrophobic residues within the predicted N-terminal amphiphilic alpha-helix of a plant mitochondrial targeting presequence play a major role in in vivo import. Plant J 27 (2001) 539-549
    • (2001) Plant J , vol.27 , pp. 539-549
    • Duby, G.1    Oufattole, M.2    Boutry, M.3
  • 5
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets. The roles of intrinsic disorder in protein interaction networks
    • Dunker A.K., Cortese M.S., Romero P., Iakoucheva L.M., and Uversky V.N. Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS J 272 (2005) 5129-5148
    • (2005) FEBS J , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 6
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., and Wright P.E. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6 (2005) 197-208
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 7
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson O., Nielsen H., and von Heijne G. ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci 8 (1999) 978-984
    • (1999) Protein Sci , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    von Heijne, G.3
  • 9
    • 0037826944 scopus 로고    scopus 로고
    • The small protein CP12: a protein linker for supramolecular complex assembly
    • Graciet E., Gans P., Wedel N., Lebreton S., Camadro J.M., and Gontero B. The small protein CP12: a protein linker for supramolecular complex assembly. Biochemistry 42 (2003) 8163-8170
    • (2003) Biochemistry , vol.42 , pp. 8163-8170
    • Graciet, E.1    Gans, P.2    Wedel, N.3    Lebreton, S.4    Camadro, J.M.5    Gontero, B.6
  • 10
    • 2942692516 scopus 로고    scopus 로고
    • Emergence of new regulatory mechanisms in the Benson-Calvin pathway via protein-protein interactions: a glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase complex
    • Graciet E., Lebreton S., and Gontero B. Emergence of new regulatory mechanisms in the Benson-Calvin pathway via protein-protein interactions: a glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase complex. J Exp Bot 55 (2004) 1245-1254
    • (2004) J Exp Bot , vol.55 , pp. 1245-1254
    • Graciet, E.1    Lebreton, S.2    Gontero, B.3
  • 11
    • 41649092090 scopus 로고    scopus 로고
    • Thioredoxin-mediated reversible dissociation of a stromal multiprotein complex in response to changes in light availability
    • Howard T.P., Metodiev M., Lloyd J.C., and Raines C.A. Thioredoxin-mediated reversible dissociation of a stromal multiprotein complex in response to changes in light availability. Proc Natl Acad Sci USA 105 (2008) 4056-4061
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 4056-4061
    • Howard, T.P.1    Metodiev, M.2    Lloyd, J.C.3    Raines, C.A.4
  • 12
    • 23444456924 scopus 로고    scopus 로고
    • How to study proteins by circular dichroism
    • Kelly S.M., Jess T.J., and Price N.C. How to study proteins by circular dichroism. Biochim Biophys Acta 1751 (2005) 119-139
    • (2005) Biochim Biophys Acta , vol.1751 , pp. 119-139
    • Kelly, S.M.1    Jess, T.J.2    Price, N.C.3
  • 13
    • 33745625418 scopus 로고    scopus 로고
    • Mapping of the interaction site of CP12 with glyceraldehyde-3-phosphate dehydrogenase from Chlamydomonas reinhardtii. Functional consequences for glyceraldehyde-3-phosphate dehydrogenase
    • Lebreton S., Andreescu S., Graciet E., and Gontero B. Mapping of the interaction site of CP12 with glyceraldehyde-3-phosphate dehydrogenase from Chlamydomonas reinhardtii. Functional consequences for glyceraldehyde-3-phosphate dehydrogenase. FEBS J 273 (2006) 3358-3369
    • (2006) FEBS J , vol.273 , pp. 3358-3369
    • Lebreton, S.1    Andreescu, S.2    Graciet, E.3    Gontero, B.4
  • 14
    • 33845873289 scopus 로고    scopus 로고
    • Interactive Tree Of Life (iTOL): an online tool for phylogenetic tree display and annotation
    • Letunic I., and Bork P. Interactive Tree Of Life (iTOL): an online tool for phylogenetic tree display and annotation. Bioinformatics 23 (2006) 127-128
    • (2006) Bioinformatics , vol.23 , pp. 127-128
    • Letunic, I.1    Bork, P.2
  • 15
    • 11444265790 scopus 로고    scopus 로고
    • Co-ordinated gene expression of photosynthetic glyceraldehyde-3-phosphate dehydrogenase, phosphoribulokinase, and CP12 in Arabidopsis thaliana
    • Marri L., Sparla F., Pupillo P., and Trost P. Co-ordinated gene expression of photosynthetic glyceraldehyde-3-phosphate dehydrogenase, phosphoribulokinase, and CP12 in Arabidopsis thaliana. J Exp Bot 56 (2005) 73-80
    • (2005) J Exp Bot , vol.56 , pp. 73-80
    • Marri, L.1    Sparla, F.2    Pupillo, P.3    Trost, P.4
  • 16
    • 33644840144 scopus 로고    scopus 로고
    • Reconstitution and properties of the recombinant glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase supramolecular complex of Arabidopsis
    • Marri L., Trost P., Pupillo P., and Sparla F. Reconstitution and properties of the recombinant glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase supramolecular complex of Arabidopsis. Plant Physiol 139 (2005) 1433-1443
    • (2005) Plant Physiol , vol.139 , pp. 1433-1443
    • Marri, L.1    Trost, P.2    Pupillo, P.3    Sparla, F.4
  • 17
    • 38349085008 scopus 로고    scopus 로고
    • Spontaneous assembly of photosynthetic supramolecular complexes as mediated by the intrinsically unstructured protein CP12
    • Marri L., Trost P., Trivelli X., Gonnelli L., Pupillo P., and Sparla F. Spontaneous assembly of photosynthetic supramolecular complexes as mediated by the intrinsically unstructured protein CP12. J Biol Chem 283 (2008) 1831-1838
    • (2008) J Biol Chem , vol.283 , pp. 1831-1838
    • Marri, L.1    Trost, P.2    Trivelli, X.3    Gonnelli, L.4    Pupillo, P.5    Sparla, F.6
  • 18
    • 65249135989 scopus 로고    scopus 로고
    • Prompt and easy activation by specific thioredoxins of Calvin cycle enzymes of Arabidopsis thaliana associated in the GAPDH/CP12/PRK supramolecular complex
    • Marri L., Zaffagnini M., Collin V., Issakidis-Bourguet E., Lemaire S.D., Pupillo P., et al. Prompt and easy activation by specific thioredoxins of Calvin cycle enzymes of Arabidopsis thaliana associated in the GAPDH/CP12/PRK supramolecular complex. Mol Plant 2 (2009) 259-269
    • (2009) Mol Plant , vol.2 , pp. 259-269
    • Marri, L.1    Zaffagnini, M.2    Collin, V.3    Issakidis-Bourguet, E.4    Lemaire, S.D.5    Pupillo, P.6
  • 19
    • 34548794129 scopus 로고    scopus 로고
    • Redox regulation of chloroplast enzymes in Galdieria sulphuraria in view of eukaryotic evolution
    • Oesterhelt C., Klocke S., Holtgrefe S., Linke V., Weber A.P., and Scheibe R. Redox regulation of chloroplast enzymes in Galdieria sulphuraria in view of eukaryotic evolution. Plant Cell Physiol 48 (2007) 1359-1373
    • (2007) Plant Cell Physiol , vol.48 , pp. 1359-1373
    • Oesterhelt, C.1    Klocke, S.2    Holtgrefe, S.3    Linke, V.4    Weber, A.P.5    Scheibe, R.6
  • 20
    • 0042672742 scopus 로고    scopus 로고
    • Origin, evolution, and metabolic role of a novel glycolytic GAPDH enzyme recruited by land plant plastids
    • Petersen J., Brinkmann H., and Cerff R. Origin, evolution, and metabolic role of a novel glycolytic GAPDH enzyme recruited by land plant plastids. J Mol Evol 57 (2003) 16-26
    • (2003) J Mol Evol , vol.57 , pp. 16-26
    • Petersen, J.1    Brinkmann, H.2    Cerff, R.3
  • 21
    • 33646867843 scopus 로고    scopus 로고
    • The GapA/B gene duplication marks the origin of Streptophyta (Charophytes and land plants)
    • Petersen J., Teich R., Becker B., Cerff R., and Brinkmann H. The GapA/B gene duplication marks the origin of Streptophyta (Charophytes and land plants). Mol Biol Evol 23 (2006) 1109-1118
    • (2006) Mol Biol Evol , vol.23 , pp. 1109-1118
    • Petersen, J.1    Teich, R.2    Becker, B.3    Cerff, R.4    Brinkmann, H.5
  • 22
    • 0030445521 scopus 로고    scopus 로고
    • CP12: a small nuclear-encoded chloroplast protein provides novel insights into higher-plant GAPDH evolution
    • Pohlmeyer K., Paap B.K., Soll J., and Wedel N. CP12: a small nuclear-encoded chloroplast protein provides novel insights into higher-plant GAPDH evolution. Plant Mol Biol 32 (1996) 969-978
    • (1996) Plant Mol Biol , vol.32 , pp. 969-978
    • Pohlmeyer, K.1    Paap, B.K.2    Soll, J.3    Wedel, N.4
  • 23
    • 34248188187 scopus 로고    scopus 로고
    • Unique regulation of the Calvin cycle in the ultrasmall green alga Ostreococcus
    • Robbens S., Petersen J., Brinkmann H., Rouzé P., and Van de Peer Y. Unique regulation of the Calvin cycle in the ultrasmall green alga Ostreococcus. J Mol Evol 64 (2007) 601-604
    • (2007) J Mol Evol , vol.64 , pp. 601-604
    • Robbens, S.1    Petersen, J.2    Brinkmann, H.3    Rouzé, P.4    Van de Peer, Y.5
  • 25
    • 0036441528 scopus 로고    scopus 로고
    • Co-existence of two regulatory NADP-glyceraldehyde 3-P dehydrogenase complexes in higher plant chloroplasts
    • Scheibe R., Wedel N., Vetter S., Emmerlich V., and Sauermann S.M. Co-existence of two regulatory NADP-glyceraldehyde 3-P dehydrogenase complexes in higher plant chloroplasts. Eur J Biochem 269 (2002) 5617-5624
    • (2002) Eur J Biochem , vol.269 , pp. 5617-5624
    • Scheibe, R.1    Wedel, N.2    Vetter, S.3    Emmerlich, V.4    Sauermann, S.M.5
  • 26
    • 55249092927 scopus 로고    scopus 로고
    • Expression analysis of the Arabidopsis CP12 gene family suggests novel roles for these proteins in roots and floral tissues
    • Singh P., Kaloudas D., and Raines C.A. Expression analysis of the Arabidopsis CP12 gene family suggests novel roles for these proteins in roots and floral tissues. J Exp Bot 59 (2008) 3975-3985
    • (2008) J Exp Bot , vol.59 , pp. 3975-3985
    • Singh, P.1    Kaloudas, D.2    Raines, C.A.3
  • 27
    • 33745961686 scopus 로고    scopus 로고
    • Redox regulation of a novel plastid-targeted beta-amylase of Arabidopsis
    • Sparla F., Costa A., Lo Schiavo F., Pupillo P., and Trost P. Redox regulation of a novel plastid-targeted beta-amylase of Arabidopsis. Plant Physiol 141 (2006) 840-850
    • (2006) Plant Physiol , vol.141 , pp. 840-850
    • Sparla, F.1    Costa, A.2    Lo Schiavo, F.3    Pupillo, P.4    Trost, P.5
  • 28
    • 19444376568 scopus 로고    scopus 로고
    • The Calvin cycle in cyanobacteria is regulated by CP12 via the NAD(H)/NADP(H) ratio under light/dark conditions
    • Tamoi M., Miyazaki T., Fukamizo T., and Shigeoka S. The Calvin cycle in cyanobacteria is regulated by CP12 via the NAD(H)/NADP(H) ratio under light/dark conditions. Plant J 42 (2005) 504-513
    • (2005) Plant J , vol.42 , pp. 504-513
    • Tamoi, M.1    Miyazaki, T.2    Fukamizo, T.3    Shigeoka, S.4
  • 29
    • 33749840484 scopus 로고    scopus 로고
    • Thioredoxin-dependent regulation of photosynthetic glyceraldehyde-3-phosphate dehydrogenase: autonomous vs. CP12-dependent mechanisms
    • Trost P., Fermani S., Marri L., Zaffagnini M., Falini G., Scagliarini S., et al. Thioredoxin-dependent regulation of photosynthetic glyceraldehyde-3-phosphate dehydrogenase: autonomous vs. CP12-dependent mechanisms. Photosynth Res 89 (2006) 263-275
    • (2006) Photosynth Res , vol.89 , pp. 263-275
    • Trost, P.1    Fermani, S.2    Marri, L.3    Zaffagnini, M.4    Falini, G.5    Scagliarini, S.6
  • 30
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: a point where biology waits for physics
    • Uversky V.N. Natively unfolded proteins: a point where biology waits for physics. Protein Sci 11 (2002) 739-756
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 31
    • 0032482983 scopus 로고    scopus 로고
    • Evolutionarily conserved light regulation of Calvin cycle activity by NADPH-mediated reversible phosphoribulokinase/CP12/glyceraldehyde-3-phosphate dehydrogenase complex dissociation
    • Wedel N., and Soll J. Evolutionarily conserved light regulation of Calvin cycle activity by NADPH-mediated reversible phosphoribulokinase/CP12/glyceraldehyde-3-phosphate dehydrogenase complex dissociation. Proc Natl Acad Sci USA 95 (1998) 9699-9704
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9699-9704
    • Wedel, N.1    Soll, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.