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Volumn 75, Issue 13, 2012, Pages 4027-4037

Analysis of N-glycosylation in maize cytokinin oxidase/dehydrogenase 1 using a manual microgradient chromatographic separation coupled offline to MALDI-TOF/TOF mass spectrometry

Author keywords

Cytokinin oxidase dehydrogenase; Endoglycosidase h; Glycan; Mass spectrometry; N glycosylation; Yarrowia lipolytica

Indexed keywords

CYTOKININ; ENDOGLYCOSIDASE H; GLYCAN; GLYCOPEPTIDE; GLYCOSIDASE; ISOENZYME; OXIDOREDUCTASE; RECOMBINANT ENZYME; RECOMBINANT ZMCKO1; UNCLASSIFIED DRUG;

EID: 84862639145     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.05.013     Document Type: Article
Times cited : (16)

References (43)
  • 1
    • 33947460869 scopus 로고
    • Kinetin, a cell division factor from deoxyribonucleic acid
    • Miller C.O., Skoog F., von Saltza M.H., Strong M. Kinetin, a cell division factor from deoxyribonucleic acid. J Am Chem Soc 1955, 77:1329-1334.
    • (1955) J Am Chem Soc , vol.77 , pp. 1329-1334
    • Miller, C.O.1    Skoog, F.2    von Saltza, M.H.3    Strong, M.4
  • 5
    • 70349647028 scopus 로고    scopus 로고
    • Unraveling the evolution of cytokinin signaling
    • Pils B., Heyl A. Unraveling the evolution of cytokinin signaling. Plant Physiol 2009, 151:782-791.
    • (2009) Plant Physiol , vol.151 , pp. 782-791
    • Pils, B.1    Heyl, A.2
  • 6
    • 33745957013 scopus 로고    scopus 로고
    • Cytokinins: activity, biosynthesis, and translocation
    • Sakakibara H. Cytokinins: activity, biosynthesis, and translocation. Annu Rev Plant Biol 2006, 57:431-449.
    • (2006) Annu Rev Plant Biol , vol.57 , pp. 431-449
    • Sakakibara, H.1
  • 7
    • 0034928185 scopus 로고    scopus 로고
    • Identification of plant cytokinin biosynthetic enzymes as dimethylallyl diphosphate: ATP/ADP isopentenyltransferases
    • Kakimoto T. Identification of plant cytokinin biosynthetic enzymes as dimethylallyl diphosphate: ATP/ADP isopentenyltransferases. Plant Cell Physiol 2001, 42:677-685.
    • (2001) Plant Cell Physiol , vol.42 , pp. 677-685
    • Kakimoto, T.1
  • 8
    • 0035854758 scopus 로고    scopus 로고
    • Identification of genes encoding adenylate isopentenyltransferase, a cytokinin biosynthesis enzyme, in Arabidopsis thaliana
    • Takei K., Sakakibara H., Sugiyama T. Identification of genes encoding adenylate isopentenyltransferase, a cytokinin biosynthesis enzyme, in Arabidopsis thaliana. J Biol Chem 2001, 276:26405-26410.
    • (2001) J Biol Chem , vol.276 , pp. 26405-26410
    • Takei, K.1    Sakakibara, H.2    Sugiyama, T.3
  • 9
    • 0034832289 scopus 로고    scopus 로고
    • Cytokinin oxidase or dehydrogenase? Mechanism of cytokinin degradation in cereals
    • Galuszka P., Frébort I., Šebela M., Sauer P., Jacobsen S., Peč P. Cytokinin oxidase or dehydrogenase? Mechanism of cytokinin degradation in cereals. Eur J Biochem 2001, 268:450-461.
    • (2001) Eur J Biochem , vol.268 , pp. 450-461
    • Galuszka, P.1    Frébort, I.2    Šebela, M.3    Sauer, P.4    Jacobsen, S.5    Peč, P.6
  • 10
    • 0001641879 scopus 로고
    • 2-isopentenyl)adenosine to adenosine by enzyme activity in tobacco tissue
    • 2-isopentenyl)adenosine to adenosine by enzyme activity in tobacco tissue. Plant Physiol 1971, 48:775-778.
    • (1971) Plant Physiol , vol.48 , pp. 775-778
    • Pačes, V.1    Werstiuk, E.2    Hall, R.H.3
  • 11
    • 0016162545 scopus 로고
    • A cytokinin oxidase in Zea mays
    • Whitty C.D., Hall R.H. A cytokinin oxidase in Zea mays. Can J Biochem 1974, 52:789-799.
    • (1974) Can J Biochem , vol.52 , pp. 789-799
    • Whitty, C.D.1    Hall, R.H.2
  • 13
    • 0040370514 scopus 로고    scopus 로고
    • Cytokinin oxidase from Zea mays: purification, cDNA cloning and expression in moss protoplasts
    • Houba-Hérin N., Pethe C., d'Alayer J., Laloue M. Cytokinin oxidase from Zea mays: purification, cDNA cloning and expression in moss protoplasts. Plant J 1999, 17:615-626.
    • (1999) Plant J , vol.17 , pp. 615-626
    • Houba-Hérin, N.1    Pethe, C.2    d'Alayer, J.3    Laloue, M.4
  • 16
    • 25444499704 scopus 로고    scopus 로고
    • High-level expression and characterization of Zea mays cytokinin oxidase/dehydrogenase in Yarrowia lipolytica
    • Kopečný D., Pethe C., Šebela M., Houba-Hérin N., Madzak C., Majira A., et al. High-level expression and characterization of Zea mays cytokinin oxidase/dehydrogenase in Yarrowia lipolytica. Biochimie 2005, 87:1011-1022.
    • (2005) Biochimie , vol.87 , pp. 1011-1022
    • Kopečný, D.1    Pethe, C.2    Šebela, M.3    Houba-Hérin, N.4    Madzak, C.5    Majira, A.6
  • 17
    • 0037997624 scopus 로고    scopus 로고
    • Structure and function of cytokinin oxidase/dehydrogenase genes of maize, rice, Arabidopsis and other species
    • Schmülling T., Werner T., Riefler M., Krupková E., Bartrina y Manns I. Structure and function of cytokinin oxidase/dehydrogenase genes of maize, rice, Arabidopsis and other species. J Plant Res 2003, 116:241-252.
    • (2003) J Plant Res , vol.116 , pp. 241-252
    • Schmülling, T.1    Werner, T.2    Riefler, M.3    Krupková, E.4    Bartrina y Manns, I.5
  • 18
    • 34648819277 scopus 로고    scopus 로고
    • Biochemical characterization of cytokinin oxidases/dehydrogenases from Arabidopsis thaliana expressed in Nicotiana tabacum L
    • Galuszka P., Popelková H., Werner T., Frébortová J., Pospíšilová H., Mik V., et al. Biochemical characterization of cytokinin oxidases/dehydrogenases from Arabidopsis thaliana expressed in Nicotiana tabacum L. J Plant Growth Regul 2007, 26:255-267.
    • (2007) J Plant Growth Regul , vol.26 , pp. 255-267
    • Galuszka, P.1    Popelková, H.2    Werner, T.3    Frébortová, J.4    Pospíšilová, H.5    Mik, V.6
  • 19
    • 4143057296 scopus 로고    scopus 로고
    • Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis
    • Malito E., Coda A., Bilyeu K.D., Fraaije M.W., Mattevi A. Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis. J Mol Biol 2004, 341:1237-1249.
    • (2004) J Mol Biol , vol.341 , pp. 1237-1249
    • Malito, E.1    Coda, A.2    Bilyeu, K.D.3    Fraaije, M.W.4    Mattevi, A.5
  • 20
    • 37349080167 scopus 로고    scopus 로고
    • Crystal structure of Arabidopsis thaliana cytokinin dehydrogenase
    • Bae E., Bingman C.A., Bitto E., Aceti D.J., Phillips G.N. Crystal structure of Arabidopsis thaliana cytokinin dehydrogenase. Proteins 2008, 70:303-306.
    • (2008) Proteins , vol.70 , pp. 303-306
    • Bae, E.1    Bingman, C.A.2    Bitto, E.3    Aceti, D.J.4    Phillips, G.N.5
  • 21
    • 77954658189 scopus 로고    scopus 로고
    • Phenyl- and benzylurea cytokinins as competitive inhibitors of cytokinin oxidase/dehydrogenase: a structural study
    • Kopečný D., Briozzo P., Popelková H., Šebela M., Končitíková R., Spíchal L., et al. Phenyl- and benzylurea cytokinins as competitive inhibitors of cytokinin oxidase/dehydrogenase: a structural study. Biochimie 2010, 92:1052-1062.
    • (2010) Biochimie , vol.92 , pp. 1052-1062
    • Kopečný, D.1    Briozzo, P.2    Popelková, H.3    Šebela, M.4    Končitíková, R.5    Spíchal, L.6
  • 25
    • 0031734879 scopus 로고    scopus 로고
    • A general approach to desalting oligosaccharides released from glycoproteins
    • Packer N.H., Lawson M.A., Jardine D.R., Redmond J.W. A general approach to desalting oligosaccharides released from glycoproteins. Glycoconj J 1998, 15:737-747.
    • (1998) Glycoconj J , vol.15 , pp. 737-747
    • Packer, N.H.1    Lawson, M.A.2    Jardine, D.R.3    Redmond, J.W.4
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A., Tomas H., Havliš J., Olsen J.V., Mann M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat Protoc 2006, 1:2856-2860.
    • (2006) Nat Protoc , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havliš, J.3    Olsen, J.V.4    Mann, M.5
  • 28
    • 78249257564 scopus 로고    scopus 로고
    • Vacuolar and cytosolic cytokinin dehydrogenases of Arabidopsis thaliana: heterologous expression, purification and properties
    • Kowalska M., Galuszka P., Frébortová J., Šebela M., Béres T., Hluska T., et al. Vacuolar and cytosolic cytokinin dehydrogenases of Arabidopsis thaliana: heterologous expression, purification and properties. Phytochemistry 2010, 71:1970-1978.
    • (2010) Phytochemistry , vol.71 , pp. 1970-1978
    • Kowalska, M.1    Galuszka, P.2    Frébortová, J.3    Šebela, M.4    Béres, T.5    Hluska, T.6
  • 29
    • 0033370567 scopus 로고    scopus 로고
    • N-Linked oligosaccharide structures in the diamine oxidase from porcine kidney
    • Huang Y., Mechref Y., Novotny M.V. N-Linked oligosaccharide structures in the diamine oxidase from porcine kidney. Carbohydr Res 2000, 323:111-125.
    • (2000) Carbohydr Res , vol.323 , pp. 111-125
    • Huang, Y.1    Mechref, Y.2    Novotny, M.V.3
  • 30
    • 77951859489 scopus 로고    scopus 로고
    • 3-Aminoquinoline acting as matrix and derivatizing agent for MALDI MS analysis of oligosaccharides
    • Rohmer M., Meyer B., Mank M., Stahl B., Bahr U., Karas M. 3-Aminoquinoline acting as matrix and derivatizing agent for MALDI MS analysis of oligosaccharides. Anal Chem 2010, 82:3719-3726.
    • (2010) Anal Chem , vol.82 , pp. 3719-3726
    • Rohmer, M.1    Meyer, B.2    Mank, M.3    Stahl, B.4    Bahr, U.5    Karas, M.6
  • 31
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • Rappsilber J., Mann M., Ishihama Y. Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat Protoc 2007, 2:1896-1906.
    • (2007) Nat Protoc , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 32
    • 15144343751 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry sample preparation techniques designed for various peptide and protein analytes
    • Kussmann M., Nordhoff E., Rahbek-Nielsen H., Haebel S., Rossel-Larsen M., Jakobsen L., et al. Matrix-assisted laser desorption/ionization mass spectrometry sample preparation techniques designed for various peptide and protein analytes. J Mass Spectrom 1997, 32:593-601.
    • (1997) J Mass Spectrom , vol.32 , pp. 593-601
    • Kussmann, M.1    Nordhoff, E.2    Rahbek-Nielsen, H.3    Haebel, S.4    Rossel-Larsen, M.5    Jakobsen, L.6
  • 33
    • 63449093468 scopus 로고    scopus 로고
    • Short monolithic columns for purification and fractionation of peptide samples for matrix-assisted laser desorption/ionization time-of-flight/time-of-flight mass spectrometry analysis in proteomics
    • Moravcová D., Kahle V., Řehulková H., Chmelík J., Řehulka P. Short monolithic columns for purification and fractionation of peptide samples for matrix-assisted laser desorption/ionization time-of-flight/time-of-flight mass spectrometry analysis in proteomics. J Chromatogr A 2009, 1216:3629-3636.
    • (2009) J Chromatogr A , vol.1216 , pp. 3629-3636
    • Moravcová, D.1    Kahle, V.2    Řehulková, H.3    Chmelík, J.4    Řehulka, P.5
  • 34
    • 0037459157 scopus 로고    scopus 로고
    • Automated microgradient system for capillary electrochromatography
    • Kahle V., Vázlerová M., Welsch T. Automated microgradient system for capillary electrochromatography. J Chromatogr A 2003, 990:3-9.
    • (2003) J Chromatogr A , vol.990 , pp. 3-9
    • Kahle, V.1    Vázlerová, M.2    Welsch, T.3
  • 35
    • 70349213932 scopus 로고    scopus 로고
    • Characterization of new maize genes putatively involved in cytokinin metabolism and their expression during osmotic stress in relation with cytokinin levels
    • Vyroubalová Š., Václavíková K., Turečková V., Novák O., Šmehilová M., Hluska T., et al. Characterization of new maize genes putatively involved in cytokinin metabolism and their expression during osmotic stress in relation with cytokinin levels. Plant Physiol 2009, 151:433-447.
    • (2009) Plant Physiol , vol.151 , pp. 433-447
    • Vyroubalová, Š.1    Václavíková, K.2    Turečková, V.3    Novák, O.4    Šmehilová, M.5    Hluska, T.6
  • 36
  • 37
    • 0024206786 scopus 로고
    • A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates
    • Domon B., Costello C.E. A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates. Glycoconj J 1988, 5:397-409.
    • (1988) Glycoconj J , vol.5 , pp. 397-409
    • Domon, B.1    Costello, C.E.2
  • 38
    • 0034475474 scopus 로고    scopus 로고
    • Electrospray mass spectrometry and fragmentation of N-linked carbohydrates derivatized at the reducing terminus
    • Harvey D.J. Electrospray mass spectrometry and fragmentation of N-linked carbohydrates derivatized at the reducing terminus. J Am Soc Mass Spectrom 2000, 11:900-915.
    • (2000) J Am Soc Mass Spectrom , vol.11 , pp. 900-915
    • Harvey, D.J.1
  • 40
    • 0025840338 scopus 로고
    • The oligosaccharides of glycoproteins: bioprocess factors affecting oligosaccharide structure and their effect on glycoprotein properties
    • Goochee C.F., Gramer M.J., Andersen D.C., Bahr J.B., Rasmussen J.R. The oligosaccharides of glycoproteins: bioprocess factors affecting oligosaccharide structure and their effect on glycoprotein properties. Biotechnology (N Y) 1991, 9:1347-1355.
    • (1991) Biotechnology (N Y) , vol.9 , pp. 1347-1355
    • Goochee, C.F.1    Gramer, M.J.2    Andersen, D.C.3    Bahr, J.B.4    Rasmussen, J.R.5
  • 42
    • 1842530397 scopus 로고    scopus 로고
    • Heterologous protein expression and secretion in the non-conventional yeast Yarrowia lipolytica: a review
    • Madzak C., Gaillardin C., Beckerich J.M. Heterologous protein expression and secretion in the non-conventional yeast Yarrowia lipolytica: a review. J Biotechnol 2004, 109:63-81.
    • (2004) J Biotechnol , vol.109 , pp. 63-81
    • Madzak, C.1    Gaillardin, C.2    Beckerich, J.M.3
  • 43
    • 34547178785 scopus 로고    scopus 로고
    • Engineering of the yeast Yarrowia lipolytica for the production of glycoproteins lacking the outer-chain mannose residues of N-glycans
    • Song Y., Choi M.H., Park J.N., Kim M.W., Kim E.J., Kang H.A., et al. Engineering of the yeast Yarrowia lipolytica for the production of glycoproteins lacking the outer-chain mannose residues of N-glycans. Appl Environ Microbiol 2007, 73:4446-4454.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 4446-4454
    • Song, Y.1    Choi, M.H.2    Park, J.N.3    Kim, M.W.4    Kim, E.J.5    Kang, H.A.6


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