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Volumn 10, Issue 5, 1996, Pages 903-912

Is E37, a major polypeptide of the inner membrane from plastid envelope, an S-adenosyl methionine-dependent methyltransferase?

Author keywords

[No Author keywords available]

Indexed keywords

E37 PROTEIN, SPINACIA OLERACEA; METHIONINE S METHYLTRANSFERASE; METHIONINE S-METHYLTRANSFERASE; METHYLTRANSFERASE; VEGETABLE PROTEIN;

EID: 0030295303     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1996.10050903.x     Document Type: Article
Times cited : (30)

References (31)
  • 1
    • 0028220511 scopus 로고
    • Photolabeling of the EcoP15 DNA methyltransferase with S-adenosyl-L-methionine
    • Ahmad, I. and Rao, D.N. (1994) Photolabeling of the EcoP15 DNA methyltransferase with S-adenosyl-L-methionine. Gene, 142, 67-71.
    • (1994) Gene , vol.142 , pp. 67-71
    • Ahmad, I.1    Rao, D.N.2
  • 2
  • 3
    • 0000625478 scopus 로고
    • Identification and purification of a derepressible alkaline phosphatase from Anacystis nidulans R2
    • Block, M.A. and Grossman, A.R. (1988) Identification and purification of a derepressible alkaline phosphatase from Anacystis nidulans R2. Plant Physiol. 86, 1179-1184.
    • (1988) Plant Physiol. , vol.86 , pp. 1179-1184
    • Block, M.A.1    Grossman, A.R.2
  • 4
    • 0025784735 scopus 로고
    • Purification and characterization of E37, a major chloroplast envelope protein
    • Block, M.A., Joyard, J. and Douce, R. (1991) Purification and characterization of E37, a major chloroplast envelope protein. FEBS Lett. 287, 167-170.
    • (1991) FEBS Lett. , vol.287 , pp. 167-170
    • Block, M.A.1    Joyard, J.2    Douce, R.3
  • 5
    • 12644279824 scopus 로고
    • Characterization of O-methyltransferase activities associated with spinach chloroplast fractions
    • Charriere-Ladreix, Y., Douce, R. and Joyard, J. (1981) Characterization of O-methyltransferase activities associated with spinach chloroplast fractions. FEBS Lett. 133, 55-58.
    • (1981) FEBS Lett. , vol.133 , pp. 55-58
    • Charriere-Ladreix, Y.1    Douce, R.2    Joyard, J.3
  • 6
    • 0027338134 scopus 로고
    • Crystal structure of the Hhal DNA methyltransferase complexed with S-adenosyl-L-methionine
    • Cheng, X., Kumar, S., Postfai, J., Pflugrath, J.W. and Roberts, R.J. (1993) Crystal structure of the Hhal DNA methyltransferase complexed with S-adenosyl-L-methionine. Cell. 74, 299-307.
    • (1993) Cell , vol.74 , pp. 299-307
    • Cheng, X.1    Kumar, S.2    Postfai, J.3    Pflugrath, J.W.4    Roberts, R.J.5
  • 7
    • 0001818570 scopus 로고
    • Purification of the chloroplast
    • (Edelman, M., Hallick, R. and Chua, N.-H., eds). Amsterdam: Elsevier
    • Douce, R. and Joyard, J. (1982) Purification of the chloroplast. In Methods in Chloroplast Molecular Biology (Edelman, M., Hallick, R. and Chua, N.-H., eds). Amsterdam: Elsevier, pp. 239-256.
    • (1982) Methods in Chloroplast Molecular Biology , pp. 239-256
    • Douce, R.1    Joyard, J.2
  • 8
    • 0025224152 scopus 로고
    • Biochemistry and function of the plastid envelope
    • Douce, R. and Joyard, J. (1990) Biochemistry and function of the plastid envelope. Ann. Rev. Cell. Biol. 6, 173-216.
    • (1990) Ann. Rev. Cell. Biol. , vol.6 , pp. 173-216
    • Douce, R.1    Joyard, J.2
  • 9
    • 0026065707 scopus 로고
    • cDNA sequence and deduced amino acid sequence of the precursor of the 37-kDa inner envelope membrane polypeptide from spinach chloroplasts. Its transit peptide contains an amphiphilic α-helix as the only detectable structural element
    • Dreses-Werringloer, U., Fischer, K., Wachter, E., Link, T.A. and Flügge, U.-I. (1991) cDNA sequence and deduced amino acid sequence of the precursor of the 37-kDa inner envelope membrane polypeptide from spinach chloroplasts. Its transit peptide contains an amphiphilic α-helix as the only detectable structural element. Eur. J. Biochem. 195, 361-368.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 361-368
    • Dreses-Werringloer, U.1    Fischer, K.2    Wachter, E.3    Link, T.A.4    Flügge, U.-I.5
  • 10
    • 0011212648 scopus 로고
    • The phosphate translocator of the chloroplast envelope. Isolation of the carrier protein and reconstitution of transport
    • Flügge, U.I. and Heldt, H.W. (1981) The phosphate translocator of the chloroplast envelope. Isolation of the carrier protein and reconstitution of transport. Biochim. Biophys. Acta, 638, 296-304.
    • (1981) Biochim. Biophys. Acta , vol.638 , pp. 296-304
    • Flügge, U.I.1    Heldt, H.W.2
  • 12
    • 0024574552 scopus 로고
    • The triose phosphate-3-phosphogtycerate-translocator from spinach chloroplasts: Nucleotide sequence of a full length cDNA clone and import of the in vivo synthesized precursor protein into chloroplasts
    • Flügge, U.I., Fisher, K., Gross, A., Sebald, W., Lottspeich, F. and Eckerskorn, C. (1989) The triose phosphate-3-phosphogtycerate-translocator from spinach chloroplasts: nucleotide sequence of a full length cDNA clone and import of the in vivo synthesized precursor protein into chloroplasts. EMBO J. 8, 39-46.
    • (1989) EMBO J. , vol.8 , pp. 39-46
    • Flügge, U.I.1    Fisher, K.2    Gross, A.3    Sebald, W.4    Lottspeich, F.5    Eckerskorn, C.6
  • 13
    • 0026730226 scopus 로고
    • Rat guanidinoacetate methyltransferase: Mutation of amino acids within a common sequence motif of mammalian methyltransferase does not affect catalytic activity but alters proteolytic susceptibility
    • Gomi, T., Tanihara, K., Date, T. and Fujioka, M. (1992) Rat guanidinoacetate methyltransferase: mutation of amino acids within a common sequence motif of mammalian methyltransferase does not affect catalytic activity but alters proteolytic susceptibility. Int. J. Biochem. 24, 1639-1649.
    • (1992) Int. J. Biochem. , vol.24 , pp. 1639-1649
    • Gomi, T.1    Tanihara, K.2    Date, T.3    Fujioka, M.4
  • 14
    • 0001067511 scopus 로고
    • Posttranslational modifications in the amino-terminal region of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from several plant species
    • Houtz, R.L., Poneleit, L., Jones, S.B., Royer, M. and Stults, J.T. (1992) Posttranslational modifications in the amino-terminal region of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from several plant species. Plant Physiol. 98, 1170-1174.
    • (1992) Plant Physiol. , vol.98 , pp. 1170-1174
    • Houtz, R.L.1    Poneleit, L.2    Jones, S.B.3    Royer, M.4    Stults, J.T.5
  • 15
    • 0001510436 scopus 로고
    • Solubilization of plant membrane proteins for analysis by two-dimensional gel electrophoresis
    • Hurkman, W.J. and Tanaka, C.K. (1986) Solubilization of plant membrane proteins for analysis by two-dimensional gel electrophoresis. Plant Physiol. 81, 802-806.
    • (1986) Plant Physiol. , vol.81 , pp. 802-806
    • Hurkman, W.J.1    Tanaka, C.K.2
  • 16
    • 0021112417 scopus 로고
    • Localization of polypeptides to the cytosolic side of the outer envelope membrane of spinach chloroplasts
    • Joyard, J., Billecocq, A., Bartlett, S.G., Block, M.A., Chua, N.-H. and Douce, R. (1983) Localization of polypeptides to the cytosolic side of the outer envelope membrane of spinach chloroplasts. J. Biol. Chem. 258, 10 000-10 006.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10000-10006
    • Joyard, J.1    Billecocq, A.2    Bartlett, S.G.3    Block, M.A.4    Chua, N.-H.5    Douce, R.6
  • 17
    • 12644293768 scopus 로고
    • Comparison of envelope membranes from higher plants and algae plastids and of outer membranes from cyanobacteria (blue-green aigea)
    • (Wiessner, W., Robinson, D.G. and Starr, R.C., eds). Berlin: Springer Verlag
    • Joyard, J., Block, M.A., Dorne, A.J. and Douce, R. (1987) Comparison of envelope membranes from higher plants and algae plastids and of outer membranes from cyanobacteria (blue-green aigea). In Algal Development (Molecular and Cellular Aspects) (Wiessner, W., Robinson, D.G. and Starr, R.C., eds). Berlin: Springer Verlag, pp. 123-133.
    • (1987) Algal Development (Molecular and Cellular Aspects) , pp. 123-133
    • Joyard, J.1    Block, M.A.2    Dorne, A.J.3    Douce, R.4
  • 18
    • 0025766501 scopus 로고
    • Molecular aspects of plastid envelope biochemistry
    • Joyard, J., Block, M.A. and Douce, R. (1991) Molecular aspects of plastid envelope biochemistry. Eur. J. Biochem. 199, 489-509.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 489-509
    • Joyard, J.1    Block, M.A.2    Douce, R.3
  • 19
    • 0028179364 scopus 로고
    • Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure of these enzymes
    • Kagan, R.M. and Clarke, S. (1994) Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure of these enzymes. Arch. Biochem. Biophys. 310, 417-427.
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 417-427
    • Kagan, R.M.1    Clarke, S.2
  • 20
    • 0029310495 scopus 로고
    • Identification of a gibberellin-induced gene in deepwater rice using differential display of mRNA
    • van der Knaap, E. and Kende, H. (1995) Identification of a gibberellin-induced gene in deepwater rice using differential display of mRNA. Plant Mol. Biol. 28, 589-592.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 589-592
    • Van Der Knaap, E.1    Kende, H.2
  • 21
    • 0028258669 scopus 로고
    • Expression of genes encoding the tobacco chloroplast phosphate translocator is not light-regulated and is repressed by sucrose
    • Knight, J.S. and Gray, J. (1994) Expression of genes encoding the tobacco chloroplast phosphate translocator is not light-regulated and is repressed by sucrose. Mol. Gen. Genet. 242, 586-594.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 586-594
    • Knight, J.S.1    Gray, J.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-683.
    • (1970) Nature , vol.227 , pp. 680-683
    • Laemmli, U.K.1
  • 23
    • 11944260898 scopus 로고
    • Protein methylation in pea chloroplasts
    • Niemi, K.J., Adler, J. and Selman, B.R. (1990) Protein methylation in pea chloroplasts Plant Physiol. 93, 1235-1240.
    • (1990) Plant Physiol. , vol.93 , pp. 1235-1240
    • Niemi, K.J.1    Adler, J.2    Selman, B.R.3
  • 24
    • 0000153631 scopus 로고
    • Isolation and characterization of the cytoplasmic membranes from the blue-green alga (cyanobacterium) Anacystis nidulans
    • Omata, T. and Murata, N. (1983) Isolation and characterization of the cytoplasmic membranes from the blue-green alga (cyanobacterium) Anacystis nidulans. Plant Cell Physiol. 24, 1101-1112.
    • (1983) Plant Cell Physiol. , vol.24 , pp. 1101-1112
    • Omata, T.1    Murata, N.2
  • 25
    • 0023059178 scopus 로고
    • A conformational preference parameter to predict helices in integral membrane proteins
    • Rao, M.J.K. and Argos, P. (1986) A conformational preference parameter to predict helices in integral membrane proteins. Biochem. Biophys, Acta, 869, 197-214.
    • (1986) Biochem. Biophys, Acta , vol.869 , pp. 197-214
    • Rao, M.J.K.1    Argos, P.2
  • 26
    • 0018827612 scopus 로고
    • Site of biosynthesis of α-tocopherol in spinach chloroplasts
    • Soll, J., Douce, R. and Schultz, G. (1980) Site of biosynthesis of α-tocopherol in spinach chloroplasts. FEBS Lett. 112, 243-246.
    • (1980) FEBS Lett. , vol.112 , pp. 243-246
    • Soll, J.1    Douce, R.2    Schultz, G.3
  • 27
    • 0022049227 scopus 로고
    • Localization and synthesis of prenylquinones in isolated outer and inner envelope membranes from spinach chloroplasts
    • Soll, J., Schultz, G., Joyard J., Douce, R. and Block, M. (1985) Localization and synthesis of prenylquinones in isolated outer and inner envelope membranes from spinach chloroplasts. Arch. Biochem. Biophys. 238, 290-299.
    • (1985) Arch. Biochem. Biophys. , vol.238 , pp. 290-299
    • Soll, J.1    Schultz, G.2    Joyard, J.3    Douce, R.4    Block, M.5
  • 28
    • 0025264932 scopus 로고
    • Direct photolabeling of the EcoRII methyltransferase with S-adenosyl-L-methionine
    • Som, S. and Friedman, S. (1990) Direct photolabeling of the EcoRII methyltransferase with S-adenosyl-L-methionine. J. Biol. Chem. 265, 4278-4283.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4278-4283
    • Som, S.1    Friedman, S.2
  • 29
    • 0026700025 scopus 로고
    • Photolabeling of CheR methyltransferase with S-adenosyl-L-methionine (AdoMet). Studies on the AdoMet binding site
    • Subbaramaiah, K. and Simms, S.A. (1992) Photolabeling of CheR methyltransferase with S-adenosyl-L-methionine (AdoMet). Studies on the AdoMet binding site. J. Biol. Chem. 267, 8636-8642.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8636-8642
    • Subbaramaiah, K.1    Simms, S.A.2
  • 30
    • 0028144752 scopus 로고
    • MapA, an iron-regulated, cytoplasmic membrane protein in the cyanobacterium Synechococcus sp. strain PCC7942
    • Webb, R., Troyan, T., Sherman, D. and Sherman, L. (1994) MapA, an iron-regulated, cytoplasmic membrane protein in the cyanobacterium Synechococcus sp. strain PCC7942. J. Bacteriol. 176, 4906-4913.
    • (1994) J. Bacteriol. , vol.176 , pp. 4906-4913
    • Webb, R.1    Troyan, T.2    Sherman, D.3    Sherman, L.4
  • 31
    • 0028917799 scopus 로고
    • The 2-oxoglutarate/malate translocator of chloroplast envelope membranes: Molecular cloning of a transporter containing a 12-helix motif and expression of the functional protein in yeast cells
    • Weber, A., Menzlaff, E., Arbinger, B., Gutensohn, M., Eckerskorn, C. and Flügge, U.-I. (1995) The 2-oxoglutarate/malate translocator of chloroplast envelope membranes: molecular cloning of a transporter containing a 12-helix motif and expression of the functional protein in yeast cells Biochemistry, 34, 2621-2627.
    • (1995) Biochemistry , vol.34 , pp. 2621-2627
    • Weber, A.1    Menzlaff, E.2    Arbinger, B.3    Gutensohn, M.4    Eckerskorn, C.5    Flügge, U.-I.6


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