메뉴 건너뛰기




Volumn 123, Issue 3, 2000, Pages 1163-1171

β-Cyanoalanine synthase is a mitochondrial cysteine synthase-like protein in spinach and Arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

BETA CYANOALANINE SYNTHASE; COMPLEMENTARY DNA; CYANIDE; CYSTEINE SYNTHASE LIKE PROTEIN; ENZYME ACTIVITY; ENZYME ISOFORM; EXPRESSED SEQUENCE TAG; MITOCHONDRION; RECOMBINANT PROTEIN; SEQUENCE HOMOLOGY; SPINACIA OLERACEA;

EID: 0033927405     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.123.3.1163     Document Type: Article
Times cited : (177)

References (49)
  • 2
    • 0014430124 scopus 로고
    • Cyanide metabolism in higher plants: III. The biosynthesis of β-cyanoalanine
    • Blumenthal S, Hendrickson H, Abrol Y, Conn E (1968) Cyanide metabolism in higher plants: III. The biosynthesis of β-cyanoalanine. J Biol Chem 243: 5302-5307
    • (1968) J Biol Chem , vol.243 , pp. 5302-5307
    • Blumenthal, S.1    Hendrickson, H.2    Abrol, Y.3    Conn, E.4
  • 3
    • 0031079570 scopus 로고    scopus 로고
    • Cysteine synthesis in plants: Protein-protein interactions of serine acetyltransferase from Arabidopsis thaliana
    • Bogdanova N, Hell R (1997) Cysteine synthesis in plants: protein-protein interactions of serine acetyltransferase from Arabidopsis thaliana. Plant J 11: 251-262
    • (1997) Plant J , vol.11 , pp. 251-262
    • Bogdanova, N.1    Hell, R.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 5
    • 0015402509 scopus 로고
    • Cyanide metabolism in higher plants: V. The formation of asparagine from β-cyanoalanine
    • Castric P, Farnden K, Conn E (1972) Cyanide metabolism in higher plants: V. The formation of asparagine from β-cyanoalanine. Arch Biochem Biophys 152: 62-69
    • (1972) Arch Biochem Biophys , vol.152 , pp. 62-69
    • Castric, P.1    Farnden, K.2    Conn, E.3
  • 6
    • 0027320121 scopus 로고
    • Cysteine biosynthesis in Saccharomyces cerevisiae occurs through the transsulfuration pathway which has been built up by enzyme recruitment
    • Cherest H, Thomas D, Surdin-Kerjan Y (1993) Cysteine biosynthesis in Saccharomyces cerevisiae occurs through the transsulfuration pathway which has been built up by enzyme recruitment. J Bacteriol 175: 5366-5374
    • (1993) J Bacteriol , vol.175 , pp. 5366-5374
    • Cherest, H.1    Thomas, D.2    Surdin-Kerjan, Y.3
  • 7
    • 0026637901 scopus 로고
    • Purification and characterization of O-acetylserine(thiol) lyase from spinach chloroplasts
    • Droux M, Martins J, Sajus P, Douce R (1992) Purification and characterization of O-acetylserine(thiol) lyase from spinach chloroplasts. Arch Biochem Biophys 295: 379-390
    • (1992) Arch Biochem Biophys , vol.295 , pp. 379-390
    • Droux, M.1    Martins, J.2    Sajus, P.3    Douce, R.4
  • 8
    • 0032125745 scopus 로고    scopus 로고
    • Interactions between serine acetyltransferase and O-acetylserine(thiol) lyase in higher plants: Structural and kinetic properties of the free and bound enzymes
    • Droux M, Ruffet M, Douce R, Job D (1998) Interactions between serine acetyltransferase and O-acetylserine(thiol) lyase in higher plants: structural and kinetic properties of the free and bound enzymes. Eur J Biochem 255: 235-245
    • (1998) Eur J Biochem , vol.255 , pp. 235-245
    • Droux, M.1    Ruffet, M.2    Douce, R.3    Job, D.4
  • 9
    • 0013850975 scopus 로고
    • Enzymatic formation of β-cyanoalanine from cyanide by Escherichia coli extracts
    • Dunnill P, Fowden L (1965) Enzymatic formation of β-cyanoalanine from cyanide by Escherichia coli extracts. Nature 208: 1206-1207
    • (1965) Nature , vol.208 , pp. 1206-1207
    • Dunnill, P.1    Fowden, L.2
  • 10
    • 0013850979 scopus 로고
    • Enzymatic formation of β-cyanoalanine from cyanide
    • Floss H, Hadwiger L, Conn E (1965) Enzymatic formation of β-cyanoalanine from cyanide. Nature 208: 1207-1208
    • (1965) Nature , vol.208 , pp. 1207-1208
    • Floss, H.1    Hadwiger, L.2    Conn, E.3
  • 11
    • 0014118789 scopus 로고
    • A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids
    • Gaitonde M (1967) A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids. Biochem J 104: 627-633
    • (1967) Biochem J , vol.104 , pp. 627-633
    • Gaitonde, M.1
  • 12
    • 0028045313 scopus 로고
    • Presence of β-cyanoalanine synthase in unimbibed dry seeds and its activation by ethylene during pre-germination
    • Hasegawa R, Tada T, Torii Y, Esashi Y (1994) Presence of β-cyanoalanine synthase in unimbibed dry seeds and its activation by ethylene during pre-germination. Physiol Plant 91: 141-146
    • (1994) Physiol Plant , vol.91 , pp. 141-146
    • Hasegawa, R.1    Tada, T.2    Torii, Y.3    Esashi, Y.4
  • 13
    • 0028025227 scopus 로고
    • Isolation and characterization of two cDNAs encoding for compartment specific isoforms of O-acetylserine(thiol) lyase from Arabidopsis thaliana
    • Hell R, Bork C, Bogdanova N, Frolov I, Hauschild R (1994) Isolation and characterization of two cDNAs encoding for compartment specific isoforms of O-acetylserine(thiol) lyase from Arabidopsis thaliana. FEBS Lett 351: 257-262
    • (1994) FEBS Lett , vol.351 , pp. 257-262
    • Hell, R.1    Bork, C.2    Bogdanova, N.3    Frolov, I.4    Hauschild, R.5
  • 14
    • 0014690491 scopus 로고
    • Cyanide metabolism in higher plants: IV. Purification and properties of the β-cyanoalanine synthase of blue lupin
    • Hendrickson H, Conn E (1969) Cyanide metabolism in higher plants: IV. Purification and properties of the β-cyanoalanine synthase of blue lupin. J Biol Chem 244: 2632-2640
    • (1969) J Biol Chem , vol.244 , pp. 2632-2640
    • Hendrickson, H.1    Conn, E.2
  • 15
    • 0032915394 scopus 로고    scopus 로고
    • Molecular cloning and expression analyses of mitochondrial and plastidic isoforms of cysteine synthase (O-acetylserine (thiol) lyase) from Arabidopsis thaliana
    • Hesse H, Lipke J, Altmann T, Hofgen R (1999) Molecular cloning and expression analyses of mitochondrial and plastidic isoforms of cysteine synthase (O-acetylserine (thiol) lyase) from Arabidopsis thaliana. Amino Acids 16: 113-131
    • (1999) Amino Acids , vol.16 , pp. 113-131
    • Hesse, H.1    Lipke, J.2    Altmann, T.3    Hofgen, R.4
  • 16
    • 44049111777 scopus 로고
    • Purification and characterization of two forms of cysteine synthase from Allium tuberosum
    • Ikegami F, Itagaki S, Murakoshi I (1993) Purification and characterization of two forms of cysteine synthase from Allium tuberosum. Phytochemistry 32: 31-34
    • (1993) Phytochemistry , vol.32 , pp. 31-34
    • Ikegami, F.1    Itagaki, S.2    Murakoshi, I.3
  • 17
    • 0028133985 scopus 로고
    • Enzymic synthesis of non-protein β-substituted alanines and some higher homologues in plants
    • Ikegami F, Murakoshi I (1994) Enzymic synthesis of non-protein β-substituted alanines and some higher homologues in plants. Phytochemistry 35: 1089-1104
    • (1994) Phytochemistry , vol.35 , pp. 1089-1104
    • Ikegami, F.1    Murakoshi, I.2
  • 18
    • 38249031429 scopus 로고
    • Purification and properties of β-cyano-L-alanine synthase from Lathyrus latifolius
    • Ikegami F, Takayama K, Murakoshi I (1988a) Purification and properties of β-cyano-L-alanine synthase from Lathyrus latifolius. Phytochemistry 27: 3385-3389
    • (1988) Phytochemistry , vol.27 , pp. 3385-3389
    • Ikegami, F.1    Takayama, K.2    Murakoshi, I.3
  • 19
    • 38249032944 scopus 로고
    • Purification and properties of β-cyano-L-alanine synthase from Spinacia oleracea
    • Ikegami F, Takayama K, Tajima C, Murakoshi I (1988b) Purification and properties of β-cyano-L-alanine synthase from Spinacia oleracea. Phytochemistry 27: 2011-2016
    • (1988) Phytochemistry , vol.27 , pp. 2011-2016
    • Ikegami, F.1    Takayama, K.2    Tajima, C.3    Murakoshi, I.4
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 21
    • 0001113803 scopus 로고
    • Localization of ATP sulfurylase and O-acetylserine(thiol) lyase in spinach leaves
    • Lunn J, Droux M, Martin J, Douce R (1990) Localization of ATP sulfurylase and O-acetylserine(thiol) lyase in spinach leaves. Plant Physiol 94: 1345-1352
    • (1990) Plant Physiol , vol.94 , pp. 1345-1352
    • Lunn, J.1    Droux, M.2    Martin, J.3    Douce, R.4
  • 22
    • 0034055164 scopus 로고    scopus 로고
    • Purification and characterization of β-cyanoalanine synthase and cysteine synthases from potato tubers: Are β-cyanoalanine synthase and mitochondrial cysteine synthase the same enzyme?
    • Maruyama A, Ishizawa K, Takagi T (2000) Purification and characterization of β-cyanoalanine synthase and cysteine synthases from potato tubers: are β-cyanoalanine synthase and mitochondrial cysteine synthase the same enzyme? Plant Cell Physiol 41: 200-208
    • (2000) Plant Cell Physiol , vol.41 , pp. 200-208
    • Maruyama, A.1    Ishizawa, K.2    Takagi, T.3
  • 23
    • 0031850228 scopus 로고    scopus 로고
    • Cytosolic β-cyanoalanine synthase activity attributed to cysteine synthases in cocklebur seeds: Purification and characterization of cytosolic cysteine synthases
    • Maruyama A, Ishizawa K, Takagi T, Esashi Y (1998) Cytosolic β-cyanoalanine synthase activity attributed to cysteine synthases in cocklebur seeds: purification and characterization of cytosolic cysteine synthases. Plant Cell Physiol 39: 671-680
    • (1998) Plant Cell Physiol , vol.39 , pp. 671-680
    • Maruyama, A.1    Ishizawa, K.2    Takagi, T.3    Esashi, Y.4
  • 24
    • 0016505439 scopus 로고
    • Cysteine synthase from rape leaves
    • Masada M, Fukushima K, Tamura G (1975) Cysteine synthase from rape leaves. J Biochem 77: 1107-1115
    • (1975) J Biochem , vol.77 , pp. 1107-1115
    • Masada, M.1    Fukushima, K.2    Tamura, G.3
  • 25
    • 0001269713 scopus 로고
    • Purification and properties of β-cyanoalanine synthase from the cyanide-producing bacterium Chromobacterium violacenm
    • McAdam A, Knowles C (1984) Purification and properties of β-cyanoalanine synthase from the cyanide-producing bacterium Chromobacterium violacenm. Biochem Biophys Acta 786: 123-132
    • (1984) Biochem Biophys Acta , vol.786 , pp. 123-132
    • McAdam, A.1    Knowles, C.2
  • 26
    • 0026094953 scopus 로고
    • Link between L-3-cyanoalanine synthase activity and differential cyanide sensitivity of insects
    • Meyers D, Ahmad S (1991) Link between L-3-cyanoalanine synthase activity and differential cyanide sensitivity of insects. Biochim Biophys Acta 1075: 195-197
    • (1991) Biochim Biophys Acta , vol.1075 , pp. 195-197
    • Meyers, D.1    Ahmad, S.2
  • 27
    • 0001626381 scopus 로고
    • Metabolism of hydrogen cyanaide by higher plants
    • Miller J, Conn E (1980) Metabolism of hydrogen cyanaide by higher plants. Plant Physiol 65: 1199-1202
    • (1980) Plant Physiol , vol.65 , pp. 1199-1202
    • Miller, J.1    Conn, E.2
  • 28
    • 0027105007 scopus 로고
    • A knowledge base for predicting protein localization sites in eukaryotic cells
    • Nakai K, Kanehisa M (1992) A knowledge base for predicting protein localization sites in eukaryotic cells. Genomics 14: 897-911
    • (1992) Genomics , vol.14 , pp. 897-911
    • Nakai, K.1    Kanehisa, M.2
  • 29
    • 0032483994 scopus 로고    scopus 로고
    • Isoform-dependant differences in feedback regulation and subcellular localization of serine acetyltransferase involved in cysteine biosynthesis from Arabidopsis thaliana
    • Noji M, Inoue K, Kimura N, Gouda A, Saito K (1998) Isoform-dependant differences in feedback regulation and subcellular localization of serine acetyltransferase involved in cysteine biosynthesis from Arabidopsis thaliana. J Biol Chem 273: 32739-32745
    • (1998) J Biol Chem , vol.273 , pp. 32739-32745
    • Noji, M.1    Inoue, K.2    Kimura, N.3    Gouda, A.4    Saito, K.5
  • 30
    • 0001213003 scopus 로고
    • Formation of cyanide from carbon 1 of 1-aminocydopropane-1-carboxylic acid during its conversion to ethylene
    • Peiser G, Wang T-T, Hoffman N, Yang S-F, Liu H-W, Walsh C (1984) Formation of cyanide from carbon 1 of 1-aminocydopropane-1-carboxylic acid during its conversion to ethylene. Proc Natl Acad Sci USA 81: 3059-3063
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 3059-3063
    • Peiser, G.1    Wang, T.-T.2    Hoffman, N.3    Yang, S.-F.4    Liu, H.-W.5    Walsh, C.6
  • 31
    • 0014666771 scopus 로고
    • Toxic principle in vetch: Isolation and identification of γ-L-glutamyl-L-β-cyanoalanine from common vetch seeds: Distribution in some legumes
    • Ressler C, Nigam S, Giza Y (1969) Toxic principle in vetch: isolation and identification of γ-L-glutamyl-L-β-cyanoalanine from common vetch seeds: distribution in some legumes. J Am Chem Soc 91: 2758-2765
    • (1969) J Am Chem Soc , vol.91 , pp. 2758-2765
    • Ressler, C.1    Nigam, S.2    Giza, Y.3
  • 32
    • 0000153222 scopus 로고
    • Subcellular distribution of O-acetylserine(thiol) lyase in cauliflower (Brassica oleracea L.) inflorescence
    • Rolland N, Droux M, Douce R (1992) Subcellular distribution of O-acetylserine(thiol) lyase in cauliflower (Brassica oleracea L.) inflorescence. Plant Physiol 98: 927-935
    • (1992) Plant Physiol , vol.98 , pp. 927-935
    • Rolland, N.1    Droux, M.2    Douce, R.3
  • 33
    • 0027279804 scopus 로고
    • O-acetylserine(thiol) lyase from spinach (Spinacia oleracea L.) leaf: cDNA cloning, characterization, and overexpression in Escherichia coli of the chloroplast isoform
    • Rolland N, Droux M, Lebrun M, Douce R (1993) O-acetylserine(thiol) lyase from spinach (Spinacia oleracea L.) leaf: cDNA cloning, characterization, and overexpression in Escherichia coli of the chloroplast isoform. Arch Biochem Biophys 300: 213-222
    • (1993) Arch Biochem Biophys , vol.300 , pp. 213-222
    • Rolland, N.1    Droux, M.2    Lebrun, M.3    Douce, R.4
  • 34
    • 0026770274 scopus 로고
    • Molecular cloning and bacterial expression of cDNA encoding a plant cysteine synthase
    • Saito K, Miura N, Yamazaki M, Hirano H, Murakoshi I (1992) Molecular cloning and bacterial expression of cDNA encoding a plant cysteine synthase. Proc Natl Acad Sci USA 89: 8078-8082
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8078-8082
    • Saito, K.1    Miura, N.2    Yamazaki, M.3    Hirano, H.4    Murakoshi, I.5
  • 35
    • 0025913926 scopus 로고
    • Integration and expression of a rabbit liver cytochrome P-450 gene in transgenic Nicotiana tabacum
    • Saito K, Noji M, Ohmori S, Imai Y, Murakoshi I (1991) Integration and expression of a rabbit liver cytochrome P-450 gene in transgenic Nicotiana tabacum. Proc Natl Acad Sci USA 88: 7041-7045
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7041-7045
    • Saito, K.1    Noji, M.2    Ohmori, S.3    Imai, Y.4    Murakoshi, I.5
  • 36
    • 0027288172 scopus 로고
    • cDNA cloning and expression of cysteine synthase B localized in chloroplasts of Spinacia oleracea
    • Saito K, Tatsuguchi K, Murakoshi I, Hirano H (1993) cDNA cloning and expression of cysteine synthase B localized in chloroplasts of Spinacia oleracea. FEBS Lett 324: 247-252
    • (1993) FEBS Lett , vol.324 , pp. 247-252
    • Saito, K.1    Tatsuguchi, K.2    Murakoshi, I.3    Hirano, H.4
  • 37
    • 0028097282 scopus 로고
    • Isolation and characterization of cDNA that encodes a putative mitochondrion-localizing isoform of cysteine synthase (O-acetylserine(thiol) lyase) from Spinacia oleracea
    • Saito K, Tatsuguchi K, Takagi Y, Murakoshi I (1994) Isolation and characterization of cDNA that encodes a putative mitochondrion-localizing isoform of cysteine synthase (O-acetylserine(thiol) lyase) from Spinacia oleracea. J Biol Chem 269: 28187-28192
    • (1994) J Biol Chem , vol.269 , pp. 28187-28192
    • Saito, K.1    Tatsuguchi, K.2    Takagi, Y.3    Murakoshi, I.4
  • 38
    • 0029028281 scopus 로고
    • Molecular cloning and characterization of a plant serine acetyltransferase playing a regulatory role in cysteine biosynthesis from watermelon
    • Saito K, Yokoyama H, Noji M, Murakoshi I (1995) Molecular cloning and characterization of a plant serine acetyltransferase playing a regulatory role in cysteine biosynthesis from watermelon. J Biol Chem 270: 16321-16326
    • (1995) J Biol Chem , vol.270 , pp. 16321-16326
    • Saito, K.1    Yokoyama, H.2    Noji, M.3    Murakoshi, I.4
  • 40
    • 0002326857 scopus 로고
    • Cysteine synthase
    • P Lea, P Dey, J Harborne, eds, Academic Press, New York
    • Schmidt A (1990) Cysteine synthase. In P Lea, P Dey, J Harborne, eds, Methods in Plant Biochemistry, Vol 3. Academic Press, New York, pp 349-354
    • (1990) Methods in Plant Biochemistry , vol.3 , pp. 349-354
    • Schmidt, A.1
  • 42
    • 0026933289 scopus 로고
    • A mess of red pottage
    • Tate M, Enneking D (1992) A mess of red pottage. Nature 359: 357-358
    • (1992) Nature , vol.359 , pp. 357-358
    • Tate, M.1    Enneking, D.2
  • 43
    • 0031457095 scopus 로고    scopus 로고
    • Metabolism of sulfur amino-acids in Saccharomyces cercvisiae
    • Thomas D, Surdin-Kerjan Y (1997) Metabolism of sulfur amino-acids in Saccharomyces cercvisiae. Microbiol Mol Biol Rev 61: 503-532
    • (1997) Microbiol Mol Biol Rev , vol.61 , pp. 503-532
    • Thomas, D.1    Surdin-Kerjan, Y.2
  • 44
    • 0031574072 scopus 로고    scopus 로고
    • The clustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 24: 4876-4882
    • (1997) Nucleic Acids Res , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 45
    • 0031669094 scopus 로고    scopus 로고
    • Separation, subcellular location and influence of sulphur nutrition on isoforms of cysteine synthase in spinach
    • Warrilow A, Hawkesford M (1998) Separation, subcellular location and influence of sulphur nutrition on isoforms of cysteine synthase in spinach. J Exp Bot 49: 1625-1636
    • (1998) J Exp Bot , vol.49 , pp. 1625-1636
    • Warrilow, A.1    Hawkesford, M.2
  • 46
    • 0034121969 scopus 로고    scopus 로고
    • Cysteine synthase (O-acetylserine(thiol) lyase) substrate specificities classify the mitochondrial isoform as a cyanoalanine synthase
    • in press
    • Warrilow A, Hawkesford M (2000) Cysteine synthase (O-acetylserine(thiol) lyase) substrate specificities classify the mitochondrial isoform as a cyanoalanine synthase. J Exp Bot (in press)
    • (2000) J Exp Bot
    • Warrilow, A.1    Hawkesford, M.2
  • 47
    • 0001237406 scopus 로고
    • Cyanide metabolism in relation to ethylene production in plant tissues
    • Yip W-K, Yang S (1988) Cyanide metabolism in relation to ethylene production in plant tissues. Plant Physiol 88: 473-476
    • (1988) Plant Physiol , vol.88 , pp. 473-476
    • Yip, W.-K.1    Yang, S.2
  • 48
    • 0027688450 scopus 로고
    • Tobacco plants transformed with the O-acetylserine(thiol) lyase gene of wheat are resistant to toxic levels of hydrogen sulphide gas
    • Youssefian S, Nakamura M, Sano H (1993) Tobacco plants transformed with the O-acetylserine(thiol) lyase gene of wheat are resistant to toxic levels of hydrogen sulphide gas. Plant J 4: 759-769
    • (1993) Plant J , vol.4 , pp. 759-769
    • Youssefian, S.1    Nakamura, M.2    Sano, H.3
  • 49
    • 0028693407 scopus 로고
    • Ethylene biosynthesis and action: A case of conservation
    • Zarembinski T, Theologis A (1994) Ethylene biosynthesis and action: a case of conservation. Plant Mol Biol 26: 1579-1597
    • (1994) Plant Mol Biol , vol.26 , pp. 1579-1597
    • Zarembinski, T.1    Theologis, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.