메뉴 건너뛰기




Volumn 34, Issue 2, 1998, Pages 112-119

Characterization of a galactose-1-phosphate uridylyltransferase gene from the marine red alga Graeilaria gracilis

Author keywords

Galactose metabolism; Gracilaria gracilis; Nuclear gene; Rhodophyceae; Uridylyltransferase

Indexed keywords

CELL NUCLEUS DNA; GALACTOSE 1 PHOSPHATE URIDYLYLTRANSFERASE; RIBONUCLEASE;

EID: 0031664501     PISSN: 01728083     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002940050374     Document Type: Article
Times cited : (16)

References (47)
  • 1
    • 3542997181 scopus 로고
    • A polyubiquitin cDNA from a red alga
    • Apt KE, Grossman AR (1992) A polyubiquitin cDNA from a red alga. Plant Physiol 99:1732-1733
    • (1992) Plant Physiol , vol.99 , pp. 1732-1733
    • Apt, K.E.1    Grossman, A.R.2
  • 2
    • 0027290730 scopus 로고
    • The γ subunit of R-phycoerythrin and its possible mode of transport into the plastid of red algae
    • Apt KE, Hoffman NE, Grossman AR (1993) The γ subunit of R-phycoerythrin and its possible mode of transport into the plastid of red algae. J Biol Chem 268:16208-16215
    • (1993) J Biol Chem , vol.268 , pp. 16208-16215
    • Apt, K.E.1    Hoffman, N.E.2    Grossman, A.R.3
  • 3
    • 51249168775 scopus 로고
    • World-wide use and importance of Gracilaria
    • Armisen R (1995) World-wide use and importance of Gracilaria. J Appl Phycol 7:231-243
    • (1995) J Appl Phycol , vol.7 , pp. 231-243
    • Armisen, R.1
  • 4
    • 0027950564 scopus 로고
    • Molecular relationships among the Gracilariaceae (Rhodophyta): Further observations on some undetermined species
    • Bird CJ, Ragan MA, Critchley AT, Rice EL, Gutell RR (1994) Molecular relationships among the Gracilariaceae (Rhodophyta): further observations on some undetermined species. Eur J Phycol 29:195-202
    • (1994) Eur J Phycol , vol.29 , pp. 195-202
    • Bird, C.J.1    Ragan, M.A.2    Critchley, A.T.3    Rice, E.L.4    Gutell, R.R.5
  • 5
    • 0002464211 scopus 로고
    • Cell walls
    • Cole KM, Sheath RG (eds) Cambridge University Press, Cambridge
    • Craigie JS (1990) Cell walls. In: Cole KM, Sheath RG (eds) Biology of the red algae. Cambridge University Press, Cambridge, pp 221-257
    • (1990) Biology of the Red Algae , pp. 221-257
    • Craigie, J.S.1
  • 6
    • 0002723873 scopus 로고
    • D-galactose-containing oligosaccharides
    • Dey PM, Dixon RA (eds) Academic Press, London
    • Dey PM (1985) D-galactose-containing oligosaccharides. In: Dey PM, Dixon RA (eds) Biochemistry of storage carbohydrates in green plants. Academic Press, London, pp 53-129
    • (1985) Biochemistry of Storage Carbohydrates in Green Plants , pp. 53-129
    • Dey, P.M.1
  • 7
    • 0000168271 scopus 로고
    • Effects of altered salinity, darkness, and algal nutrient status on floridoside and starch content, α-galactosidase activity and agar yield of cultivated Gracilaria sordida
    • Ekman P, Yu S, Pedersen M (1991) Effects of altered salinity, darkness, and algal nutrient status on floridoside and starch content, α-galactosidase activity and agar yield of cultivated Gracilaria sordida. Br Phycol J 26:123-131
    • (1991) Br Phycol J , vol.26 , pp. 123-131
    • Ekman, P.1    Yu, S.2    Pedersen, M.3
  • 9
    • 0024963669 scopus 로고
    • Galactose 1-phosphate uridylyltransferase: Identification of histidine-164 and histidine-166 as critical residues by site-directed mutagenesis
    • Field TL, Reznikoff WS, Frey PA (1989) Galactose 1-phosphate uridylyltransferase: identification of histidine-164 and histidine-166 as critical residues by site-directed mutagenesis. Biochemistry 28:2094-2099
    • (1989) Biochemistry , vol.28 , pp. 2094-2099
    • Field, T.L.1    Reznikoff, W.S.2    Frey, P.A.3
  • 10
    • 0029920614 scopus 로고    scopus 로고
    • The Leloir pathway: A mechanistic imperative for three enzymes to change the stereochemical configuration of a single carbon in galactose
    • Frey PA (1996) The Leloir pathway: a mechanistic imperative for three enzymes to change the stereochemical configuration of a single carbon in galactose. FASEB J 10:461-470
    • (1996) FASEB J , vol.10 , pp. 461-470
    • Frey, P.A.1
  • 11
    • 0020390815 scopus 로고
    • Galactose-1-phosphate uridyltransferase: Detection, isolation, and characterization of the uridyl enzyme
    • Frey PA, Wong L-J, Sheu K-F, Yang S-L (1982) Galactose-1-phosphate uridyltransferase: detection, isolation, and characterization of the uridyl enzyme. Methods Enzymol 87:20-36
    • (1982) Methods Enzymol , vol.87 , pp. 20-36
    • Frey, P.A.1    Wong, L.-J.2    Sheu, K.-F.3    Yang, S.-L.4
  • 12
    • 0000653208 scopus 로고
    • A potential pathway for galactose metabolism in Cucumis sativas L., a stachyose transporting species
    • Gross KC, Phar DM (1982) A potential pathway for galactose metabolism in Cucumis sativas L., a stachyose transporting species. Plant Physiol 69:117-121
    • (1982) Plant Physiol , vol.69 , pp. 117-121
    • Gross, K.C.1    Phar, D.M.2
  • 13
    • 0028851273 scopus 로고
    • Heterotrophic growth of two strains of the acido-thermophilic red alga Galdieria sulphuraria
    • Gross W, Schnarrenberger C (1995a) Heterotrophic growth of two strains of the acido-thermophilic red alga Galdieria sulphuraria. Plant Cell Physiol 36:633-638
    • (1995) Plant Cell Physiol , vol.36 , pp. 633-638
    • Gross, W.1    Schnarrenberger, C.2
  • 14
    • 0028790162 scopus 로고
    • Purification and characterization of a galactose-1-phosphate: UDP-glucose uridyltransferase from the red alga Galdieria sulphuraria
    • Gross W, Schnarrenberger C (1995b) Purification and characterization of a galactose-1-phosphate: UDP-glucose uridyltransferase from the red alga Galdieria sulphuraria. Eur J Biochem 234:258-263
    • (1995) Eur J Biochem , vol.234 , pp. 258-263
    • Gross, W.1    Schnarrenberger, C.2
  • 15
    • 0030473801 scopus 로고    scopus 로고
    • 3′-end-forming signals of yeast mRNA
    • Guo Z, Sherman F (1996) 3′-end-forming signals of yeast mRNA. Trends Biochem Sci 21:477-481
    • (1996) Trends Biochem Sci , vol.21 , pp. 477-481
    • Guo, Z.1    Sherman, F.2
  • 16
    • 0027355291 scopus 로고
    • Rat galactose-1-phosphate uridyltransferase coding sequence, transcription start site and genomic organization
    • Heidenreich RA, Mallee J, Segal S (1993) Rat galactose-1-phosphate uridyltransferase coding sequence, transcription start site and genomic organization. DNA Seq 3:311-318
    • (1993) DNA Seq , vol.3 , pp. 311-318
    • Heidenreich, R.A.1    Mallee, J.2    Segal, S.3
  • 17
    • 0026458378 scopus 로고
    • Amino-acid substitution matrices from protein blocks
    • Henikoff S, Henikoff JG (1992) Amino-acid substitution matrices from protein blocks. Proc Natl Acad Sci USA 89:10915-10919
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 19
    • 0023664776 scopus 로고
    • An inspection of the domain between putative TATA box and translation start site in 79 plant genes
    • Joshi CP (1987) An inspection of the domain between putative TATA box and translation start site in 79 plant genes. Nucleic Acids Res 15:6643-6653
    • (1987) Nucleic Acids Res , vol.15 , pp. 6643-6653
    • Joshi, C.P.1
  • 20
    • 0000426305 scopus 로고
    • Low-MW carbohydrates and ions in Rhodophyceae: Quantitative measurement of floridoside and digeneaside
    • Kirst GO (1980) Low-MW carbohydrates and ions in Rhodophyceae: quantitative measurement of floridoside and digeneaside. Phytochemistry 19:1107-1110
    • (1980) Phytochemistry , vol.19 , pp. 1107-1110
    • Kirst, G.O.1
  • 21
    • 0345211662 scopus 로고
    • Patterns of photoassimilatory products in Pacific Rhodophyceae
    • Kremer BP (1978) Patterns of photoassimilatory products in Pacific Rhodophyceae. Can J Bot 56:1655-1659
    • (1978) Can J Bot , vol.56 , pp. 1655-1659
    • Kremer, B.P.1
  • 22
    • 0000417759 scopus 로고
    • Biosynthesis of 2-O-D-glycerol-α-D-galactopyranoside (floridoside) in marine Rhodophyceae
    • Kremer BP, Kirst GO (1981) Biosynthesis of 2-O-D-glycerol-α-D-galactopyranoside (floridoside) in marine Rhodophyceae. Plant Sci Lett 23:349-357
    • (1981) Plant Sci Lett , vol.23 , pp. 349-357
    • Kremer, B.P.1    Kirst, G.O.2
  • 24
    • 0027748981 scopus 로고
    • The GAPDH gene system of the red alga Chondrus crispus: Promoter structures, intron/exon organization, genomic complexity and differential expression of genes
    • Liaud M-F, Valentin C, Brandt U, Bouget F-Y, Kloareg B, Cerff R (1993) The GAPDH gene system of the red alga Chondrus crispus: promoter structures, intron/exon organization, genomic complexity and differential expression of genes. Plant Mol Biol 23:981-994
    • (1993) Plant Mol Biol , vol.23 , pp. 981-994
    • Liaud, M.-F.1    Valentin, C.2    Brandt, U.3    Bouget, F.-Y.4    Kloareg, B.5    Cerff, R.6
  • 25
    • 0029294024 scopus 로고
    • The marine red alga Chondrus crispus has a highly divergent β-tubulin gene with a characteristic 5′ intron: Functional and evolutionary implications
    • Liaud M-F, Brandt U, Cerff R (1995) The marine red alga Chondrus crispus has a highly divergent β-tubulin gene with a characteristic 5′ intron: functional and evolutionary implications. Plant Mol Biol 28:313-325
    • (1995) Plant Mol Biol , vol.28 , pp. 313-325
    • Liaud, M.-F.1    Brandt, U.2    Cerff, R.3
  • 26
    • 0030697828 scopus 로고    scopus 로고
    • Expressed sequence tags (ESTs) from the marine red alga Gracilaria gracilis
    • Lluisma AO, Ragan MA (1997) Expressed sequence tags (ESTs) from the marine red alga Gracilaria gracilis. J Appl Phycol 9:287-293
    • (1997) J Appl Phycol , vol.9 , pp. 287-293
    • Lluisma, A.O.1    Ragan, M.A.2
  • 27
    • 0031693058 scopus 로고    scopus 로고
    • Cloning and characterization of a nuclear gene encoding a starch-branching enzyme from the marine red alga Gracilaria gracilis
    • in press
    • Lluisma AO, Ragan MA (1998) Cloning and characterization of a nuclear gene encoding a starch-branching enzyme from the marine red alga Gracilaria gracilis. Curr Genet (in press)
    • (1998) Curr Genet
    • Lluisma, A.O.1    Ragan, M.A.2
  • 28
    • 0002351669 scopus 로고
    • Regulation of carbon flow by nitrogen and light in the red alga, Gelidium coulteri
    • Macler BA (1986) Regulation of carbon flow by nitrogen and light in the red alga, Gelidium coulteri. Plant Physiol 82:136-141
    • (1986) Plant Physiol , vol.82 , pp. 136-141
    • Macler, B.A.1
  • 29
    • 0000991235 scopus 로고
    • Characteristics of a galactose-adapted sugarcane cell line grown in suspension culture
    • Maretzki A, Thom M (1978) Characteristics of a galactose-adapted sugarcane cell line grown in suspension culture. Plant Physiol 61:544-548
    • (1978) Plant Physiol , vol.61 , pp. 544-548
    • Maretzki, A.1    Thom, M.2
  • 30
    • 84989626317 scopus 로고
    • Variations in floridoside content and floridoside phosphate synthase activity in Porphyra perforata (Rhodophyta)
    • Meng J, Srivastava LM (1993) Variations in floridoside content and floridoside phosphate synthase activity in Porphyra perforata (Rhodophyta). J Phycol 29:82-84
    • (1993) J Phycol , vol.29 , pp. 82-84
    • Meng, J.1    Srivastava, L.M.2
  • 31
    • 0344686746 scopus 로고
    • Galactose-1-phosphate uridyl transferase activity in soybean extracts
    • Pazur JH, Shadaksharaswamy M (1961) Galactose-1-phosphate uridyl transferase activity in soybean extracts. Biochem Biophys Res Commun 5:130-134
    • (1961) Biochem Biophys Res Commun , vol.5 , pp. 130-134
    • Pazur, J.H.1    Shadaksharaswamy, M.2
  • 32
    • 0003039738 scopus 로고
    • Solute accumulation and osmotic adjustment
    • Cole KM, Sheath RG (eds) Cambridge University Press, Cambridge
    • Reed RH (1990) Solute accumulation and osmotic adjustment. In: Cole KM, Sheath RG (eds) Biology of the red algae. Cambridge University Press, Cambridge, pp 147-169
    • (1990) Biology of the Red Algae , pp. 147-169
    • Reed, R.H.1
  • 33
    • 0029057216 scopus 로고
    • Galactose-1-phosphate uridylyltransferase from Escherichia coli, a zinc and iron metalloenzyme
    • Ruzicka FJ, Wedekind JE, Kim J, Rayment I, Frey PA (1995) Galactose-1-phosphate uridylyltransferase from Escherichia coli, a zinc and iron metalloenzyme. Biochemistry 34:5610-5617
    • (1995) Biochemistry , vol.34 , pp. 5610-5617
    • Ruzicka, F.J.1    Wedekind, J.E.2    Kim, J.3    Rayment, I.4    Frey, P.A.5
  • 35
    • 0030158571 scopus 로고    scopus 로고
    • The Staden sequence analysis package
    • Staden R (1996) The Staden sequence analysis package. Mol Biotechnol 5:233-241
    • (1996) Mol Biotechnol , vol.5 , pp. 233-241
    • Staden, R.1
  • 36
    • 0022122705 scopus 로고
    • Primary structure of the Saccharomyces cerevisiae GAL7 gene
    • Tajima M, Nogi Y, Fukusawa T (1985) Primary structure of the Saccharomyces cerevisiae GAL7 gene. Yeast 1:67-77
    • (1985) Yeast , vol.1 , pp. 67-77
    • Tajima, M.1    Nogi, Y.2    Fukusawa, T.3
  • 37
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 38
    • 0029113143 scopus 로고
    • Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 Å resolution
    • Wedekind JE, Frey PA, Rayment I (1995) Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 Å resolution. Biochemistry 34:11049-11061
    • (1995) Biochemistry , vol.34 , pp. 11049-11061
    • Wedekind, J.E.1    Frey, P.A.2    Rayment, I.3
  • 39
    • 0029810819 scopus 로고    scopus 로고
    • The structure of nucleotidylated histidine-166 of galactose1-phosphate uridylyltransferase provides insight into phosphoryl group transfer
    • Wedekind JE, Frey PA, Rayment I (1996) The structure of nucleotidylated histidine-166 of galactose1-phosphate uridylyltransferase provides insight into phosphoryl group transfer. Biochemistry 35:11560-11569
    • (1996) Biochemistry , vol.35 , pp. 11560-11569
    • Wedekind, J.E.1    Frey, P.A.2    Rayment, I.3
  • 40
    • 0029360329 scopus 로고
    • The formation of mRNA 3′ ends in plants
    • Wu L, Ueda T, Messing J (1995) The formation of mRNA 3′ ends in plants. Plant J 8:323-329
    • (1995) Plant J , vol.8 , pp. 323-329
    • Wu, L.1    Ueda, T.2    Messing, J.3
  • 41
    • 0000589366 scopus 로고
    • The α-galactosidase of Gracilaria tenuistipitata and G. sordida (Gracilariales, Rhodophyta)
    • Yu S, Pedersen M (1990) The α-galactosidase of Gracilaria tenuistipitata and G. sordida (Gracilariales, Rhodophyta). Phycologia 29:454-460
    • (1990) Phycologia , vol.29 , pp. 454-460
    • Yu, S.1    Pedersen, M.2
  • 42
    • 0027285537 scopus 로고
    • cDNA cloning and characterization of the nuclear gene encoding chloroplast glyceraldehyde-3-phosphate dehydrogenase from the marine red alga Gracilaria verrucosa
    • Zhou Y-H, Ragan MA (1993) cDNA cloning and characterization of the nuclear gene encoding chloroplast glyceraldehyde-3-phosphate dehydrogenase from the marine red alga Gracilaria verrucosa. Curr Genet 23:483-489
    • (1993) Curr Genet , vol.23 , pp. 483-489
    • Zhou, Y.-H.1    Ragan, M.A.2
  • 43
    • 0028357394 scopus 로고
    • Cloning and characterization of the nuclear gene encoding plastid glyceraldehyde-3-phosphate dehydrogenase from the marine red alga Gracilaria verrucosa
    • Zhou Y-H, Ragan MA (1994) Cloning and characterization of the nuclear gene encoding plastid glyceraldehyde-3-phosphate dehydrogenase from the marine red alga Gracilaria verrucosa. Curr Genet 26:79-86
    • (1994) Curr Genet , vol.26 , pp. 79-86
    • Zhou, Y.-H.1    Ragan, M.A.2
  • 44
    • 0029328318 scopus 로고
    • Characterization of the nuclear gene encoding mitochondrial aconitase in the marine red alga Gracilaria verrucosa
    • Zhou Y-H, Ragan MA (1995a) Characterization of the nuclear gene encoding mitochondrial aconitase in the marine red alga Gracilaria verrucosa. Plant Mol Biol 28:635-646
    • (1995) Plant Mol Biol , vol.28 , pp. 635-646
    • Zhou, Y.-H.1    Ragan, M.A.2
  • 45
    • 0029133476 scopus 로고
    • Cloning and characterization of the nuclear gene and cDNAs for triosephosphate isomerase of the marine red alga Gracilaria verrucosa
    • Zhou Y-H, Ragan MA (1995b) Cloning and characterization of the nuclear gene and cDNAs for triosephosphate isomerase of the marine red alga Gracilaria verrucosa. Curr Genet 28:317-323
    • (1995) Curr Genet , vol.28 , pp. 317-323
    • Zhou, Y.-H.1    Ragan, M.A.2
  • 46
    • 0029113590 scopus 로고
    • The nuclear gene andcDNAs encoding cytosolic glyceraldehyde-3-phosphate dehydrogenase from the marine red alga Gracilaria verrucosa: Cloning, characterization and phylogenetic analysis
    • Zhou Y-H, Ragan MA (1995c) The nuclear gene andcDNAs encoding cytosolic glyceraldehyde-3-phosphate dehydrogenase from the marine red alga Gracilaria verrucosa: cloning, characterization and phylogenetic analysis. Curr Genet 28:324-332
    • (1995) Curr Genet , vol.28 , pp. 324-332
    • Zhou, Y.-H.1    Ragan, M.A.2
  • 47
    • 0029827979 scopus 로고    scopus 로고
    • Nuclear-encoded protein-encoding genes of the agarophyte Gracilaria verrucosa (Gracilariales, Rhodophyta)
    • Lindstrom SC, Chapman DJ (eds)
    • Zhou Y-H, Ragan MA (1996) Nuclear-encoded protein-encoding genes of the agarophyte Gracilaria verrucosa (Gracilariales, Rhodophyta). In: Lindstrom SC, Chapman DJ (eds) Hydrobiologia 326/327:429-436
    • (1996) Hydrobiologia , vol.326-327 , pp. 429-436
    • Zhou, Y.-H.1    Ragan, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.