Cloning and nucleotide sequence of the alpha-galactosidase cDNA from Cyamopsis tetragonoloba (guar)
Polyadenylated mRNA was purified from the aleurone cells of Cyamopsis tetragonoloba (guar) seeds germinated for 18 h and used for the construction of a cDNA library. Clones with the alpha-galactosidase encoding gene were identified using oligo-nucleotide mixed probes based on the NH2 terminal amino...
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Veröffentlicht in: | Plant molecular biology 1989-11, Vol.13 (5), p.541-550 |
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description | Polyadenylated mRNA was purified from the aleurone cells of Cyamopsis tetragonoloba (guar) seeds germinated for 18 h and used for the construction of a cDNA library. Clones with the alpha-galactosidase encoding gene were identified using oligo-nucleotide mixed probes based on the NH2 terminal amino acid sequence and on the sequence of an internal peptide. The nucleotide sequence of the cDNA clone showed that the enzyme is synthesized as a precursor with a 47 amino acid NH2 terminal extension. This pre-sequence most likely functions to target the protein outside the aleurone cells into the endosperm. Based upon structural features, it is proposed to divide the precursor into a pre-(signal sequence) part and a glycosylated pro-part comparable with those of the yeast mat A/alpha factor and killer factor. A comparison of the derived amino acid sequence of this alpha-galactosidase from plant origin revealed significant stretches of homology with respect to the amino acid sequences of the enzymes from Saccharomyces cerevisiae and from human origin but only to a minor extent compared with the alpha-galactosidase from Escherichia coli. |
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(Unilever Research Lab., Vlaardingen (Netherlands)) ; Fellinger, A.J ; Toonen, M.Y ; Wassenaar, D. van ; Verrips, C.T</creator><creatorcontrib>Overbeeke, N. (Unilever Research Lab., Vlaardingen (Netherlands)) ; Fellinger, A.J ; Toonen, M.Y ; Wassenaar, D. van ; Verrips, C.T</creatorcontrib><description>Polyadenylated mRNA was purified from the aleurone cells of Cyamopsis tetragonoloba (guar) seeds germinated for 18 h and used for the construction of a cDNA library. Clones with the alpha-galactosidase encoding gene were identified using oligo-nucleotide mixed probes based on the NH2 terminal amino acid sequence and on the sequence of an internal peptide. The nucleotide sequence of the cDNA clone showed that the enzyme is synthesized as a precursor with a 47 amino acid NH2 terminal extension. This pre-sequence most likely functions to target the protein outside the aleurone cells into the endosperm. Based upon structural features, it is proposed to divide the precursor into a pre-(signal sequence) part and a glycosylated pro-part comparable with those of the yeast mat A/alpha factor and killer factor. A comparison of the derived amino acid sequence of this alpha-galactosidase from plant origin revealed significant stretches of homology with respect to the amino acid sequences of the enzymes from Saccharomyces cerevisiae and from human origin but only to a minor extent compared with the alpha-galactosidase from Escherichia coli.</description><identifier>ISSN: 0167-4412</identifier><identifier>EISSN: 1573-5028</identifier><identifier>DOI: 10.1007/BF00027314</identifier><identifier>PMID: 2577496</identifier><identifier>CODEN: PMBIDB</identifier><language>eng</language><publisher>Dordrecht: Springer</publisher><subject>ADN ; alpha -galactosidase ; Amino Acid Sequence ; Base Sequence ; Biological and medical sciences ; Biotechnology ; CLONACION ; CLONAGE ; CLONING ; Cloning, Molecular ; CODE GENETIQUE ; CODIGO GENETICO ; CYAMOPSIS PSORALIOIDES ; DNA ; DNA - genetics ; Enzyme Precursors - genetics ; Fundamental and applied biological sciences. Psychology ; GALACTOSIDASA ; GALACTOSIDASE ; GALACTOSIDASES ; Galactosidases - genetics ; genes ; Genes. Genome ; GENETIC CODE ; Genetic engineering ; Genetic technics ; Humans ; Methods. Procedures. 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(Unilever Research Lab., Vlaardingen (Netherlands))</creatorcontrib><creatorcontrib>Fellinger, A.J</creatorcontrib><creatorcontrib>Toonen, M.Y</creatorcontrib><creatorcontrib>Wassenaar, D. van</creatorcontrib><creatorcontrib>Verrips, C.T</creatorcontrib><title>Cloning and nucleotide sequence of the alpha-galactosidase cDNA from Cyamopsis tetragonoloba (guar)</title><title>Plant molecular biology</title><addtitle>Plant Mol Biol</addtitle><description>Polyadenylated mRNA was purified from the aleurone cells of Cyamopsis tetragonoloba (guar) seeds germinated for 18 h and used for the construction of a cDNA library. Clones with the alpha-galactosidase encoding gene were identified using oligo-nucleotide mixed probes based on the NH2 terminal amino acid sequence and on the sequence of an internal peptide. The nucleotide sequence of the cDNA clone showed that the enzyme is synthesized as a precursor with a 47 amino acid NH2 terminal extension. This pre-sequence most likely functions to target the protein outside the aleurone cells into the endosperm. Based upon structural features, it is proposed to divide the precursor into a pre-(signal sequence) part and a glycosylated pro-part comparable with those of the yeast mat A/alpha factor and killer factor. A comparison of the derived amino acid sequence of this alpha-galactosidase from plant origin revealed significant stretches of homology with respect to the amino acid sequences of the enzymes from Saccharomyces cerevisiae and from human origin but only to a minor extent compared with the alpha-galactosidase from Escherichia coli.</description><subject>ADN</subject><subject>alpha -galactosidase</subject><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>CLONACION</subject><subject>CLONAGE</subject><subject>CLONING</subject><subject>Cloning, Molecular</subject><subject>CODE GENETIQUE</subject><subject>CODIGO GENETICO</subject><subject>CYAMOPSIS PSORALIOIDES</subject><subject>DNA</subject><subject>DNA - genetics</subject><subject>Enzyme Precursors - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GALACTOSIDASA</subject><subject>GALACTOSIDASE</subject><subject>GALACTOSIDASES</subject><subject>Galactosidases - genetics</subject><subject>genes</subject><subject>Genes. Genome</subject><subject>GENETIC CODE</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>Humans</subject><subject>Methods. Procedures. Technologies</subject><subject>Molecular and cellular biology</subject><subject>Molecular cloning</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Plants - enzymology</subject><subject>Plants - genetics</subject><subject>Poly A - genetics</subject><subject>Restriction Mapping</subject><subject>RNA, Messenger - genetics</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Species Specificity</subject><issn>0167-4412</issn><issn>1573-5028</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0E1v1DAQBmALgcpSuHBEQvIBIaiUYsdf8bFsKUValQuco4kzToOceGsnh_573O6qHDnNYR69M3oJecvZOWfMfPl6xRirjeDyGdlwZUSlWN08JxvGtamk5PVL8irnP4wVLvQJOamVMdLqDXHbEOdxHijMPZ1XFzAuY480492Ks0MaPV1ukULY30I1QAC3xDz2kJG6y5sL6lOc6PYeprjPY6YLLgmGOMcQO6CfhhXS59fkhYeQ8c1xnpLfV99-ba-r3c_vP7YXu8oJzZeqq41kTiN41ysBTjfOGI891NZK5NKKru6swMYp5FqwTkivgHFrtbPGKnFKPh5y9ymW7_PSTmN2GALMGNfcFmOs5PK_kCtRQhtR4NkBuhRzTujbfRonSPctZ-1D9e2_6gt-f0xduwn7J3rsuuw_HPeQHQSfYHZjfmJaK2Ueb747MA-xhSEVcrOz5UrTMPEXe5uScg</recordid><startdate>19891101</startdate><enddate>19891101</enddate><creator>Overbeeke, N. 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(Unilever Research Lab., Vlaardingen (Netherlands)) ; Fellinger, A.J ; Toonen, M.Y ; Wassenaar, D. van ; Verrips, C.T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c361t-b2740c6eafcd53ac68c77feda2994e1493b2b93e8c5e1630b34f5a01996c97953</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>ADN</topic><topic>alpha -galactosidase</topic><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>CLONACION</topic><topic>CLONAGE</topic><topic>CLONING</topic><topic>Cloning, Molecular</topic><topic>CODE GENETIQUE</topic><topic>CODIGO GENETICO</topic><topic>CYAMOPSIS PSORALIOIDES</topic><topic>DNA</topic><topic>DNA - genetics</topic><topic>Enzyme Precursors - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GALACTOSIDASA</topic><topic>GALACTOSIDASE</topic><topic>GALACTOSIDASES</topic><topic>Galactosidases - genetics</topic><topic>genes</topic><topic>Genes. Genome</topic><topic>GENETIC CODE</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>Humans</topic><topic>Methods. Procedures. Technologies</topic><topic>Molecular and cellular biology</topic><topic>Molecular cloning</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Plants - enzymology</topic><topic>Plants - genetics</topic><topic>Poly A - genetics</topic><topic>Restriction Mapping</topic><topic>RNA, Messenger - genetics</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Species Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Overbeeke, N. (Unilever Research Lab., Vlaardingen (Netherlands))</creatorcontrib><creatorcontrib>Fellinger, A.J</creatorcontrib><creatorcontrib>Toonen, M.Y</creatorcontrib><creatorcontrib>Wassenaar, D. van</creatorcontrib><creatorcontrib>Verrips, C.T</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Plant molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Overbeeke, N. (Unilever Research Lab., Vlaardingen (Netherlands))</au><au>Fellinger, A.J</au><au>Toonen, M.Y</au><au>Wassenaar, D. van</au><au>Verrips, C.T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and nucleotide sequence of the alpha-galactosidase cDNA from Cyamopsis tetragonoloba (guar)</atitle><jtitle>Plant molecular biology</jtitle><addtitle>Plant Mol Biol</addtitle><date>1989-11-01</date><risdate>1989</risdate><volume>13</volume><issue>5</issue><spage>541</spage><epage>550</epage><pages>541-550</pages><issn>0167-4412</issn><eissn>1573-5028</eissn><coden>PMBIDB</coden><abstract>Polyadenylated mRNA was purified from the aleurone cells of Cyamopsis tetragonoloba (guar) seeds germinated for 18 h and used for the construction of a cDNA library. Clones with the alpha-galactosidase encoding gene were identified using oligo-nucleotide mixed probes based on the NH2 terminal amino acid sequence and on the sequence of an internal peptide. The nucleotide sequence of the cDNA clone showed that the enzyme is synthesized as a precursor with a 47 amino acid NH2 terminal extension. This pre-sequence most likely functions to target the protein outside the aleurone cells into the endosperm. Based upon structural features, it is proposed to divide the precursor into a pre-(signal sequence) part and a glycosylated pro-part comparable with those of the yeast mat A/alpha factor and killer factor. A comparison of the derived amino acid sequence of this alpha-galactosidase from plant origin revealed significant stretches of homology with respect to the amino acid sequences of the enzymes from Saccharomyces cerevisiae and from human origin but only to a minor extent compared with the alpha-galactosidase from Escherichia coli.</abstract><cop>Dordrecht</cop><pub>Springer</pub><pmid>2577496</pmid><doi>10.1007/BF00027314</doi><tpages>10</tpages></addata></record> |
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subjects | ADN alpha -galactosidase Amino Acid Sequence Base Sequence Biological and medical sciences Biotechnology CLONACION CLONAGE CLONING Cloning, Molecular CODE GENETIQUE CODIGO GENETICO CYAMOPSIS PSORALIOIDES DNA DNA - genetics Enzyme Precursors - genetics Fundamental and applied biological sciences. Psychology GALACTOSIDASA GALACTOSIDASE GALACTOSIDASES Galactosidases - genetics genes Genes. Genome GENETIC CODE Genetic engineering Genetic technics Humans Methods. Procedures. Technologies Molecular and cellular biology Molecular cloning Molecular genetics Molecular Sequence Data Plants - enzymology Plants - genetics Poly A - genetics Restriction Mapping RNA, Messenger - genetics Sequence Homology, Nucleic Acid Species Specificity |
title | Cloning and nucleotide sequence of the alpha-galactosidase cDNA from Cyamopsis tetragonoloba (guar) |
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