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Functional activity of sporamin from sweet potato (Ipomoea batatas Lam.): a tuber storage protein with trypsin inhibitory activity
Sporamin accounts for about 60% to 80% of total soluble protein in sweet potato tubers, and the predicted protein sequence of sporamin shares significant amino acid sequence identity with some Kunitz-type trypsin inhibitors. We constructed three recombinant plasmids with cDNAs that encode preprospor...
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Published in: | Plant molecular biology 1997-02, Vol.33 (3), p.565-570 |
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description | Sporamin accounts for about 60% to 80% of total soluble protein in sweet potato tubers, and the predicted protein sequence of sporamin shares significant amino acid sequence identity with some Kunitz-type trypsin inhibitors. We constructed three recombinant plasmids with cDNAs that encode preprosporamin, prosporamin, and sporamin, and these three were expressed in Escherichia coli cells as fusion proteins. All three forms of sporamin expressed in E. coli were shown to have strong inhibitory activity to trypsin in vitro, suggesting that post-translational modifications are not essential for trypsin inhibitory activity. Northern blot analysis showed that sporamin transcripts could be systemically induced in leaf tissue of sweet potato by wounding. Therefore, sporamin may have a defense role as a protease inhibitor, in addition to its role as a storage protein. |
doi_str_mv | 10.1023/A:1005764702510 |
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We constructed three recombinant plasmids with cDNAs that encode preprosporamin, prosporamin, and sporamin, and these three were expressed in Escherichia coli cells as fusion proteins. All three forms of sporamin expressed in E. coli were shown to have strong inhibitory activity to trypsin in vitro, suggesting that post-translational modifications are not essential for trypsin inhibitory activity. Northern blot analysis showed that sporamin transcripts could be systemically induced in leaf tissue of sweet potato by wounding. Therefore, sporamin may have a defense role as a protease inhibitor, in addition to its role as a storage protein.</description><identifier>ISSN: 0167-4412</identifier><identifier>EISSN: 1573-5028</identifier><identifier>DOI: 10.1023/A:1005764702510</identifier><identifier>PMID: 9049277</identifier><language>eng</language><publisher>Netherlands: Springer Nature B.V</publisher><subject>ADN ; Amino Acid Sequence ; Amino acids ; Bacteria ; DNA ; E coli ; Escherichia coli ; Gene Expression Regulation, Plant ; Genes, Plant ; Genetic Vectors ; HERIDAS ; INHIBIDORES DE TRIPSINA ; INHIBITEUR DE TRYPSINE ; IPOMOEA BATATAS ; Molecular Sequence Data ; NUCLEOTIDE SEQUENCE ; PLAIE ; Plant Leaves - genetics ; Plant Proteins - chemistry ; Plant Proteins - genetics ; Plant Proteins - physiology ; PLANT RESPONSE ; Plant Stems - chemistry ; Plant Stems - enzymology ; Plant tissues ; Potatoes ; PROTEINAS DE RESERVA ; Proteinase inhibitors ; PROTEINE DE RESERVE ; Proteins ; Recombinant Fusion Proteins - biosynthesis ; Recombinant Fusion Proteins - isolation & purification ; REPONSE DE LA PLANTE ; RESPUESTA DE LA PLANTA ; SECUENCIA NUCLEOTIDICA ; SEQUENCE NUCLEOTIDIQUE ; STORAGE PROTEINS ; Trypsin Inhibitor, Kunitz Soybean - chemistry ; TRYPSIN INHIBITORS ; Trypsin Inhibitors - chemistry ; Trypsin Inhibitors - metabolism ; TUBERCULE ; TUBERCULO ; TUBERS ; Vegetables - chemistry ; Vegetables - enzymology ; WOUNDS</subject><ispartof>Plant molecular biology, 1997-02, Vol.33 (3), p.565-570</ispartof><rights>Kluwer Academic Publishers 1997</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c332t-aa23498797f6d4fce4778c40ff1ed3a0e1cabd3f94f8799c4e04bd6b67db88953</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9049277$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yeh, K W</creatorcontrib><creatorcontrib>Chen, J C</creatorcontrib><creatorcontrib>Lin, M I</creatorcontrib><creatorcontrib>Chen, Y M</creatorcontrib><creatorcontrib>Lin, C Y</creatorcontrib><title>Functional activity of sporamin from sweet potato (Ipomoea batatas Lam.): a tuber storage protein with trypsin inhibitory activity</title><title>Plant molecular biology</title><addtitle>Plant Mol Biol</addtitle><description>Sporamin accounts for about 60% to 80% of total soluble protein in sweet potato tubers, and the predicted protein sequence of sporamin shares significant amino acid sequence identity with some Kunitz-type trypsin inhibitors. We constructed three recombinant plasmids with cDNAs that encode preprosporamin, prosporamin, and sporamin, and these three were expressed in Escherichia coli cells as fusion proteins. All three forms of sporamin expressed in E. coli were shown to have strong inhibitory activity to trypsin in vitro, suggesting that post-translational modifications are not essential for trypsin inhibitory activity. Northern blot analysis showed that sporamin transcripts could be systemically induced in leaf tissue of sweet potato by wounding. Therefore, sporamin may have a defense role as a protease inhibitor, in addition to its role as a storage protein.</description><subject>ADN</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Bacteria</subject><subject>DNA</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Gene Expression Regulation, Plant</subject><subject>Genes, Plant</subject><subject>Genetic Vectors</subject><subject>HERIDAS</subject><subject>INHIBIDORES DE TRIPSINA</subject><subject>INHIBITEUR DE TRYPSINE</subject><subject>IPOMOEA BATATAS</subject><subject>Molecular Sequence Data</subject><subject>NUCLEOTIDE SEQUENCE</subject><subject>PLAIE</subject><subject>Plant Leaves - genetics</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - physiology</subject><subject>PLANT RESPONSE</subject><subject>Plant Stems - chemistry</subject><subject>Plant Stems - enzymology</subject><subject>Plant tissues</subject><subject>Potatoes</subject><subject>PROTEINAS DE RESERVA</subject><subject>Proteinase inhibitors</subject><subject>PROTEINE DE RESERVE</subject><subject>Proteins</subject><subject>Recombinant Fusion Proteins - biosynthesis</subject><subject>Recombinant Fusion Proteins - isolation & purification</subject><subject>REPONSE DE LA PLANTE</subject><subject>RESPUESTA DE LA PLANTA</subject><subject>SECUENCIA NUCLEOTIDICA</subject><subject>SEQUENCE NUCLEOTIDIQUE</subject><subject>STORAGE PROTEINS</subject><subject>Trypsin Inhibitor, Kunitz Soybean - chemistry</subject><subject>TRYPSIN INHIBITORS</subject><subject>Trypsin Inhibitors - chemistry</subject><subject>Trypsin Inhibitors - metabolism</subject><subject>TUBERCULE</subject><subject>TUBERCULO</subject><subject>TUBERS</subject><subject>Vegetables - chemistry</subject><subject>Vegetables - enzymology</subject><subject>WOUNDS</subject><issn>0167-4412</issn><issn>1573-5028</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><recordid>eNqFkb9P5TAMx6MTCB7czUxIEQOCoeA0aZOwIXT8kJ64hZsrt00g6LUpSQp66_3lF4knkFjwYlv--GvLJuSAwRmDkp9fXjCAStZCQlkx-EEWrJK8qKBUW2QBrJaFEKzcJXsxPgNkmNc7ZEeD0KWUC_Lveh675PyIK4o5eHVpTb2lcfIBBzdSG_xA45sxiU4-YfL05G7ygzdIW8w5RrrE4ez0giJNc2sCjSm3Pho6BZ9MVnhz6YmmsJ5iTtz45FqXifXHuJ9k2-Iqml8bv0_-Xv9-uLotln9u7q4ul0XHeZkKxJILraSWtu6F7YyQUnUCrGWm5wiGddj23GphM6Q7YUC0fd3Wsm-V0hXfJ8fvunmxl9nE1Awudma1wtH4OTZSqUpL0N-CrNKKSWAZPPoCPvs55FNmMclEpXktM3S4geZ2MH0zBTdgWDebF3zWLfoGH4OLzf2Saa0gm1D8P1ncks8</recordid><startdate>199702</startdate><enddate>199702</enddate><creator>Yeh, K W</creator><creator>Chen, J C</creator><creator>Lin, M I</creator><creator>Chen, Y M</creator><creator>Lin, C Y</creator><general>Springer Nature B.V</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>199702</creationdate><title>Functional activity of sporamin from sweet potato (Ipomoea batatas Lam.): a tuber storage protein with trypsin inhibitory activity</title><author>Yeh, K W ; Chen, J C ; Lin, M I ; Chen, Y M ; Lin, C Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c332t-aa23498797f6d4fce4778c40ff1ed3a0e1cabd3f94f8799c4e04bd6b67db88953</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>ADN</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Bacteria</topic><topic>DNA</topic><topic>E coli</topic><topic>Escherichia coli</topic><topic>Gene Expression Regulation, Plant</topic><topic>Genes, Plant</topic><topic>Genetic Vectors</topic><topic>HERIDAS</topic><topic>INHIBIDORES DE TRIPSINA</topic><topic>INHIBITEUR DE TRYPSINE</topic><topic>IPOMOEA BATATAS</topic><topic>Molecular Sequence Data</topic><topic>NUCLEOTIDE SEQUENCE</topic><topic>PLAIE</topic><topic>Plant Leaves - genetics</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - physiology</topic><topic>PLANT RESPONSE</topic><topic>Plant Stems - chemistry</topic><topic>Plant Stems - enzymology</topic><topic>Plant tissues</topic><topic>Potatoes</topic><topic>PROTEINAS DE RESERVA</topic><topic>Proteinase inhibitors</topic><topic>PROTEINE DE RESERVE</topic><topic>Proteins</topic><topic>Recombinant Fusion Proteins - biosynthesis</topic><topic>Recombinant Fusion Proteins - isolation & purification</topic><topic>REPONSE DE LA PLANTE</topic><topic>RESPUESTA DE LA PLANTA</topic><topic>SECUENCIA NUCLEOTIDICA</topic><topic>SEQUENCE NUCLEOTIDIQUE</topic><topic>STORAGE PROTEINS</topic><topic>Trypsin Inhibitor, Kunitz Soybean - chemistry</topic><topic>TRYPSIN INHIBITORS</topic><topic>Trypsin Inhibitors - chemistry</topic><topic>Trypsin Inhibitors - metabolism</topic><topic>TUBERCULE</topic><topic>TUBERCULO</topic><topic>TUBERS</topic><topic>Vegetables - chemistry</topic><topic>Vegetables - enzymology</topic><topic>WOUNDS</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yeh, K W</creatorcontrib><creatorcontrib>Chen, J C</creatorcontrib><creatorcontrib>Lin, M I</creatorcontrib><creatorcontrib>Chen, Y M</creatorcontrib><creatorcontrib>Lin, C Y</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>ProQuest Central (Corporate)</collection><collection>Nucleic Acids Abstracts</collection><collection>ProQuest Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest research library</collection><collection>ProQuest Biological Science Journals</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</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>Yeh, K W</au><au>Chen, J C</au><au>Lin, M I</au><au>Chen, Y M</au><au>Lin, C Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional activity of sporamin from sweet potato (Ipomoea batatas Lam.): a tuber storage protein with trypsin inhibitory activity</atitle><jtitle>Plant molecular biology</jtitle><addtitle>Plant Mol Biol</addtitle><date>1997-02</date><risdate>1997</risdate><volume>33</volume><issue>3</issue><spage>565</spage><epage>570</epage><pages>565-570</pages><issn>0167-4412</issn><eissn>1573-5028</eissn><abstract>Sporamin accounts for about 60% to 80% of total soluble protein in sweet potato tubers, and the predicted protein sequence of sporamin shares significant amino acid sequence identity with some Kunitz-type trypsin inhibitors. We constructed three recombinant plasmids with cDNAs that encode preprosporamin, prosporamin, and sporamin, and these three were expressed in Escherichia coli cells as fusion proteins. All three forms of sporamin expressed in E. coli were shown to have strong inhibitory activity to trypsin in vitro, suggesting that post-translational modifications are not essential for trypsin inhibitory activity. Northern blot analysis showed that sporamin transcripts could be systemically induced in leaf tissue of sweet potato by wounding. Therefore, sporamin may have a defense role as a protease inhibitor, in addition to its role as a storage protein.</abstract><cop>Netherlands</cop><pub>Springer Nature B.V</pub><pmid>9049277</pmid><doi>10.1023/A:1005764702510</doi><tpages>6</tpages></addata></record> |
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subjects | ADN Amino Acid Sequence Amino acids Bacteria DNA E coli Escherichia coli Gene Expression Regulation, Plant Genes, Plant Genetic Vectors HERIDAS INHIBIDORES DE TRIPSINA INHIBITEUR DE TRYPSINE IPOMOEA BATATAS Molecular Sequence Data NUCLEOTIDE SEQUENCE PLAIE Plant Leaves - genetics Plant Proteins - chemistry Plant Proteins - genetics Plant Proteins - physiology PLANT RESPONSE Plant Stems - chemistry Plant Stems - enzymology Plant tissues Potatoes PROTEINAS DE RESERVA Proteinase inhibitors PROTEINE DE RESERVE Proteins Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - isolation & purification REPONSE DE LA PLANTE RESPUESTA DE LA PLANTA SECUENCIA NUCLEOTIDICA SEQUENCE NUCLEOTIDIQUE STORAGE PROTEINS Trypsin Inhibitor, Kunitz Soybean - chemistry TRYPSIN INHIBITORS Trypsin Inhibitors - chemistry Trypsin Inhibitors - metabolism TUBERCULE TUBERCULO TUBERS Vegetables - chemistry Vegetables - enzymology WOUNDS |
title | Functional activity of sporamin from sweet potato (Ipomoea batatas Lam.): a tuber storage protein with trypsin inhibitory activity |
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