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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
Main Authors: Yeh, K W, Chen, J C, Lin, M I, Chen, Y M, Lin, C Y
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Chen, Y M
Lin, C Y
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.
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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. 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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.</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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identifier ISSN: 0167-4412
ispartof Plant molecular biology, 1997-02, Vol.33 (3), p.565-570
issn 0167-4412
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source Springer Nature
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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