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Cloning of cDNA encoding the sweet-tasting plant protein thaumatin and its expression in Escherichia coli.
The structural gene of the sweet-tasting plant protein (prepro)thaumatin was cloned and expressed in Escherichia coli. Expression was effected under control of lac and trp promoter/operator systems and through the use of bacterial ribosome-binding sites. The naturally occurring thaumatin II represents a processed form. The primary translation product, preprothaumatin, of the cloned mRNA-derived cDNA contains extensions at both the amino terminus and the carboxy terminus. The amino terminal extension of 22 amino acids is hydrophobic and very much resembles an excretion-related signal sequence. The six amino acids-long carboxy terminal extension is very acidic in character, in contrast to the overall highly basic thaumatin molecule. The possible role of such an acidic tail with respect to compartmentalization is discussed.
PMID: 7049841 [PubMed - indexed for MEDLINE]
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Cited by 22 PubMed Central articles
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Expression of Osmotin-Like Genes in the Halophyte Atriplex nummularia L.
Casas AM, Nelson DE, Raghothama KG, D'Urzo MP, Singh NK, Bressan RA, Hasegawa PM.
Plant Physiol. 1992 May; 99(1):329-337.
[Plant Physiol. 1992]
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Complete Amino Acid Sequence of Soybean Leaf P21 : Similarity to the Thaumatin-Like Polypeptides.
Graham JS, Burkhart W, Xiong J, Gillikin JW.
Plant Physiol. 1992 Jan; 98(1):163-165.
[Plant Physiol. 1992]
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Nucleotide Sequence of a cDNA for Osmotin-Like Protein from Cultured Tobacco Cells.
Takeda S, Sato F, Ida K, Yamada Y.
Plant Physiol. 1991 Oct; 97(2):844-846.
[Plant Physiol. 1991]
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