Cloning of cDNA encoding the sweet-tasting plant protein thaumatin and its expression in Escherichia coli.
Gene
; 18(1): 1-12, 1982 Apr.
Article
en En
| MEDLINE
| ID: mdl-7049841
ABSTRACT
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.
Buscar en Google
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas de Plantas
/
Edulcorantes
Idioma:
En
Revista:
Gene
Año:
1982
Tipo del documento:
Article