Cloning of cDNA encoding the sweet-tasting plant protein thaumatin and its expression in Eschericha coli

Tipo de material: Texto

TextoSeries ; Gene, 18, p.1-12, 1982Trabajos contenidos:

Edens, L
Heslinga, L
Klok, R
Ledeboer, A.M
Maat, J
Toonen, M.Y
Visser, C
Visser, C

Recursos en línea:

Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx

Resumen: The structural gene of the sweet-tasting plant protein (prepro)thaumatin was cloned and expressed in Escherichia coli. Expression was effected under control of fuc 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.

Tags from this library: No tags from this library for this title. Log in to add tags.

Average rating: 0.0 (0 votes)

Holdings
Item type	Current library	Collection	Call number	Status	Date due	Barcode
Documentos solicitados	CICY Documento préstamo interbibliotecario	Ref1	B-14744 (Browse shelf(Opens below))	Available

Browsing CICY shelves, Shelving location: Documento préstamo interbibliotecario, Collection: Ref1 Close shelf browser (Hides shelf browser)

Previous	No cover image available	No cover image available	No cover image available	No cover image available	No cover image available	No cover image available	No cover image available	Next
Previous	B-14741 Molecular Cloning and Characterization of a Novel Jasmonate Inducible Pathogenesis-Related Class 10 Protein Gene,JIOsPR10,from Rice (Oryza sativaL.)Seedling Leaves	B-14742 Global microRNA elevation by inducible Exportin 5 regulates cell cycle entry	B-14743 Transgenerational epigenetic inheritance: how important is it?	B-14744 Cloning of cDNA encoding the sweet-tasting plant protein thaumatin and its expression in Eschericha coli	B-14745 Senescing Cells Share Common Features with Dedifferentiating Cells	B-14746 Lactobacillus sp. as a potential probiotic for the prevention of Paenibacillus larvaeinfection in honey bees	B-14747 Essential oils from brazilian Verbenaceae. genus Lippia	Next

The structural gene of the sweet-tasting plant protein (prepro)thaumatin was cloned and expressed in Escherichia coli. Expression was effected under control of fuc 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.

There are no comments on this title.

to post a comment.