Synthesis and processing of the plant protein thaumatin in yeast

Edens, Luppo; Bom, I.J.; Ledeboer, A.M.; Maat, Jaap; Toonen, Marjolein Y.; Visser, Chris J.; Verrips, C. Theo

doi:10.1016/0092-8674(84)90394-5

Cited by 90 publications

(27 citation statements)

References 23 publications

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“…in yeast (13,14). For example, when human pre-IFNs were expressed in yeast, a large fraction of the IFN-a-1 and IFNa-2 polypeptides had the same amino termini as that of the mature IFN in human cells, suggesting that yeast was able to remove the same signal sequence processed by human cells (13).…”

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“…For example, when human pre-IFNs were expressed in yeast, a large fraction of the IFN-a-1 and IFNa-2 polypeptides had the same amino termini as that of the mature IFN in human cells, suggesting that yeast was able to remove the same signal sequence processed by human cells (13). Moreover, a plant protein, thaumatin, has recently been expressed in yeast and the signal sequence of preprothaumatin is cleaved at the site used in plant cells (14). However, none of these proteins is an integral membrane protein requiring anchorage to the plasma membrane.…”

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confidence: 99%

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Influenza viral (A/WSN/33) hemagglutinin is expressed and glycosylated in the yeast Saccharomyces cerevisiae.

Jabbar¹,

Sivasubramanian²,

Nayak³

1985

Proc. Natl. Acad. Sci. U.S.A.

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Recombinant plasmids were constructed in which genes coding for either the entire or the signal-minus (amino acid residues 2-17 deleted) hemagglutinin (HA) of WSN influenza virus were placed under the control of the alcohol dehydrogenase I gene promoter of Saccharomyces cerevisiae. Both recombinant plasmids were shown to direct the synthesis of HA-specific polypeptides that were detected by immunoprecipitation with antiviral antibodies. The complete HA produced in yeast had an approximate Mr of 70,000 and was glycosylated, as determined by the endoglycosidase H sensitiv-

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confidence: 99%

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confidence: 99%

Influenza viral (A/WSN/33) hemagglutinin is expressed and glycosylated in the yeast Saccharomyces cerevisiae.

Jabbar¹,

Sivasubramanian²,

Nayak³

1985

Proc. Natl. Acad. Sci. U.S.A.

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“…In an attempt to exploit the yeast sec mutants for studies of animal virus glycoproteins, we took advantage of the recently developed ability to efficiently express foreign genes in yeast (10)(11)(12)(13)(14). Plasmids with virus genes fused to the yeast galactokinase (GALl) promoter (15) (16).…”

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confidence: 99%

Regulated expression of Sindbis and vesicular stomatitis virus glycoproteins in Saccharomyces cerevisiae.

Wen¹,

Schlesinger²

1986

Proc. Natl. Acad. Sci. U.S.A.

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ABSTRACTcDNAs encoding either the structural proteins (capsid and glycoproteins El and E2) of Sindbis virus or the glycoprotein of vesicular stomatitis virus (VSV) were fused to the Saccharomyces cerevisiae galactokinase gene (GALI) promoter and inserted into a yeast shuttle vector. After addition pf galactose to yeast transformed with this vector, 2.5-3% of total yeast protein synthesis was detected as virus proteins by specific anti-virus protein antibodies. In cells containing the Sindbis virus structural genes, the virus capsid protein was effectively released from the nascent polypeptide and two endoglycosidase H-sensitive glycoproteins were produced. One of these was identical in its gel mobility to El and the other appeared to be p62, a precursor to E2. A low level of El protein was detected on the cell's surface membranes. A single molecular weight species of glycosylated VSV glycoprotein was produced and halfofthe total protein could be detected at the surface membranes of yeast. Addition of long mannose chains and acylation of the virus proteins with fatty acids were not observed. Formation of virus proteins was also examined in yeast secretory mutants; one of these (sec53) failed to glycosylate the virus proteins.

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“…S. cerevisiae also apparently recognizes and processes the thaumatin signal sequence. 32 ) The thaumatin signal sequence in A. oryzae is presumably cleaved after the Ala-22 residue; absolute proof will require purification of the secreted protein and amino terminal sequencing. The processing of the signal sequence is not apparently efficient, as evidenced by the accumulation inside of the cell of the unprocessed form of the protein.…”

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confidence: 99%