1987
DOI: 10.1128/mcb.7.1.121
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Signal peptide specificity in posttranslational processing of the plant protein phaseolin in Saccharomyces cerevisiae.

Abstract: We linked the cDNA coding region for the bean storage protein phaseolin to the promoter and regulatory region of the Saccharomyces cerevisiae repressible acid phosphatase gene (PH05) in multicopy expression plasmids. Yeast transformants containing these plasmids expressed phaseolin at levels up to 3% of the total soluble cellular protein. Phaseolin polypeptides in S. cerevisiae were glycosylated, and their molecular weights suggested that the signal peptide had been processed. We also constructed a series of p… Show more

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Cited by 19 publications
(11 citation statements)
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“…This mechanism has been proposed for the dual localization of the PDI, RB60 (which contains a signal peptide and C-terminal KDEL), to the ER and chloroplast in Chlamydomonas (Levitan et al, 2005). Post-translational insertion of the signal peptide-containing polypeptide was observed in a few cases in animals, yeast and plants (Cramer et al, 1987;Plath et al, 1998;Rapoport et al, 1999). Alternatively, PDI2 could enter the nucleus by interacting with MEE8, which has a strong NLS ( Table 2) that can mask the signal peptide (Karniely and Pines, 2005).…”
Section: Discussionmentioning
confidence: 91%
“…This mechanism has been proposed for the dual localization of the PDI, RB60 (which contains a signal peptide and C-terminal KDEL), to the ER and chloroplast in Chlamydomonas (Levitan et al, 2005). Post-translational insertion of the signal peptide-containing polypeptide was observed in a few cases in animals, yeast and plants (Cramer et al, 1987;Plath et al, 1998;Rapoport et al, 1999). Alternatively, PDI2 could enter the nucleus by interacting with MEE8, which has a strong NLS ( Table 2) that can mask the signal peptide (Karniely and Pines, 2005).…”
Section: Discussionmentioning
confidence: 91%
“…Another plant vacuolar storage protein, phaseolin from P, vulgaris, has been expressed in yeast (Cramer et al, 1985(Cramer et al, , 1987. It is glycosylated and remains intracellular.…”
Section: Discussionmentioning
confidence: 99%
“…It has been shown that fava bean lectin, barley hordein, sweet potato sporamin A, tomato polygalacturonase, and wheat high molecular weight glutenin all contain an amino-terminal presequence that can be processed in vitro using canine microsomal membranes (Hemperly et al, 1982;Weber and Brandt, 1985;Hattori et al, 1987;Bulleid and Freedman, 1988;DellaPenna and Bennett, 1988). Furthermore, plant proteins known to be localized in storage bodies or secreted can translocate the ER and trave1 through the secretory pathway of yeast, animal cells, and heterologous plants (Bassüner et al, 1983;Rothstein et al, 1984;Beachy et al, 1985;Greenwood and Chrispeels, 1985;Voelker et al, 1986;Cramer et al, 1987;Hoffman et al, 1987;Neill et al, 1987;Tague and Chrispeels, 1987;Bustos et al, 1988;Sturm et al, 1988;Wallace et al, 1988).…”
Section: Introductionmentioning
confidence: 99%
“…It has been shown that fava bean lectin, barley hordein, sweet potato sporamin A, tomato polygalacturonase, and wheat high molecular weight glutenin all contain an amino-terminal presequence that can be processed in vitro using canine microsomal membranes (Hemperly et al, 1982; Weber and Brandt, 1985;Hattori et al, 1987;Bulleid and Freedman, 1988;DellaPenna and Bennett, 1988). Furthermore, plant proteins known to be localized in storage bodies or secreted can translocate the ER and trave1 through the secretory pathway of yeast, animal cells, and heterologous plants (Bassüner et al, 1983;Rothstein et al, 1984;Beachy et al, 1985; Greenwood and Chrispeels, 1985;Voelker et al, 1986;Cramer et al, 1987; Hoffman et al, 1987;Neill et al, 1987;Tague and Chrispeels, 1987; Bustos et al, 1988; Sturm et al, 1988; Wallace et al, 1988).A useful way of, studying the function of these signal sequences, and defining their important domains, is to construct hybrid proteins containing the putative signal peptide and a protein that is normally located in a different compartment and to study their translocation in vitro using microsomes (Blobel and Dobberstein, 1975) and in vivo by introducing genes encoding the hybrid proteins into plants using transformation. In the latter case, studies have been conducted using the transit peptides of the small subunit of ribulose-l,5-bisphophate carboxylase/oxygenase fused to neomycin phosphotransferase (Schreier et al, 1985;Van den Broeck et al, 1985), chlorophyll a/b binding protein fused to P-glucuronidase (GUS) (Kavanagh et al, 1988) and the p subunit of ATPase fused to chloramphenicol acetyltransferase (CAT) (Boutry et al, 1987).…”
mentioning
confidence: 99%