The plant vacuolar protein, phytohemagglutinin, is transported to the vacuole of transgenic yeast.

Tague, Brian W.; Chrispeels, Maarten J.

doi:10.1083/jcb.105.5.1971

Cited by 65 publications

(39 citation statements)

References 59 publications

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“…Even though phytohemagglutinin (PHA) was one of the first plant vacuolar proteins analysed in this respect it is still unclear where its sorting determinants reside. The sorting determinants for PHA were first studied by fusion of truncated PHA with invertase and expression in yeast [110,111], but it was recognized later that yeast and plants probably utilize different sorting determinants. The determinants were tentatively localized within a surface loop [118], but, because the results were obtained by fusion of truncated PHA with invertase, concerns about possible misfolding of the chimeric reporter protein would need to be addressed.…”

Section: The Physical Structure (Ps-vsd) Vacuolar Sorting Determinantsmentioning

confidence: 99%

Sorting of proteins to vacuoles in plant cells

Neuhaus

Rogers

1998

Protein Trafficking in Plant Cells

132

149

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An individual plant cell may contain at least two functionally and structurally distinct types of vacuoles: protein storage vacuoles and lytic vacuoles. Presumably a cell that stores proteins in vacuoles must maintain these separate compartments to prevent exposure of the storage proteins to an acidified environment with active hydrolytic enzymes where they would be degraded. Thus, the organization of the secretory pathway in plant cells, which includes the vacuoles, has a fascinating complexity not anticipated from the extensive genetic and biochemical studies of the secretory pathway in yeast. Plant cells must generate the membranes to form two separate types of tonoplast, maintain them as separate organelles, and direct soluble proteins from the secretory flow specifically to one or the other via separate vesicular pathways. Individual soluble and membrane proteins must be recognized and sorted into one or the other pathway by distinct, specific mechanisms. Here we review the emerging picture of how separate plant vacuoles are organized structurally and how proteins are recognized and sorted to each type.

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Section: The Physical Structure (Ps-vsd) Vacuolar Sorting Determinantsmentioning

confidence: 99%

Sorting of proteins to vacuoles in plant cells

Neuhaus

Rogers

1998

Protein Trafficking in Plant Cells

132

149

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“…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).…”

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confidence: 99%

Endoplasmic reticulum targeting and glycosylation of hybrid proteins in transgenic tobacco.

Iturriaga¹,

Jefferson²,

Bevan³

1989

Plant Cell

106

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The correct compartmentation of proteins to the endomembrane system, mitochondria, or chloroplasts requires an amino-terminal signal peptide. The major tuber protein of potato, patatin, has a signal peptide in common with many other plant storage proteins. When the putative signal peptide of patatin was fused to the bacterial reporter protein @-glucuronidase, the fusion proteins were translocated to the endoplasmic reticulum in planta and in vitro. In addition, translocated j3-glucuronidase was modified by glycosylation, and the signal peptide was correctly processed. In the presence of an inhibitor of glycosylation, tunicamycin, the enzymatically active form of 8-glucuronidase was assembled in the endoplasmic reticulum. This is the first report of targeting a cytoplasmic protein to the endoplasmic reticulum of plants using a signal peptide. INTRODUCTIONThe compartmentation of eukaryotic cells by the endomembrane system and organelle membranes requires the correct delivery of newly synthesized proteins to their site of function. The signal directing a protein to a target membrane is generally found at the amino terminus (the signal peptide or transit peptide) and in most cases is removed by cleavage with a specific signal peptidase on the frans side of the target membrane (reviewed by Verner and Schatz, 1988). In higher plants, targeting of the nuclear-encoded ribulose-l,5-bisphosphate carboxylase/oxygenase small subunit and chlorophyll a/b binding proteins to the chloroplast requires an amino-terminal transit peptide that is proteolytically cleaved during import (Dobberstein et al., 1977; Schmidt et al., 1981). Similarly, import of the p subunit of ATPase to the mitochondrion requires an amino-terminal transit peptide (Boutry et al., 1987). Transport of proteins into the eukaryotic secretory pathway follows the vectorial route: ER (endoplasmic reticulum) + Golgi + vacuole/lysosomes/plasma membrane (Walter and Lingappa, 1986). The coupling of protein elongation to protein translocation into the ER varies between proteins. For example, yeast prepro-a-factor is translocated posttranslationally into the ER, whereas yeast pre-invertase requires translocation to be initiated at an early stage of protein elongation (Hansen and Walter, 1987).Signal peptides targeting proteins to the ER are characterized by a positively charged N-terminal region, a central hydrophobic region, and a more polar C-terminal region that is thought to define the cleavage site (von Heijne, 1985). The abundant storage proteins of higher plants are sequestered within protein bodies, which are derived from the vacuole (Yoo and Chrispeels, 1980). TheTo whom correspondence should be addressed. correct translocation to the ER of the storage proteins as well as other plant proteins, requires an amino-terminal transit peptide that is cotranslationally removed (Chrispeels, 1984). 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-termi...

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“…This could alter the accessibility of the targeting signals. Altered glycosylation, observed in yeast (Hasnain et aL, 1992;Tague and Chrispeels, 1987), could also affect recognition of the targeting signal, as was seen in plants with mutated BL proteins (Dombrowski et aL, 1993). Preliminary evidence suggests that BL expressed in yeast is not in the correct conformation as the protein does not bind to an N-acetylglucosamine column (data not shown).…”

Section: Barley Lectin In Yeast 237mentioning

confidence: 90%

“…In plants, three types of signals have been identified: those within an amino-terminal propeptide (Holwerda et aL, 1992;Matsuoka and Nakamura, 1991), those within a carboxyl-terminal propeptide (CTPP) (Bednarek et aL, 1990;Melchers et aL, 1993;Neuhaus et aL, 1991), and those internal to the protein which are not cleaved (Saalbach et aL, 1991;Tague and Chrispeels, 1987). In the first two cases, the targeting domain has been shown to reside within the propeptide because synthesis of the protein without the propeptide causes secretion.…”

Section: Introductionmentioning

confidence: 99%