cDNA Sequence for the Plastidic Phosphoglucomutase from Spinacia oleracea (L.)

Penger, Anja; Pelzer-Reith, Birgit; Schnarrenberger, Claus

doi:10.1104/pp.105.4.1439

Cited by 8 publications

(5 citation statements)

References 5 publications

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“…These experiments revealed that St pPGM was imported into the plastid and that the transit peptide was cleaved resulting in the formation of a 62 kDa mature peptide. The sequence homology of St pPGM cDNA in comparison to that from Spinacea oleracea is only 19%, which is surprisingly low ( Penger et al . 1994 ).…”

Section: Discussionmentioning

confidence: 99%

Antisense inhibition of plastidial phosphoglucomutase provides compelling evidence that potato tuber amyloplasts import carbon from the cytosol in the form of glucose‐6‐phosphate

Tauberger¹,

Fernie²,

Emmermann³

et al. 2000

The Plant Journal

138

136

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SummaryThe aim of this work was to establish whether plastidial phosphoglucomutase is involved in the starch biosynthetic pathway of potato tubers and thereby to determine the form in which carbon is imported into the potato amyloplast. For this purpose, we cloned the plastidial isoform of potato PGM (StpPGM), and using an antisense approach generated transgenic potato plants that exhibited decreased expression of the StpPGM gene and contained signi®cantly reduced total phosphoglucomutase activity. We con®rmed that this loss in activity was due speci®cally to a reduction in plastidial PGM activity. Potato lines with decreased activities of plastidial PGM exhibited no major changes in either whole-plant or tuber morphology. However, tubers from these lines exhibited a dramatic (up to 40%) decrease in the accumulation of starch, and signi®cant increases in the levels of sucrose and hexose phosphates. As tubers from these lines exhibited no changes in the maximal catalytic activities of other key enzymes of carbohydrate metabolism, we conclude that plastidial PGM forms part of the starch biosynthetic pathway of the potato tuber, and that glucose-6-phosphate is the major precursor taken up by amyloplasts in order to support starch synthesis.

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Section: Discussionmentioning

confidence: 99%

Antisense inhibition of plastidial phosphoglucomutase provides compelling evidence that potato tuber amyloplasts import carbon from the cytosol in the form of glucose‐6‐phosphate

Tauberger¹,

Fernie²,

Emmermann³

et al. 2000

The Plant Journal

138

136

View full text Add to dashboard Cite

show abstract

“…This is perhaps consistent with the hypothesis that plastids are derived from ancient prokaryote symbionts. A spinach PGM sequence reported by Penger et al (1994) does not show a high degree of homology to any of the identified plant PGMs. With the sequence data now available from numerous plant species, it seems highly unlikely that this clone was a PGM.…”

Section: Discussionmentioning

confidence: 99%

The rug3 Locus of Pea Encodes Plastidial Phosphoglucomutase

et al. 2000

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Two cDNA clones were isolated from pea (Pisum sativum L.) and their deduced amino acid sequences shown to have significant homology to phosphoglucomutases from eukaryotic and prokaryotic sources. The longer cDNA contained a putative transit-peptideencoding sequence, supporting the hypothesis that the isolated clones represent the cytosolic and plastidial isoforms of phosphoglucomutase in pea. Plastid protein import assays confirmed that the putative plastidial isoform was targeted to the plastid stroma where it was proteolytically processed. Expression, co-segregation, linkage, and molecular analyses have confirmed that the rug3 locus of pea encodes plastidial phosphoglucomutase. Mutations at this locus result in a near-starchless phenotype of the plant.

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“…The DNA species of 4 kb may be assigned to the yeast DNA fragment detected by Boles et al (1994) containing short dispersed similarities to yeast PGM genes. PGM was sequenced in a variety of cell types including bacteria (Lu and Kleckner 1994;Qian et al 1994), plant (Penger et al 1994) and mammals (Ray et al 1983;Whitehouse et al 1992;Rivera et al 1993;Lee at al. 1992) with three genes and several isoforms found in humans (Edwards et al 1995).…”

Section: Discussionmentioning

confidence: 99%

A comparative hybridization analysis of yeast DNA withParameciumparafusin- and different phosphoglucomutase-specific probes

Wyroba¹,

Satir²

2000

Biochem. Cell Biol.

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Molecular probes designed for the parafusin (PFUS), the Paramecium exocytic-sensitive phosphoglycoprotein, gave distinct hybridization patterns in Saccharomyces cerevisiae genomic DNA when compared with different phosphoglucomutase specific probes. These include two probes identical to segments of yeast phosphoglucomutase (PGM) genes 1 and 2. Neither of the PGM probes revealed the 7.4 and 5.9 kb fragments in Bgl II-cut yeast DNA digest detected with the 1.6 kb cloned PFUS cDNA and oligonucleotide constructed to the PFUS region (insertion 3--I-3) not found in other species. PCR amplification with PFUS-specific primers generated yeast DNA-species of the predicted molecular size which hybridized to the I-3 probe. A search of the yeast genome database produced an unassigned nucleotide sequence that showed 55% identity to parafusin gene and 37% identity to PGM2 (the major isoform of yeast phosphoglucomutase) within the amplified region.

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cDNA Sequence for the Plastidic Phosphoglucomutase from Spinacia oleracea (L.)

Abstract: , for providing the yeast mutant strain.

Cited by 8 publications

References 5 publications

Antisense inhibition of plastidial phosphoglucomutase provides compelling evidence that potato tuber amyloplasts import carbon from the cytosol in the form of glucose‐6‐phosphate

Antisense inhibition of plastidial phosphoglucomutase provides compelling evidence that potato tuber amyloplasts import carbon from the cytosol in the form of glucose‐6‐phosphate

The rug3 Locus of Pea Encodes Plastidial Phosphoglucomutase

A comparative hybridization analysis of yeast DNA withParameciumparafusin- and different phosphoglucomutase-specific probes

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