Starch phosphorylase isoenzymes in mesophyll and bundle sheath cells of corn leaves

Mateyka, Christian; Schnarrenberger, Claus

doi:10.1016/0304-4211(84)90245-1

Cited by 11 publications

(5 citation statements)

References 18 publications

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“…Within the resolution of the method, this is in agreement with previous findings that the proportion of chloroplastic enzyme activity is 90, 20, and 40%, respectively, of the total activity for these enzymes in green leaves (Schnarrenberger and Oeser, 1974;Kurzok and Feierabend, 1984;Schnarrenberger, 1984;Schnarrenberger and Kriiger, 1986). These results strengthen the conclusion that only little, if any, of the activities of transaldolase, transketolase, Rib-5-P isomerase, and ribulose-5-P epimerase is attributable to the cytosolic cell fraction.…”

Section: Resultssupporting

confidence: 92%

“…However, it has been possible by using anion-exchange chromatography to separate a11 other chloroplast/cytosol isoenzymes of sugar phosphate metabolism investigated to date, e.g. starch phosphorylase (Steup et al, 1980;Mateyka and Schnarrenberger, 1984), phosphoglucomutase (Mühlbach and Schnarrenberger, 1978), Glc-P isomerase (Schnarrenberger and Oeser, 1974), FBPase (Latzko et al, 19741, FBP aldolase (Kriiger and Schnarrenberger, 1983;Lebherz et al, 1984;Schnarrenberger and Kriiger, 1986), hexokinase (Schnarrenberger, 1990), G6PDH and 6PGDH (Schnarrenberger et al, 1973(Schnarrenberger et al, , 1975Simcox et al, 1977;Simcox and Dennis, 1978;Nishimura and Beevers, 19811, glyceraldehyde-3-P dehydrogenase (Miernyk and Dennis, 19821, 3-phosphoglycerate kinase (Miernyk and Dennis, 1982;Kopke-Secundo et al, 1990;Morrow and Bradbeer, 1990), triose-P isomerase (Kurzok and Feierabend, 1984), pyruvate kinase (Ireland et al, 1979), and enolase and phosphoglycerate mutase (Miernyk and Dennis, 1982;Plaxton, 1989). It is conceivable, yet we consider it highly unlikely, that isoenzymes for transaldolase, transketolase, Rib-5-P isomerase, and ribulose-5-P epimerase exist but are undetectable.…”

Section: Resultsmentioning

confidence: 99%

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Enzymatic Evidence for a Complete Oxidative Pentose Phosphate Pathway in Chloroplasts and an Incomplete Pathway in the Cytosol of Spinach Leaves

1995

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l h e intracellular localization of transaldolase, transketolase, ribose-5-phosphate isomerase, and ribulose-5-phosphate epimerase was reexamined in spinach (Spinacia oleracea 1,) leaves. We found a highly predominant if not exclusive localization of these enzyme activities in chloroplasts isolated by isopyknic centrifugation in sucrose gradients. Clucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, glucose phosphate isomerase, and triose phosphate isomerase activity was present in the chloroplast fraction but showed additional activity in the cytosol (supernatant) fraction attributable to the cytosol-specific isoforms known to exist for these enzymes. Anion-exchange chromatography of proteins of crude extracts on diethylaminoethyl-Fractogel revealed only a single enzyme each for transaldolase, transketolase, ribose-5-phosphate isomerase, and ribulose-5-phosphate epimerase. The data indicate that chloroplasts of spinach leaf cells possess the complete complement of enzymes of the oxidative pentose phosphate pathway (OPPP), whereas the cytosol contains only the first two reactions, contrary to the widely held view that plants generally possess a cytosolic OPPP capable of cyclic function. l h e chloroplast enzymes transketolase, ribose-5-phosphate isomerase, and ribulose-5-phosphate epimerase appear to be amphibolic for the Calvin cycle and OPPP.

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Section: Resultssupporting

confidence: 92%

Section: Resultsmentioning

confidence: 99%

Enzymatic Evidence for a Complete Oxidative Pentose Phosphate Pathway in Chloroplasts and an Incomplete Pathway in the Cytosol of Spinach Leaves

1995

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“…The results of one representative experiment are shown. The elution profiles of the plastidic and cytosolic isoenzymes were very similar to previously published results from other plant tissues (19,22,23,26,29,32).…”

Section: Resultssupporting

confidence: 86%

Repression of the Plastidic Isoenzymes of Aldolase, 3-Phosphoglycerate Kinase, and Triosephosphate Isomerase in the Barley Mutant “albostrians”

Boldt¹,

Börner²,

Schnarrenberger³

1992

Plant Physiol.

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White leaves of the mutant line albostrians and green leaves of the wild-type cultivar Salome of barley (Hordeum vulgare L.) were screened for the presence of plastidic and cytosolic isoenzymes of sugar-phosphate metabolism. lsoenzyme separation was achieved by anion-exchange chromatography on Fractogel TSK DEAE-650(S). The mutant tissue had a markedly reduced level of plastidic 3-phosphoglycerate kinase, triosephosphate isomerase, and aldolase activity. In contrast, the activity of plastidic glucosephosphate isomerase, fructose 1,6-bisphosphatase, 6-phosphogluconate dehydrogenase, starch phosphorylase, and ADP-glucose pyrophosphorylase was in the same range as in wild-type leaf tissue. The activity of the corresponding cytosolic isoenzymes (including UDPglucose pyrophosphorylase) showed essentially no differences in mutant and wild type. The same trend was observed in dark-grown mutant and wild-type leaves. Interestingly, the total activity levels of all isoenzymes were about the same when comparing darkgrown and light-grown mutant or wild-type plants. From these data, it is concluded that mutant leaves exhibit a selective decrease of a subgroup of plastidic isoenzymes associated with the Calvin cycle.

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“…The differential expression of Calvin cycle enzymes in the mesophyll and bundle-sheath of C4 plants [ 16,20,27,44,45] provides a convenient and effective tool for the isolation of molecular probes for Calvin cycle genes. Here we have used the differential screening approach with subtracted mesophyll and bundle-sheath cDNA probes to isolate the first plant cDNA for R5P3Es from bundle-sheath cells of the C4 plant Sorghum bicolor.…”

Section: Introductionmentioning

confidence: 99%

Cloning of the amphibolic Calvin cycle/OPPP enzyme d-ribulose-5-phosphate 3-epimerase (EC 5.1.3.1) from spinach chloroplasts: functional and evolutionary aspects

et al. 1995

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Exploiting the differential expression of genes for Calvin cycle enzymes in bundle-sheath and mesophyll cells of the C4 plant Sorghum bicolor L., we isolated via subtractive hybridization a molecular probe for the Calvin cycle enzyme D-ribulose-5-phosphate 3-epimerase (R5P3E)(EC 5.1.3.1), with the help of which several full-size cDNAs were isolated from spinach. Functional identity of the encoded mature subunit was shown by R5P3E activity found in affinity-purified glutatione S-transferase fusions expressed in Escherichia coli and by three-fold increase of R5P3E activity upon induction of E. coli overexpressing the spinach subunit under the control of the bacteriophage T7 promoter, demonstrating that we have cloned the first functional ribulose-5-phosphate 3-epimerase from any eukaryotic source. The chloroplast enzyme from spinach shares about 50% amino acid identity with its homologues from the Calvin cycle operons of the autotrophic purple bacteria Alcaligenes eutrophus and Rhodospirillum rubrum. A R5P3E-related eubacterial gene family was identified which arose through ancient duplications in prokaryotic chromosomes, three R5P3E-related genes of yet unknown function have persisted to the present within the E. coli genome. A gene phylogeny reveals that spinach R5P3E is more similar to eubacterial homologues than to the yeast sequence, suggesting a eubacterial origin for this plant nuclear gene.

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Starch phosphorylase isoenzymes in mesophyll and bundle sheath cells of corn leaves

Cited by 11 publications

References 18 publications

Enzymatic Evidence for a Complete Oxidative Pentose Phosphate Pathway in Chloroplasts and an Incomplete Pathway in the Cytosol of Spinach Leaves

Enzymatic Evidence for a Complete Oxidative Pentose Phosphate Pathway in Chloroplasts and an Incomplete Pathway in the Cytosol of Spinach Leaves

Repression of the Plastidic Isoenzymes of Aldolase, 3-Phosphoglycerate Kinase, and Triosephosphate Isomerase in the Barley Mutant “albostrians”

Cloning of the amphibolic Calvin cycle/OPPP enzyme d-ribulose-5-phosphate 3-epimerase (EC 5.1.3.1) from spinach chloroplasts: functional and evolutionary aspects

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