Sucrose-phosphate synthase is regulated via metabolites and protein phosphorylation in potato tubers, in a manner analogous to the enzyme in ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-02

AUTHORS

Ralph Reimholz, Peter Geigenberger, Mark Stitt

ABSTRACT

(i) Sucrose-phosphate synthase (SPS) was purified 40-fold from stored potato (Solanum tuberosum L.) tubers to a final specific activity of 33–70 nkat·(mg protein)−1 via batch elution from diethylaminoethyl (DEAE)-sephacel, polyethylene glycol (PEG) precipitation and Mono Q anion-exchange chromatography. (ii) Immunoblotting revealed a major and a minor band with molecular weights of 124.8 kDa and 133.5 kDa, respectively. Both bands were also present in extracts prepared in boiling SDS to exclude proteolysis. No smaller polypeptides were seen, except when the preparations were incubated before application on a polyacrylamide gel. (iii) The enzyme preparation was activated by glucose-6-phosphate and inhibited by inorganic phosphate. Both effectors had a large effect on the Km (fructose-6-phosphate) and the Km (uridine-5-diphosphoglucose) with phosphate acting antagonistically to glucose-6-phosphate. (iv) Preincubation of potato slices with low concentrations of okadaic acid or microcystin resulted in a three- to fourfold decrease in the activity of SPS when the tissue was subsequently extracted and assayed. The decrease was especially marked when the assay contained low concentrations of substrates and glucose-6-phosphate, and inorganic phosphate was included. Preincubation with mannose or in high osmoticum resulted in an increase of SPS activity. (v) Analogous changes were observed in germinating Ricinus communis L. seedlings. After preincubation of the cotyledons in glucose, high SPS activity could be measured, whereas okadaic acid, omission of glucose, or addition of phosphate or sucrose led to a large decrease of SPS activity in the “selective” assay. (vi) It is argued that SPS from non-photosynthetic tissues is regulated by metabolites and by protein phosphorylation in an analogous manner to the leaf enzyme. More... »

PAGES

480-488

Journal

TITLE

Planta

ISSUE

4

VOLUME

192

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00203585

DOI

http://dx.doi.org/10.1007/bf00203585

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1051185207


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