The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Sucrose synthase isoforms in cultured tobacco cells

Author

Summary, in English

The plant enzyme sucrose synthase (SuSy; EC 2.4.1.13) catalyzes the reversible conversion of sucrose and UDP into UDP-glucose (UDP-Glc) and fructose. The enzyme exists in different isoforms and is both located in the cytosol, membrane-bound and associated to the actin cytoskeleton. We here investigate sucrose synthase from tobacco (Nicotiana tabacum L.) BY-2 heterotrophic cell suspensions. Two different isoforms of sucrose synthase SuSy1 and SuSy2, could be purified from cytosolic extracts of these cells using a combination of poly(ethylene glycol) (PEG) precipitation, gel filtration, ion-exchange chromatography and affinity chromatography. They were clearly distinct. both with regard to the binding to the ion-exchange column and with regard to their kinetic and regulatory properties. SuSy 1, the more abundant species, showed lower V-max and K-m for sucrose and UDP compared to the less abundant SuSy2. The activity of SuSy2 in the breakdown direction was stimulated by 60% by actin, in contrast to that of SuSy 1, which showed a 17% inhibition. An indication of interaction between SuSy I and actin was obtained by partitioning in aqueous Dextran-PEG two-phase systems. Furthermore, fructose 2,6-bisphosphate (F26BP) at micromolar concentrations stimulated SuSy2 in the presence of actin while SuSy I was strongly inhibited by fructose. Possible roles of these two isoforms in the sucrose turnover in BY-2 cells are discussed. (C) 2004 Elsevier SAS. All rights reserved.

Publishing year

2004

Language

English

Pages

299-306

Publication/Series

Plant Physiology and Biochemistry

Volume

42

Issue

4

Document type

Journal article

Publisher

Elsevier

Topic

  • Biological Sciences

Keywords

  • Two-phase partitioning
  • Tobacco
  • Sucrose synthase
  • Sucrolysis
  • 6-bisphosphate
  • Fructose 2
  • Actin
  • BY-2 cells

Status

Published

ISBN/ISSN/Other

  • ISSN: 1873-2690