In situ analysis of enzymes involved in sucrose to hexose-phosphate conversion during stolon-to-tuber transition of potato.

Abstract:

:An in situ study of enzymes involved in sucrose to hexose-phosphate conversion during in vitro stolon-to-tuber transition of potato (Solanum tuberosum L. cv. Bintje) was employed to follow developmental changes in spatial patterns. In situ activity of the respective enzymes was visualized by specific activity-staining techniques and they revealed distinct spatially and developmentally regulated patterns. Two of the enzymes studied were also subject to in situ investigations at the transcriptional level. During the stages of stolon formation high hexokinase (EC 2.7.1.1) and acid (cell wall-bound) invertase (EC 3.2.1.26) activities were restricted to the mitotically active (sub)apical region, suggesting a possible importance of these enzymes for cell division. At the onset of tuberization sucrose synthase (EC 2.4.1.13) and fructokinase (EC 2.7.1.4) were strongly induced (visualized at transcriptional and translational level) and the acid invertase activities disappeared from the swelling subapical region as expected. The high degree of similarity in the spatial pattern and the temporal induction of sucrose synthase and fructokinase suggests a tightly co-ordinated coarse (up)regulation, which may be subject to a sugar-modulated mechanism(s) by which genes involved in the metabolic sucrose-starch converting potential are co-ordinately regulated during tuber growth. The overall activity of uridine-5-diphosphoglucose pyrophosphorylase (EC 2.7.7.9) was present in all tissues during stolon and tuber development, implying that its coarse control is not subject to (in)direct developmental regulation.

journal_name

Physiol Plant

journal_title

Physiologia plantarum

authors

Appeldoorn NJ,Sergeeva L,Vreugdenhil D,Van Der Plas LH,Visser RG

doi

10.1034/j.1399-3054.2002.1150218.x

subject

Has Abstract

pub_date

2002-06-01 00:00:00

pages

303-310

issue

2

eissn

0031-9317

issn

1399-3054

pii

ppl1150218

journal_volume

115

pub_type

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