Cited by 33Photosynthetic Processes and MechanismsGlycogen Storage Diseases and MyoclonusGene Regulatory Network Analysis

Ultrasensitive behavior in the synthesis of storage polysaccharides in cyanobacteria

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Gómez-Casati, Diego F., Cortassa, Sonia, Aon, Miguel A., Iglesias, Alberto A.·2003·Planta

Abstract

The glycogen synthetic pathway operates ultrasensitively as a function of the ADPglucose pyrophosphorylase (ADPGlcPPase) allosteric effectors, 3-phosphoglycerate and Pi, in permeabilized cells of the cyanobacterium Anabaena PCC 7120. In vitro data previously showed that the ultrasensitive behavior of ADPGlcPPase depends upon cross-talk between the two allosteric effectors, the enzyme's response being additionally modulated by molecular crowding [D.F. Gómez Casatiet al. (2000) Biochem J 350:139-147]. In the present work we show, experimentally and with a mathematical model, that alpha-1,4-glucan synthesis is also ultrasensitive in cells due to the propagation of the switch-like behavior of ADPGlcPPase to the synthetic pathway. Amplifications of up to 20-fold in storage-polysaccharide synthesis can be achieved with a modest 6.7-fold increase in 3-phosphoglycerate in the presence of 5 mM Pi in contrast to the 30-fold necessary in its absence. This is the first time that this phenomenon has been reported to occur in the glycogen synthetic pathway of a photosynthetic prokaryote. The implications of the results for plant cell physiology during light-dark transitions are discussed.

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Crossref · 10.1007/s00425-002-0949-4

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33 of 33 references verified0 citation errors · 0 not checkable

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  • ADP-glucose diphosphorylase (AGPase) controls glycogen synthesis in bacteria in an ATP-dependent reaction and seems to be regulated by 3PG (activator) and Pi (inhibitor).

    “The enzyme ADP-glucose diphosphorylase (AGPase; EC 2.7.7.27, encoded by the agp gene, also known as glgC) controls glycogen synthesis in bacteria in an ATP-dependent reaction and seems to be regulated by 3PG (activator) and Pi (inhibitor) (Ballicora et al. 2003; Gomez-Casati et al. 2003).”

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Authors
Gómez-Casati, D. F., Cortassa, S., Aon, M. A., & Iglesias, A. A.
Affiliations
Instituto Tecnológico de Chascomús (AR)
Venue
Planta
Published
2003-01-28
Volume
216
Issue
6
Pages
969-975
ISSN
  • 0032-0935 (ISSN-L)
  • 1432-2048
OpenAlex
W1228192507
Cited by
33
References
33
Citations by year
2023: 2 · 2022: 3 · 2021: 5 · 2020: 1 · 2019: 5 · 2017: 2 · 2015: 1 · 2014: 1 · 2012: 3
FWCI
0.80
Type
journal article
Language
en
Open access
Licence
Locations
  • Planta (publishedVersion)
  • PubMed (publishedVersion)
  • Conicet (submittedVersion, cc-by-nc-sa)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
  • Health Sciences › Medicine › Rheumatology › Glycogen Storage Diseases and Myoclonus
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Gene Regulatory Network Analysis
Keywords
ADP-glucose pyrophosphorylase, glycogen synthesis, allosteric regulation, 3-phosphoglycerate, inorganic phosphate, macromolecular crowding, switch-like behavior, storage polysaccharides, cyanobacteria, Anabaena sp. PCC 7120, mathematical modeling, photosynthetic prokaryotes, light-dark transition
MeSH terms
Adenosine Diphosphate Glucose, Cell Membrane Permeability, Glucans, Glucosephosphates, Glyceric Acids, Glycogen, Models, Biological, Nucleotidyltransferases, Anabaena, Glucose-1-Phosphate Adenylyltransferase

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