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Polysaccharides such as glycogen and starch are synthesized from nucleoside diphosphate sugars, primarily uridine diphosphate glucose (UDPG) and adenosine diphosphate glucose (ADPG). These activated glucose donors act as key intermediates in carbohydrate metabolism and biosynthesis. UDPG primarily involves glycogen synthesis in animals and many bacteria, while ADPG plays a fundamental role in starch synthesis in plants and certain bacteria.UDPG is formed when glucose-1-phosphate reacts with...
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Carbohydrates are an essential part of the diet in humans and animals. Grains, fruits, and vegetables are natural sources of carbohydrates that provide energy to the body, particularly through glucose, a simple sugar that is a component of starch and an ingredient in many staple foods. The stoichiometric formula (CH2O)n, where n is the number of carbons in the molecule represents carbohydrates. In other words, the ratio of carbon to hydrogen to oxygen is 1:2:1 in carbohydrate molecules. This...
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The <i>Arabidopsis</i> O-fucosyltransferase SPINDLY regulates root hair patterning independently of gibberellin signaling.

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Balancing O-GlcNAc and O-fucose in plants.

Krishna Vasant Mutanwad1, Doris Lucyshyn1

  • 1Department of Applied Genetics and Cell Biology, Institute for Molecular Plant Biology, University of Natural Resources and Life Sciences, Vienna, Austria.

The FEBS Journal
|May 29, 2021
PubMed
Summary

Plants utilize O-fucose and O-GlcNAc modifications for nuclear and cytosolic protein regulation, unlike animals. This study explores how O-glycan-binding proteins may introduce regulatory flexibility and signal integration in plant glycosylation.

Keywords:
O-GlcNAcO-fucoseO-glycosylationplantssignaling

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Plant Science

Background:

  • O-linked glycosylation is a crucial post-translational modification in eukaryotes, essential for nuclear and cytosolic protein function.
  • While conserved, O-glycosylation mechanisms differ significantly between plants and animals.
  • Plants employ O-GlcNAc and O-fucose modifications, regulated by specific enzymes like SECRET AGENT (SEC) and SPINDLY (SPY), unlike the OGT/OGA system in animals.

Purpose of the Study:

  • To investigate the regulatory mechanisms of nucleocytoplasmic O-glycosylation in plants.
  • To address the open question of how specificity is achieved in plant O-glycosylation, given the limited number of modifying enzymes.
  • To propose a model where O-glycan-binding proteins introduce regulatory flexibility and signal integration.

Main Methods:

  • This study is a discussion and theoretical exploration, not based on experimental data.
  • It reviews existing knowledge on plant O-glycosylation pathways.
  • It proposes a hypothesis regarding the role of O-glycan-binding proteins.

Main Results:

  • Plant O-glycosylation involves O-GlcNAc and O-fucose modifications, catalyzed by SEC and SPY, respectively.
  • Specific glycoside hydrolases for these modifications in plants remain unidentified.
  • A significant number of plant proteins are affected by nucleocytoplasmic O-glycosylation, but the system's specificity is poorly understood.

Conclusions:

  • O-glycan-binding proteins are hypothesized to provide an additional regulatory layer in plant O-glycosylation.
  • These proteins could integrate internal and external signals into O-glycosylation-mediated pathways.
  • This mechanism offers a potential explanation for specificity in plant O-glycosylation signaling.