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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Amino Acid Biosynthetic Pathways01:29

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Fluorescent Immunolocalization of Arabinogalactan Proteins and Pectins in the Cell Wall of Plant Tissues
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Plant Protein O-Arabinosylation.

Bent Larsen Petersen1, Cora A MacAlister2, Peter Ulvskov1

  • 1Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Copenhagen, Denmark.

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|April 5, 2021
PubMed
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Plant O-arabinosylation modifies hydroxyprolines (Hyp) in proteins crucial for development and stress responses. This glycosylation impacts protein transport and function, with key enzymes and protein types now better understood.

Keywords:
arabinogalactan proteinextensinhydroxyproline glycoprotein modulehydroxyproline-arabinosylationpeptide hormoneplant allergensplant protein O-glycosylationsecretory pathway

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Area of Science:

  • Plant molecular biology
  • Post-translational modifications
  • Protein glycosylation

Background:

  • O-arabinosylation of hydroxyprolines (Hyp) is vital for diverse plant proteins, including structural extensins and signaling peptides.
  • This modification involves proline hydroxylation by prolyl-4-hydroxylases (P4H) followed by O-glycosylation by arabinofuranosyltransferases (AraT).
  • Mutations affecting Hyp formation or arabinosylation often result in truncated root-hair phenotypes, complicating genotype-phenotype correlations.

Purpose of the Study:

  • To provide an updated overview of O-arabinosylated proteins in plants.
  • To detail the enzymatic machinery involved in plant O-arabinosylation.
  • To highlight the functional significance of O-arabinosylation in protein transport and the secretory pathway.

Main Methods:

  • Literature review and synthesis of recent findings.
  • Functional characterization of identified P4H and AraT enzymes.
  • Analysis of mutant phenotypes related to Hyp modification.

Main Results:

  • Identified a range of O-arabinosylated proteins with roles in development, defense, and stress.
  • Characterized a subset of P4H enzymes and most AraT enzymes involved in synthesizing arabinose chains.
  • Demonstrated that impaired arabinosylation affects protein transport in the secretory pathway.

Conclusions:

  • O-arabinosylation is a widespread and functionally important post-translational modification in plants.
  • The enzymatic machinery for O-arabinosylation is increasingly understood.
  • Proper arabinosylation is crucial for protein trafficking and function, adding another layer of regulatory complexity.