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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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.
Glycosylation occurs in...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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.
Multiple sugar molecules that may or may...
Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
Signal Sequences and Sorting Receptors01:41

Signal Sequences and Sorting Receptors

Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...

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Related Experiment Video

Updated: Jun 4, 2026

Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells
10:17

Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells

Published on: April 27, 2010

Do N-glycoproteins have preference for specific sequons?

R Shyama Prasad Rao, Wollenweber Bernd

    Bioinformation
    |March 3, 2011
    PubMed
    Summary

    Protein N-glycosylation sequon preference varies. Certain amino acids like phenylalanine (F) and glycine (G) are favored at the X position in NXS/T motifs, while proline (P) and charged amino acids are avoided, impacting protein glycosylation.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Bioinformatics

    Background:

    • Protein N-glycosylation is a crucial post-translational modification.
    • The consensus tri-peptide sequence NXS/T is required for N-glycosylation.
    • The amino acid at position X in the sequon influences glycosylation efficiency, with proline known to be inhibitory.

    Purpose of the Study:

    • To investigate the impact of different amino acids at position X of the NXS/T sequon on N-glycosylation.
    • To determine if specific amino acid preferences exist within N-glycosylation sequons across different proteomes.
    • To analyze the distribution of N-glycosylation sequon types in viral and eukaryotic proteins.

    Main Methods:

    • Markov chain analysis of NXS/T tri-peptides from viral, archaeal, and eukaryotic proteomes.
    Keywords:
    HIVInfluenzaN-glycoproteinsProbabilitySequons

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  • Analysis of experimentally confirmed N-glycosylated sequons from eukaryotic proteins.
  • Comparison of observed sequon frequencies against expected probabilities.

    • Main Results:

    • Most NXS/T sequon types occur at frequencies significantly different from expected probabilities.
    • Sequon types containing phenylalanine (F), glycine (G), isoleucine (I), serine (S), threonine (T), and valine (V) are consistently preferred.
    • Sequon types with proline (P) and charged amino acids are under-represented.
    • Viral glycoproteins like influenza hemagglutinin and HIV-1 gp120 show a prevalence of these preferred sequon types.

    Conclusions:

    • The choice of amino acid at position X significantly impacts the potential for N-glycosylation.
    • Specific amino acid preferences within N-glycosylation sequons exist across diverse biological groups.
    • These preferences may confer a selective advantage, particularly in viral glycoproteins.
    • The observed preferences for N-glycosylation sequons may not be exclusive to this modification.