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Related Concept Videos

Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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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.
Glycosylation occurs in...
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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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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.
Multiple sugar molecules that may or may...
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Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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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...
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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

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Site-Specific Protein Modification with Reducing Carbohydrates.

Qifan Wu1, Weidong Dong2, Hui Miao1

  • 1State Key Laboratory and Institute of Elemento-Organic Chemistry, College of Chemistry, Nankai University, Tianjin, 300071, China.

Angewandte Chemie (International Ed. in English)
|February 28, 2022
PubMed
Summary
This summary is machine-generated.

Researchers developed a semisynthetic method to precisely attach carbohydrates to proteins, overcoming challenges in glycobiology. This technique enables the creation of homogeneous glycoproteins for advanced biological studies and applications.

Keywords:
Aspartate DerivativesGenetic Code ExpansionHydrazidesProtein GlycosylationReducing Carbohydrates

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Area of Science:

  • Biochemistry
  • Glycobiology
  • Synthetic Biology

Background:

  • Protein glycosylation is crucial for biological functions.
  • Natural glycoproteins exhibit heterogeneous oligosaccharides, complicating research.
  • Designing and synthesizing homogeneous glycoproteins remains a challenge.

Purpose of the Study:

  • To develop a semisynthetic method for site-specific protein modification with reducing carbohydrates.
  • To enable the construction of homogeneous glycoproteins with designed glycan structures.

Main Methods:

  • Genetic incorporation of side-chain-esterified aspartate.
  • Conversion to alanine-β-hydrazide (Aβz) for chemoselective conjugation.
  • Installation of Aβz-linked N-acetylglucosamine (GlcNAc) on proteins like IL-17A and RNase A.
  • Endoglycosidase-catalyzed transglycosylation for homogeneous glycan assembly.

Main Results:

  • A semisynthetic method for site-specific protein glycosylation was established.
  • Alanine-β-hydrazide (Aβz)-linked GlcNAc was successfully installed on various proteins.
  • Homogeneous glycans were assembled on proteins via transglycosylation reactions.

Conclusions:

  • The developed method allows for precise modification of proteins with carbohydrates.
  • This approach facilitates the creation of homogeneous glycoproteins, advancing glycobiology research and applications.