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Biosynthesis of Polysaccharides

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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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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,...
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G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
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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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While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
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Uracil-DNA Glycosylase Assay by Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry Analysis
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Structural and Functional Insights into UDGs.

Shreya Roy1, Md Khabeer Azhar1,2, Vibha Gupta1

  • 1Department of Biotechnology, Jaypee Institute of Information Technology, A-10 Sec 62, Noida, 201309, India.

Protein and Peptide Letters
|January 6, 2025
PubMed
Summary
This summary is machine-generated.

Uracil DNA glycosylases (UDGs) repair DNA damage by removing uracil. A unique UDGX from Mycobacterium smegmatis forms a stable DNA complex, potentially protecting the genome, with structural insights aiding theranostic applications.

Keywords:
Base-excision repairR-loopUDGXdiagnostics.structureuracil DNA glycosylases

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • DNA damage necessitates repair pathways across all life domains.
  • Uracil DNA glycosylases (UDGs) are key enzymes in the base-excision repair (BER) pathway, removing uracil from DNA.
  • UDGs are classified into six families, sharing conserved motifs for DNA binding and catalysis.

Purpose of the Study:

  • To review the structural and functional aspects of UDG families.
  • To highlight the unique characteristics of the unconventional UDGX from Mycobacterium smegmatis.
  • To explore potential theranostic applications of UDGs.

Main Methods:

  • Structural analysis of UDG families, including UDGX.
  • Examination of UDG-DNA interactions and catalytic mechanisms.
  • Review of existing literature and PDB structural data.

Main Results:

  • UDGX forms an irreversible, highly stable complex with DNA, unlike other UDGs.
  • This UDGX mechanism prevents uracil excision and may protect genomic integrity.
  • Bacterial survival under hypoxia is reduced by MsmUDGX overexpression.
  • High-resolution 3D structures of apo and DNA-bound MsmUDGX are available.

Conclusions:

  • UDGX represents an unconventional UDG with a unique DNA-binding mechanism.
  • The UDGX suicide inactivation may confer genomic protection, particularly under stress.
  • Understanding UDG structures and functions is crucial for developing theranostic tools.