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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.
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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
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Disulfide Bonds: A Key Modification in Bacterial Extracytoplasmic Proteins.

S F Lee1,2,3,4, L Davey1,2,5

  • 11 Department of Microbiology and Immunology, Dalhousie University, Halifax, NS, Canada.

Journal of Dental Research
|August 12, 2017
PubMed
Summary

Oral bacteria utilize disulfide bonds, crucial for protein stability, impacting dental plaque formation and bacterial fitness. These bonds are formed by diverse thiol-disulfide oxidoreductases, essential for various bacterial processes.

Keywords:
Actinomyces orisStreptococcus gordoniibacteriocinsbiofilmsoral bacteriathiol-disulfide oxidoreductases

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Area of Science:

  • Microbiology
  • Biochemistry
  • Oral Biology

Background:

  • Disulfide bonds are vital posttranslational modifications for protein folding and stability in extracytoplasmic proteins across all domains of life.
  • Enzymes catalyzing disulfide bond formation are crucial for numerous biological processes, ensuring protein function.

Purpose of the Study:

  • To investigate the role and mechanisms of disulfide bond formation in oral bacteria.
  • To understand the impact of disulfide bond formation on dental plaque-related phenotypes and bacterial fitness.

Main Methods:

  • Review of existing literature and bioinformatic analysis of oral bacterial genomes.
  • Identification of thiol-disulfide oxidoreductases and their conserved motifs (CXXC active site, C-terminal cis-proline).

Main Results:

  • Gram-positive oral bacteria (e.g., Streptococcus gordonii, Actinomyces oris) use disulfide bonds for autolysis, biofilm formation, pilus assembly, and bacteriocin activity.
  • Gram-negative oral bacteria (e.g., Porphyromonas gingivalis, Tannerella forsythia) employ disulfide bonds to stabilize outer membrane porins.
  • Identified diverse thiol-disulfide oxidoreductases in oral bacteria, sharing key catalytic motifs.

Conclusions:

  • Disulfide bond formation is a significant, emerging area in oral microbiology.
  • This process critically influences dental plaque formation and the overall fitness of oral bacteria.