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Related Concept Videos

Protein Modifications in the RER01:26

Protein Modifications in the RER

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 sequences.
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Sulfur Assimilation

Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...

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Detecting, Visualizing and Quantitating the Generation of Reactive Oxygen Species in an Amoeba Model System
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In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG.

P H Bessette1, J J Cotto, H F Gilbert

  • 1Department of Chemical Engineering, University of Texas, Austin, Texas 78712, USA.

The Journal of Biological Chemistry
|March 13, 1999
PubMed
Summary

The DsbG protein in Escherichia coli is a periplasmic disulfide isomerase, not essential for growth but aids in folding complex proteins. It functions similarly to DsbC but with a more specific substrate range.

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Area of Science:

  • Microbiology
  • Protein Folding
  • Biochemistry

Background:

  • Escherichia coli possesses a complex system for protein folding in the periplasm.
  • The Dsb (disulfide bond) system is crucial for proper protein structure and function.
  • DsbG is a recently identified protein within this system, sharing homology with DsbC.

Purpose of the Study:

  • To characterize the in vivo and in vitro functions of the Escherichia coli DsbG protein.
  • To compare the properties and functions of DsbG with other known disulfide bond proteins like DsbC.
  • To investigate the role of DsbG in protein folding and disulfide bond formation.

Main Methods:

  • Characterization of DsbG expression levels in E. coli.
  • Analysis of DsbG's ability to form dimers and its equilibrium constant with glutathione.
  • Assessment of dsbG null mutants for growth defects and protein folding capabilities.
  • Evaluation of DsbG's ability to restore protein folding in dsbC mutants.
  • In vitro assays to test DsbG's catalytic activity, including insulin reduction.

Main Results:

  • DsbG forms a stable periplasmic dimer with glutathione binding properties similar to DsbA and DsbC.
  • DsbG is expressed at lower levels than DsbC and is not essential for E. coli growth.
  • DsbG can restore the folding of heterologous disulfide-containing proteins in dsbC mutants.
  • DsbG's active site thiols are reduced in vivo, suggesting a role in disulfide bond formation.
  • DsbG functions as a disulfide isomerase in vitro, but not as a reductase.

Conclusions:

  • DsbG primarily functions as a periplasmic disulfide isomerase in Escherichia coli.
  • DsbG exhibits a narrower substrate specificity compared to DsbC.
  • The dsbG gene is not essential, but DsbG plays a supportive role in disulfide bond formation for specific proteins.