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01:26Protein 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.
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.
02:26Preparation and Reactions of Sulfides
Sulfides are the sulfur analog of ethers, just as thiols are the sulfur analog of alcohol. Like ethers, sulfides also consist of two hydrocarbon groups bonded to the central sulfur atom. Depending upon the type of groups present, sulfides can be symmetrical or asymmetrical. Symmetrical sulfides can be prepared via an SN2 reaction between 2 equivalents of an alkyl halide and one equivalent of sodium sulfide.
01:20Sulfur 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...
02:33Preparation and Reactions of Thiols
Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol.
02:17Structure and Nomenclature of Thiols and Sulfides
Thiols and sulfides are sulfur analogs of alcohols and ethers, respectively, where the sulfur atom takes the place of the oxygen atom. Thus, thiols are generally represented as RSH, where R is an alkyl substituent and —SH is the functional group. On the other hand, in sulfides, the central sulfur atom is bonded to two hydrocarbon groups on either side. Depending upon the type of group, sulfides can be either symmetrical or asymmetrical. Both thiols and sulfides display a bent geometry, similar...
01:29Microbes and the Sulfur Cycle
Sulfur is a vital element in Earth's biogeochemical systems. It transitions through various inorganic states, including sulfate (SO₄²⁻), elemental sulfur (S⁰), and sulfide (S²⁻). Abiotic and biological mechanisms across oxic and anoxic environments intricately mediate these transformations. Sulfate, the most oxidized form of sulfur, is predominantly stored in rocks, marine sediments, and oceanic waters, acting as a long-term reservoir in the global sulfur cycle.In oxic environments,...
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Disulfide bond isomerization in prokaryotes.
Stefan Gleiter1, James C A Bardwell
1Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI 48109-1048, USA.
Biochimica Et Biophysica Acta
|March 18, 2008
Summary
Prokaryotic proteins need disulfide isomerization for correct folding, a process mainly catalyzed by DsbC (disulfide bond C). This review covers current knowledge on prokaryotic disulfide isomerization mechanisms.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Folding
Background:
- Proteins with multiple cysteine residues often require disulfide isomerization to achieve their native conformation.
- In prokaryotes, the disulfide bond C (DsbC) protein is the primary catalyst for this crucial reaction.
- DsbC shares significant structural and mechanistic similarities with eukaryotic protein disulfide isomerase.
Purpose of the Study:
- To review the current understanding of disulfide isomerization in prokaryotic systems.
- To highlight the role and mechanism of DsbC in prokaryotic protein folding.
- To compare prokaryotic and eukaryotic disulfide isomerization processes.
Main Methods:
- Literature review of existing research on DsbC and disulfide isomerization in prokaryotes.
Main Results:
- Disulfide isomerization is essential for the correct folding of many prokaryotic proteins.
- DsbC is a key enzyme in prokaryotes, facilitating the rearrangement of incorrect disulfide bonds.
- The mechanism of DsbC is conserved across prokaryotes and shares features with eukaryotic PDI.
Conclusions:
- Disulfide isomerization is a critical post-translational modification in prokaryotes, primarily mediated by DsbC.
- Understanding DsbC function provides insights into protein folding and quality control in bacteria.
- Further research into DsbC can inform strategies for protein engineering and therapeutic development.