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Related Concept Videos

Sulfur Assimilation01:20

Sulfur Assimilation

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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...
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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.
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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Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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Export of Misfolded Proteins out of the ER01:32

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Protein Transport to the Thylakoids01:22

Protein Transport to the Thylakoids

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Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
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Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
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Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
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Rhodanese-Fold Containing Proteins in Humans: Not Just Key Players in Sulfur Trafficking.

Razan Alsohaibani1, Anne-Lise Claudel1, Romain Perchat-Varlet1

  • 1IMoPA, CNRS, Université de Lorraine, F-54000 Nancy, France.

Antioxidants (Basel, Switzerland)
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Summary

The Rhodanese-fold is a versatile protein domain in humans, crucial for sulfur transfer, metabolism, and cell regulation. This review details its structure, biochemistry, and diverse biological roles.

Keywords:
MoCo maturationRhodanese-foldcysteine persulfidepromiscuous activitiessulfur traffickingtRNA thiolation

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Human Physiology

Background:

  • The Rhodanese-fold is a common structural domain found in human proteins.
  • These proteins have varied architectures and physiological functions.
  • Catalytically active Rhodanese domains are key in sulfur transfer and other reactions.

Purpose of the Study:

  • To provide an exhaustive analysis of human Rhodanese-containing proteins.
  • To review their structural and biochemical properties.
  • To elucidate their established and putative roles in biological functions.

Main Methods:

  • Literature review of Rhodanese-containing proteins in humans.
  • Analysis of structural and biochemical data.
  • Compilation of functional roles in physiological and pathophysiological conditions.

Main Results:

  • Rhodanese domains exhibit diverse architectures and catalytic activities.
  • Key roles include sulfur trafficking, metabolism, cofactor biosynthesis, and tRNA modification.
  • Emerging functions in cell cycle regulation and tRNA hydroxylation are highlighted.

Conclusions:

  • Human Rhodanese-containing proteins are essential for numerous biological processes.
  • Understanding their properties is vital for comprehending human health and disease.
  • This review consolidates current knowledge and identifies future research directions.