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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.
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Sulfur Assimilation01:20

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...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome01:13

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Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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Related Experiment Video

Updated: Jun 22, 2026

Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O
03:09

Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O

Published on: August 9, 2024

Selenoprotein expression and function-selenoprotein W.

P D Whanger1

  • 1Department of Environmental and Molecular Toxicology, Oregon State University, Corvallis, OR 97330, USA. phil.whanger@oregonstate.edu

Biochimica Et Biophysica Acta
|May 26, 2009
PubMed
Summary
This summary is machine-generated.

Selenoprotein W (SeW) is a selenium-binding protein found in various species. Its exact biological functions are still under investigation, but it may act as an antioxidant and play roles in cell immunity.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Comparative Genomics

Background:

  • Selenoprotein W (SeW) is a small, selenium-dependent protein identified in animals with selenium deficiency.
  • SeW is highly expressed in muscle, heart, spleen, and brain tissues.
  • Amino acid sequences of SeW have been determined across eight diverse species.

Purpose of the Study:

  • To analyze the conserved and variable regions of Selenoprotein W across different species.
  • To investigate potential functional insights based on sequence homology and known modifications.
  • To highlight the current understanding and gaps in knowledge regarding SeW's biological roles.

Main Methods:

  • Deduced amino acid sequence analysis across eight species (mice, rats, monkeys, humans, sheep, pigs, fish, chickens).
  • Comparative analysis of cysteine and selenocysteine residue positions.
  • Identification of species-specific variations in cysteine content.
  • Review of existing evidence on SeW post-translational modifications (glutathionylation).

Main Results:

  • SeW sequences are identical between rats and mice, and between monkeys and humans.
  • Cysteine at residue 9 and selenocysteine at residue 13 are conserved across all eight species.
  • Residue 37 is cysteine in six species, with exceptions in fish and chickens.
  • Rodent SeW possesses four cysteines, while other species have two; glutathionylation confirmed in rats and monkeys.
  • Potential functions include antioxidant activity, stress response, cell immunity involvement, methylmercury targeting, and thioredoxin-like activity.

Conclusions:

  • SeW exhibits conserved structural features but also species-specific variations, particularly in cysteine content.
  • While its precise function remains elusive, SeW is implicated in crucial cellular processes.
  • Further research is needed to fully elucidate the biological roles and mechanisms of SeW across different species.