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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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In 1971, Peter Perlman and Eva Engvall developed an Enzyme-linked immunosorbent assay (ELISA or EIA). ELISA differs from western blot in that the assays are conducted in microtiter plates or in vivo rather than on an absorbent membrane.
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Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
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Related Experiment Video

Updated: Apr 3, 2026

Biological Samples Preparation for Speciation at Cryogenic Temperature using High-Resolution X-Ray Absorption Spectroscopy
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The evolving versatility of selenium in biology.

Regina Brigelius-Flohé1

  • 1German Institute of Human Nutrition Potsdam-Rehbruecke , Nuthetal, Germany .

Antioxidants & Redox Signaling
|September 26, 2015
PubMed
Summary

This review highlights novel functions of selenoproteins beyond antioxidant roles. These proteins are involved in energy metabolism, posttranslational modifications, and protein trafficking, expanding our understanding of selenium

Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Metabolism
  • Protein Chemistry

Background:

  • Explores recent advancements in understanding selenoprotein biosynthesis and function.
  • Reviews the involvement of identified selenoproteins, including selenocysteine-β-lyase, in cellular processes.

Discussion:

  • Thioredoxin reductase 1 (TrxR1) exhibits dynamic antioxidant/pro-oxidant activity, influencing the Nrf2/Keap1 pathway.
  • Methionine sulfoxide reductase B1 (MsrB1) catalyzes a newly identified posttranslational protein modification.
  • Membrane-bound selenoproteins (Sel K, S, T, N, I) form crucial selenylsulfide bonds for protein complex stabilization and trafficking.

Key Insights:

  • Selenoprotein K (SelK) facilitates palmitoylation of membrane proteins via complex stabilization.

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  • Selenoproteins' roles extend beyond oxidative stress defense to encompass energy metabolism and signaling.
  • Emerging evidence reveals diverse functions for selenium and its associated proteins in cellular regulation.

    • Outlook:

    • Further research is needed to fully elucidate the complex regulatory networks involving selenoproteins.
    • Investigating the link between selenoproteins and energy metabolism may reveal new therapeutic targets.
    • The discovery of novel functions underscores the broad importance of selenium in human health.