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Related Concept Videos

Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
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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...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

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Evolutionary and Biochemical Perspectives on the Incorporation and Utilization of Selenocysteine.

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Selenoprotein synthesis is not induced by hepatotoxic drugs.

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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

Threading the needle: getting selenocysteine into proteins.

Jesse Donovan1, Paul R Copeland

  • 1Department of Microbiology, Molecular Genetics, and Immunology, Graduate School of Biomedical Sciences, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, 675 Hoes Lane, Piscataway, NJ 08854, USA.

Antioxidants & Redox Signaling
|September 15, 2009
PubMed
Summary

Selenocysteine incorporation uses UGA as a sense codon via SECIS elements and binding proteins. Recent advances clarify the elusive mechanism altering canonical protein synthesis.

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Last Updated: Jun 20, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O
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Published on: August 9, 2024

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
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Published on: March 6, 2013

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Selenocysteine (Sec) is the 21st amino acid, incorporated co-translationally.
  • UGA normally signals termination but decodes as Sec in specific contexts.
  • This process requires a Sec insertion sequence (SECIS) element, SECIS binding protein 2 (SBP2), and a ternary complex.

Purpose of the Study:

  • To provide an overview of the mechanistic perspective on Sec incorporation.
  • To highlight recent advances in understanding this complex biological process.

Main Methods:

  • Literature review and synthesis of recent findings.
  • Mechanistic analysis of protein synthesis regulation.

Main Results:

  • The concerted action of SECIS, SBP2, and the Sec-specific ternary complex is crucial.
  • Recent studies have shed light on how these factors alter the canonical translation machinery.

Conclusions:

  • Understanding Sec incorporation mechanisms is vital for comprehending genetic code expansion.
  • Continued research promises further insights into this unique co-translational modification.