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#selenocysteine

12 public questions tagged with this topic.

Both Sec and Pyl incorporation are examples of

Incorporation of twenty-first and twenty-second amino acids demonstrates natural genetic code expansion where organisms evolved extra chemistry beyond twenty canonical residues. Expansion requires novel amino acids, dedicated tRNAs with nonstandard structures, specific synthetases, and recoding signals repurposing stop codons while preserving termination fidelity. Unlike attenuation, RNA editing, or post-translational modifications, expansion alters translation table itself, increasing repertoire with selenol nucleophile and pyrroline-imine for catalysis. Synthetic biologists exploit these precedents to engineer codes incorporating unnatural amino acids. Evidence suggests code not completely frozen, acquiring new assignments when selective advantage provided.

Ref: Lodish et al., Molecular Cell Biology, 9th ed., Chapter 6: Genetic Code Expansion by Sec and Pyl

SECIS element allows UGA to function as

SECIS does not code amino acid but acts as recoding signal redefining upstream UGA termination into selenocysteine sense. Hairpin kink-turn formation creates platform for SBP2 binding, recruiting EFSec loaded with Sec-tRNASec to ribosome paused at UGA, excluding eRF1 and delaying hydrolysis. Reporter assays show inserting functional SECIS downstream restores activity when UGA placed at catalytic position, converting stop into Sec codon only when intact. Without SECIS, UGA releases peptide. Thus SECIS extends genetic code contextually, analogous to bacterial SECIS proximal element altering codon semantics via RNA structure-mediated recruitment.

Ref: Alberts et al., Molecular Biology of the Cell, 7th ed., Chapter 6: SECIS Converts UGA to Selenocysteine Codon

Selenocysteine incorporation requires which stop codon?

Universal code designates UGA as termination codon yet selenoproteins conserve in-frame UGA at catalytic centers for Sec insertion requiring recoding. Surveys show all confirmed vertebrate, bacterial, archaeal selenoproteins use UGA exclusively; UAA or UAG never encode selenium. Reason stems from anticodon compatibility, tRNASec UCA pairs perfectly with UGA requiring single modification, other stops would need different isoacceptors. Conservation allows kinetic competition control between release factor and SelB or EFSec. Fidelity depends on SECIS presence and selenium status, ensuring efficiency regulated by nutrient availability and release factor competition dynamics.

Ref: NCBI Bookshelf, Codon Usage: UGA as Selenocysteine Codon in Selenoproteins

Selenocysteine contains which atom instead of sulfur?

Chemically selenocysteine represents cysteine analogue where chalcogen sulfur replaced by heavier selenium, generating selenol side chain -SeH instead of thiol -SH. Selenium larger radius, higher polarizability, pKa approximately 5.2 versus cysteine 8.3, rendering selenolate anion predominant at physiological pH, conferring superior nucleophilicity, leaving group ability, and resistance to irreversible overoxidation forming selenenic acid reversible. This explains enhanced catalytic rate of glutathione peroxidases, thioredoxin reductases, and deiodinases. Selenium originates from dietary trace element via selenophosphate pathway, not post-translational sulfur substitution. Similarity permits substitution maintaining tertiary fold but dramatically alters redox potentials and enzymatic rate acceleration crucial for antioxidant defense.

Ref: Alberts et al., Molecular Biology of the Cell, 7th ed., Chapter 3: Selenocysteine – Selenium vs Sulfur Chemistry

Selenophosphate required for Sec synthesis is produced by

Selenium activation for selenocysteine synthesis relies on selenophosphate synthetase SelD in bacteria and SPS1/SPS2 isozymes in eukaryotes. Using ATP hydrolysis, SelD phosphorylates reduced selenide anion derived from selenite reduction via thiol systems or selenocysteine lyase, producing labile high-energy monoselenophosphate H2SePO3-. Mechanism proceeds through enzyme-bound pyrophosphate intermediate and selenide activation. Free selenocysteine extremely reactive, toxic, so selenophosphate directly delivers selenium within SepSecS or SelA active site onto tRNA-bound intermediate, avoiding cellular release. Deletion of selD eliminates all selenoproteins, causing oxidative stress hypersensitivity, embryonic lethality in mice, illustrating essential link between trace element biochemistry and translation regulation.

Ref: NCBI Bookshelf, Trace Element Biochemistry: SelD – Selenophosphate Synthetase

tRNA Sec is initially charged with

Selenocysteine biosynthesis uniquely occurs on its tRNA scaffold because free selenocysteine is unstable and oxidized spontaneously. Initial aminoacylation attaches serine, since no amino acid pool provides selenocysteine directly. Seryl-tRNA synthetase SerRS recognizes tRNASec despite unusual structure, esterifying serine to terminal A76 2' hydroxyl. This serine adduct provides hydroxyl substrate for subsequent phosphorylation reaction and replacement by selenophosphate donor. Maintaining amino acid covalently attached to tRNA throughout conversion avoids release of reactive intermediate, channels toxic selenium safely into protein, and ensures only tRNASec-dependent proteins undergo modification, preserving specificity across translation apparatus.

Ref: Lodish et al., Molecular Cell Biology, 9th ed., Chapter 5: tRNASec Aminoacylation with Serine

tRNA specific for selenocysteine is

Transfer RNA for selenocysteine tRNASec encoded by TRSP gene displays unusual architectural features distinguishing it from canonical tRNAs: nine base-pair acceptor plus TΨC helix with four unpaired nucleotides, long 6-base-pair D-stem, extra-long variable arm, and extensive modification preventing recognition by generic elongation factors. Anticodon UCA pairs with UGA, but decoding mediated by EFSec not eRF1, due to conformational dynamics. Its extended length and tertiary fold generate exclusive interface for modifying enzymes PSTK, SepSecS, and EFSec. This specialization underpins genetic code expansion ensuring selenocysteine not confused with serine or cysteine during elongation, highlighting structural basis for codon reassignment fidelity.

Ref: NCBI Bookshelf, tRNA Biology: Specialized tRNASec Structure and Function

Elongation factor specific for Sec in eukaryotes is

Eukaryotic selenocysteine delivery requires dedicated elongation factor eEFSec or EFSec, paralogous to canonical eEF1A but unable to bind standard aminoacyl-tRNAs. EFSec contains unique domain IV interacting with SBP2-SECIS complex and extended C-terminus specifically recognizing tRNASec distinct features including long variable arm and 13-base-pair acceptor-TΨC stack. GTP-bound EFSec delivers Sec-tRNASec to ribosomal A-site when UGA occupies decoding center, with GTP hydrolysis enabling accommodation and peptide transfer. This selectivity prevents misincorporation of biosynthetic intermediates serine or phosphoserine, ensuring fidelity. Regulation via GTPase cycle coordinates recoding efficiency with selenium nutritional status controlling EFSec expression.

Ref: Alberts et al., Molecular Biology of the Cell, 7th ed., Chapter 6: EFSec – Sec-Specific Elongation Factor

UGA is recoded as selenocysteine due to presence of

Recoding UGA from stop to selenocysteine relies on cis-acting SECIS element forming kink-turn hairpin structure with conserved quartet UGA, AUGA, and apical AAR motifs. Eukaryotic SECIS resides in 3' UTR; bacterial SECIS immediately downstream within coding region positioned to contact SelB. SECIS recruits trans-acting factors SBP2 and EFSec or SelB, positioning Sec-tRNASec near ribosomal A-site and antagonizing release factor access. Interaction involves ribosomal protein L30 and SBP2 Lys-rich domain, prolonging pause at UGA and favoring incorporation. Without SECIS, UGA triggers standard termination via eRF1. Hence RNA structure contextually modifies codon semantics enabling regulated selenoprotein expression.

Ref: Alberts et al., Molecular Biology of the Cell, 7th ed., Chapter 6: SECIS Element Mediated UGA Recoding

Selenocysteine is incorporated during

Unlike typical post-translational modifications such as phosphorylation or acetylation, selenocysteine incorporation occurs concurrently with polypeptide elongation at ribosome exit tunnel. UGA normally terminates translation via release factors, yet selenoprotein mRNAs carry downstream SECIS element recruiting SBP2 and EFSec. Sec-tRNASec delivered to ribosomal A-site pairs with UGA retained within coding frame, peptide bond formation directly inserts selenocysteine into nascent chain before chain release. This cotranslational recoding requires specialized tRNA, elongation factor, and SECIS-binding proteins, blurring distinction between regulatory signal and coding sequence. Thus selenocysteine becomes primary sequence component, not added after folding.

Ref: Lodish et al., Molecular Cell Biology, 9th ed., Chapter 5: Translation Exception – Co-translational Sec Insertion

Selenocysteine is known as the

Genetic code expansion beyond canonical twenty residues includes selenocysteine as unique amino acid incorporated into active sites of antioxidant oxidoreductases such as glutathione peroxidases, thioredoxin reductases, and formate dehydrogenases. Encoded by in-frame UGA codon recoded via specialized machinery, selenocysteine possesses selenol group with lower pKa ~5.2 and higher nucleophilicity than cysteine enhancing catalytic efficiency. Officially designated twenty-first proteinogenic amino acid, it occurs sparsely across all domains of life. Its discovery overturned dogma of immutable codon assignments, illustrating context-dependent recoding influenced by mRNA structure, selenium availability, and dedicated elongation factors enabling selenoprotein diversity.

Ref: Alberts et al., Molecular Biology of the Cell, 7th ed., Chapter 6: Selenocysteine – 21st Amino Acid

Which amino acid is encoded by the UGA stop codon but incorporated in certain proteins?

Selenocysteine is the scientifically accurate answer to this question. Within the study of Amino_Acids_Structure, this concept is well-established through extensive research and is documented in standard scientific literature. The specific properties, mechanisms, or characteristics of Selenocysteine directly address what is being asked. Among the other options, Pyrrolysine, Ornithine, and Citrulline do not correctly answer this question because they either refer to different concepts, describe properties of other molecules or processes, or represent common misconceptions about this topic.

Ref: Campbell Biology, Urry et al., 12th Ed.