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#selenocysteine incorporation

2 public questions tagged with this topic.

Selenocysteine and pyrrolysine incorporation represent

Selenocysteine and pyrrolysine incorporation exemplify programmed recoding events where stop codons acquire sense meaning through dedicated cis-elements and trans-factors rather than translational errors. Mechanisms involve competition with release factors RF1, RF2, eRF1, specialized tRNAs bearing UCA or CUA anticodons, unique elongation factors SelB, EFSec, and orthogonal synthetases PylRS plus mRNA signals SECIS or PYLIS. Recoding preserves genome-wide termination fidelity while permitting selective reassignment at specific loci. This represents evolutionary flexibility of genetic code, not frameshift, misincorporation, or post-translational modification. Such natural code expansion inspired synthetic biologists to engineer additional noncanonical amino acids expanding protein chemistry beyond twenty encoded residues naturally.

Ref: Alberts et al., Molecular Biology of the Cell, 7th ed., Chapter 6: Stop Codon Recoding as Genetic Code Expansion

SECIS element is located in eukaryotes at

Location of SECIS diverges between domains reflecting distinct recoding strategies. Eukaryotic SECIS lies in 3' untranslated region often 500 to 2500 nucleotides downstream of UGA, acting at distance via mRNA looping facilitated by SBP2 binding ribosome and eS31 protein. Multiple isoforms share conserved secondary structure but variable primary sequence. Bacterial SECIS immediately follows UGA within open reading frame, directly contacted by SelB C-terminal domain. Distant 3' UTR placement allows single SECIS to recode multiple UGAs and integrates selenium availability regulation effectively.

Ref: NCBI Bookshelf, Eukaryotic Translation: SECIS Location in 3′ UTR and Sec Incorporation