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    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Genetics

    Background:

    • Selenocysteine (Sec) is an amino acid naturally incorporated into proteins via recoding of the UGA stop codon.
    • The mechanism of Sec insertion typically involves competition with protein termination factors at UGA.
    • Understanding alternative Sec incorporation pathways is crucial for protein engineering and synthetic biology.

    Purpose of the Study:

    • To investigate the ability of the Sec insertion machinery to utilize codons other than UGA.
    • To determine the efficiency and fidelity of Sec incorporation at non-canonical codons.
    • To explore the implications of sense codon recoding for selenoprotein production and translation.

    Main Methods:

    • Site-specific incorporation of selenocysteine directed by various sense codons.
    • Expression and purification of recombinant proteins (E. coli formate dehydrogenase, human thioredoxin reductase).
    • Biochemical and biophysical analyses to confirm Sec incorporation and protein function.

    Main Results:

    • The Sec insertion machinery successfully recoded 58 out of 64 possible codons.
    • Complete conversion of 15 sense codons to Sec incorporation was observed.
    • A tenfold increase in selenoprotein yield was achieved compared to UGA-directed Sec insertion.
    • High-fidelity sense-codon recoding was demonstrated for specific enzymes.
    • The Sec machinery outcompeted abundant aminoacyl-tRNAs for sense codon decoding.

    Conclusions:

    • The biological cell possesses a versatile Sec insertion machinery capable of recoding a wide range of sense codons.
    • Sense codon recoding offers a powerful strategy for significantly enhancing selenoprotein yield.
    • These findings challenge existing paradigms of translation and expand the potential information storage capacity of the genetic code.