Abstract
The expression of long proteins with repetitive amino acid sequences often presents a challenge in recombinant systems. In published work, we optimized a translation system that efficiently circularizes mRNA in vivo via a permuted self-splicing group I intron from T4 bacteriophage and translates it into concatemeric protein products (termed “loopable” translation). Using our loopable translator system, we have designed a genetic construct in which the E. coli mRNA encoding the curli protein, CsgA, is circularized and translated into a CsgA concatemer through multiple ribosome transits.
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