Recognition of the mRNA selenocysteine insertion sequence by the specialized translational elongation factor SELB

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Abstract

In Escherichia coli the unusual amino acid selenocysteine is incorporated cotranslationally at an in-frame UGA codon. Incorporation of selenocysteine relies, in part, on the interaction between a specialized elongation factor, the SELB protein, and a cis-acting element within the mRNA. Boundary and toeprint experiments illustrate that the SELB-GTP-Sec-tRNA(Sec) ternary complex binds to the selenoprotein encoding mRNAs fdhF and fdnG, serving to increase the concentration of SELB and Sec-tRNA(Sec) on these mRNAs in vivo. Moreover, toeprint experiments indicate that SELB recognizes the ribosome- bound message and that, upon binding, SELB may protrude out of the ribosomal- mRNA track so as to approach the large ribosomal subunit. The results place the mRNA-bound SELB-GTP-Sec-tRNA(Sec) ternary complex at the selenocysteine codon (as expected) and suggest a mechanism to explain the specificity of selenocysteine insertion. Cis-acting mRNA regulatory elements can tether protein factors to the translation complex during protein synthesis.

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Ringquist, S., Schneider, D., Gibson, T., Baron, C., Böck, A., & Gold, L. (1994). Recognition of the mRNA selenocysteine insertion sequence by the specialized translational elongation factor SELB. Genes and Development, 8(3), 376–385. https://doi.org/10.1101/gad.8.3.376

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