PMID:8314089
| Citation |
Ringquist, S, Schneider, D, Gibson, T, Baron, C, Böck, A and Gold, L (1994) Recognition of the mRNA selenocysteine insertion sequence by the specialized translational elongation factor SELB. Genes Dev. 8:376-85 |
|---|---|
| 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. |
| Links | |
| Keywords |
Bacterial Proteins/metabolism; Base Sequence; Binding Sites; Codon; Escherichia coli/genetics; Molecular Sequence Data; Peptide Chain Elongation, Translational/physiology; Peptide Chain Initiation, Translational/physiology; Peptide Elongation Factors/metabolism; Protein Binding; Protein Biosynthesis; Proteins; RNA, Messenger/metabolism; RNA, Transfer, Amino Acid-Specific; RNA, Transfer, Amino Acyl/metabolism; RNA, Transfer, Met/metabolism; Ribosomal Proteins/metabolism; Ribosomes/metabolism; Selenocysteine/genetics; Selenocysteine/metabolism; Selenoproteins; Sequence Analysis, RNA |
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