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Recognition of the mRNA selenocysteine i ... lational elongation factor SELB
Recognition of the mRNA selenocysteine insertion sequence by the specialized translational elongation factor SELB.
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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.
Ringquist S, Schneider D, Gibson T, Baron C, Böck A, Gold L
Genes & development
1994-02-01 00:00
8
3
376-85
Bacterial Proteins,Base Sequence,Binding Sites,Codon,Escherichia coli,Molecular Sequence Data,Peptide Chain Elongation, Translational,Peptide Chain Initiation, Translational,Peptide Elongation Factors,Protein Binding,Protein Biosynthesis,Proteins,RNA, Messenger,RNA, Transfer, Amino Acid-Specific,RNA, Transfer, Amino Acyl,RNA, Transfer, Met,Ribosomal Proteins,Ribosomes,Selenocysteine,Selenoproteins,Sequence Analysis, RNA,Bacterial Proteins,Codon,Peptide Elongation Factors,Proteins,RNA, Messenger,RNA, Transfer, Amino Acid-Specific,RNA, Transfer, Amino Acyl,RNA, Transfer, Met,Ribosomal Proteins,SelB protein, Bacteria,Selenoproteins,ribosomal protein S30,selenocysteinyl-tRNA,tRNA, selenocysteine-,Selenocysteine
Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder 80309
Genes Dev.
NIGMS GM-19963, NIGMS GM-28685
0890-9369
434
True
8314089
