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Decoding with the A:I wobble pair is inefficient

J F Curran1

  • 1Department of Biology, Wake Forest University, Winston-Salem, NC 27109.

Nucleic Acids Research
|February 25, 1995
PubMed
Summary
This summary is machine-generated.

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Transfer RNAs (tRNAs) with inosine at the first position can read codons ending in A, but this is inefficient. In Escherichia coli, the codon CGA is rarely used due to slow and unstable tRNA binding, impacting protein synthesis.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Transfer RNAs (tRNAs) with inosine (I) in the first position of the anticodon can recognize codons ending in U, C, or A.
  • Despite this capability, codons ending in A are infrequently utilized in many organisms, including Escherichia coli.

Purpose of the Study:

  • To investigate the inefficiency of translation for the CGA codon in Escherichia coli.
  • To determine the underlying molecular mechanisms responsible for the rare usage of codons read by the inosine-containing tRNAICGArg.

Main Methods:

  • Utilized three independent in vivo assays to assess translation efficiency.
  • Assayed rho-mediated polar effects on a lacZ reporter gene with tandem CGA codons.
  • Substituted codons in the RF2 frameshift regulatory element and assessed amber suppression efficiency.

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Main Results:

  • Translation of the CGA codon was found to be inefficient in Escherichia coli.
  • Tandem CGA codons induced a strong rho-mediated polar effect, exacerbated by a mutation in ribosomal protein S12 (rpsL).
  • Codon substitution assays confirmed slow and/or unstable aminoacyl-tRNA (aa-tRNA) selection at CGA, and poor 5' context for amber suppression.

Conclusions:

  • The adenosine:inosine (A:I) base pair formed during CGA codon recognition destabilizes codon:anticodon complexes.
  • This destabilization occurs over two successive ribosomal cycles, leading to inefficient translation.
  • The inherent instability of the A:I pair likely contributes to the rare usage of codons read by tRNA with inosine at the first position.