Genetic Probes to Bacterial Release Factors: tRNA Mimicry Hypothesis and Beyond

Nakamura, Yoshikazu; Kawazu, Yoichi; Uno, Masashi; Yoshimura, Kuniyasu; Ito, Koichi

doi:10.1128/9781555818142.ch42

The Ribosome 2014

DOI: 10.1128/9781555818142.ch42

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Genetic Probes to Bacterial Release Factors: tRNA Mimicry Hypothesis and Beyond

Yoshikazu Nakamura

Yoichi Kawazu

Masashi Uno

et al.

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Cited by 5 publications

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Molecular Mimicry Between Protein and tRNA

Nakamura

2001

Journal of Molecular Evolution

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Mimicry is a sophisticated development in animals, fish, and plants that allows them to fool others by imitating a shape or color for diverse purposes, such as to prey, evade, lure, pollinate, or threaten. This is not restricted to the macro-world, but extends to the micro-world as molecular mimicry. Recent advances in structural and molecular biology uncovered a set of translation factors that resembles a tRNA shape and, in one case, even mimics a tRNA function for deciphering the genetic code. Nature must have evolved this art of molecular mimicry between protein and ribonucleic acid by using different protein structures until the translation factors sat in the cockpit of a ribosome machine, on behalf of tRNA, and achieved diverse actions. Structural, functional, and evolutionary aspects of molecular mimicry will be discussed.

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Molecular Mimicry Between Protein and tRNA

Nakamura

2001

Journal of Molecular Evolution

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Class-1 Translation Termination Factors Are Functional Analogs of Aminoacyl-tRNAs

Kisselev

2003

Molecular Biology

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Class-1 translation termination factors: invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition

Seit-Nebi

Frolova²,

Justesen³

et al. 2001

Nucleic Acids Research

142

125

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Previously, we have shown that all class-1 polypeptide release factors (RFs) share a common glycine-glycine-glutamine (GGQ) motif, which is critical for RF activity. Here, we subjected to site-directed mutagenesis two invariant amino acids, Gln185 and Arg189, situated in the GGQ minidomain of human eRF1, followed by determination of RF activity and the ribosome binding capacity for mutant eRF1. We show that replacement of Gln185 with polar amino acid residues causes partial inactivation of RF activity; Gln185Ile, Arg189Ala and Arg189Gln mutants are completely inactive; all mutants that retain partial RF activity respond similarly to three stop codons. We suggest that loss of RF activity for Gln185 and Arg189 mutants is caused by distortion of the conformation of the GGQ minidomain but not by damage of the stop codon recognition site of eRF1. Our data are inconsistent with the model postulating direct involvement of Gln185 side chain in orientation of water molecule toward peptidyl-tRNA ester bond at the ribosomal peptidyl transferase centre. Most of the Gln185 mutants exhibit reduced ability to bind to the ribosome, probably, to rRNA and/or (peptidyl)-tRNA(s). The data suggest that the GGQ motif is implicated both in promoting peptidyl-tRNA hydrolysis and binding to the ribosome.

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Genetic Probes to Bacterial Release Factors: tRNA Mimicry Hypothesis and Beyond

Cited by 5 publications

References 45 publications

Molecular Mimicry Between Protein and tRNA

Molecular Mimicry Between Protein and tRNA

Class-1 Translation Termination Factors Are Functional Analogs of Aminoacyl-tRNAs

Class-1 translation termination factors: invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition

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