Mimicry grasps reality in translation termination

Article Abstract:

Mimicry and translation termination are discussed in this minireview article. Termination of protein synthesis takes place on the ribosomes as a response to a stop, rather than a sense codon in the decoding site. Mechanisms of stop codon recognition and translation termination by release factors (RFs) from the perspective of molecular mimicry between translation factors and tRNA. Polypeptide release factors are essential in the termination of protein synthesis on ribosomes as a response to a stop codon. Remarkably, four decades elapsed between discovery of the genetic code and figuring out basic mechanisms behind deciphering the 64 codons.

Japan, Research, Genetic aspects, Cytochemistry, Mimicry (Biology), Molecular genetics

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Peptidyl-tRNA regulates the GTPase activity of translation factors

Article Abstract:

Research demonstrates the mechanism involved in controlling the binding and GTPase activity of translation factors by the position of peptidyl-tRNA in the ribosome. Data indicate that hybrid sites for tRNA on the ribosomes mediate translocation of tRNAs, recycling of class 1 release factors, and recycling of ribosomes.

Protein biosynthesis, G proteins, Enzyme regulation

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A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3

Article Abstract:

Research shows that the peptide release factor RF3, involved in the translation termination, is bound to GDP, whereas RF1 or RF2 complexed with ribosome function as guanine nucleotide exchange factors. Data indicate that peptidyl-tRNA hydrolysis by RF1 or RF2 leads to GTP binding to RF3 on the ribosome.

France, Proteins, Ribosomes, Peptide regulatory factors

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