Constructing ORFeome resources with removable termination codons.

Masayoshi Itoh; Ayako Yasunishi; Kengo Imamura; Mutsumi Kanamori-Katayama; Harukazu Suzuki; Masanori Suzuki; Piero Carninci; Jun Kawai; Yoshihide Hayashizaki

doi:10.2144/000112209

PubMed · 16869512

Constructing ORFeome resources with removable termination codons.

Masayoshi Itoh·Ayako Yasunishi·Kengo Imamura·Mutsumi Kanamori-Katayama·Harukazu Suzuki·Masanori Suzuki·Piero Carninci·Jun Kawai·Yoshihide Hayashizaki

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Codon, Terminator Genetic Techniques Genetic Vectors Models, Genetic Open Reading Frames Plasmids Pyrococcus horikoshii Journal Article Research Support, Non-U.S. Gov't

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Masayoshi Itoh, Ayako Yasunishi, Kengo Imamura, Mutsumi Kanamori-Katayama, Harukazu Suzuki, Masanori Suzuki, Piero Carninci, Jun Kawai, Yoshihide Hayashizaki. 2006. Constructing ORFeome resources with removable termination codons.. https://doi.org/10.2144/000112209

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Certain C-terminal sequences of nascent peptide cause an efficient protein tagging by tmRNA system at stop codons in Escherichia coli. Here, we demonstrate that both mRNA cleavage and tmRNA tagging occur at UAG stop codon recognized specifically by polypeptide release factor 1 (RF-1) when the activity of RF-1 is reduced by a mutation in the prfA gene without requirement of particular C-terminal sequences of nascent peptide. The tmRNA tagging and mRNA cleavage in the prfA mutant were eliminated when the wild-type RF-1 but not RF-2 was supplied from plasmid. In addition, depletion of either RF-1 or RF-2 induces endonucleolytic cleavage and tmRNA tagging at UAG or UGA stop codons respectively. We conclude that ribosome stalling at the cognate stop codon caused by reduced activity or expression of RF-1 or RF-2 is responsible for mRNA cleavage. The present data along with our previous studies strongly suggest that ribosome stalling leads to endonucleolytic cleavage of mRNA in general resulting in non-stop mRNA and that the 3' end of non-stop mRNA is probably only target for the tmRNA system.

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The decapping enzyme Dcp1 participates in translation termination through its interaction with the release factor eRF3 in budding yeast.

One of the rate-limiting steps in messenger RNA decay pathway is the 5'-cap cleavage of mRNAs, decapping reaction, which is conducted by the protein complex of Dcp1 and Dcp2. We find here that Dcp1p can interact with the release factor eRF3p (Sup35p) in Saccharomyces cerevisiae. Knockout of DCP1 caused not only the accumulation of nonsense mRNAs possibly due to the impaired decapping activity but also the enhancement of the read-through of nonsense codon. To examine the relationship between the two DCP1-knockout phenotypes, we produced DCP1 point mutants that lack the ability to support the translation termination. Interestingly, decapping activity of Dcp1p was still intact, but its interaction with eRF3p was abolished in the DCP1 mutants, indicating that the two functions originated from different entities of Dcp1p. These results suggest that the decapping enzyme Dcp1p may have an additional role in the translation termination through its interaction with eRF3p.

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