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• W2108791410 abstract "Mycoplasma genitalium is expected to metabolize RNA using unique pathways because its minimal genome encodes very few ribonucleases. In this work, we report that the only exoribonuclease identified in M. genitalium, RNase R, is able to remove tRNA 3′-trailers and generate mature 3′-ends. Several sequence and structural features of a tRNA precursor determine its precise processing at the 3′-end by RNase R in a purified system. The aminoacyl-acceptor stem plays a major role in stopping RNase R digestion at the mature 3′-end. Disruption of the stem causes partial or complete degradation of the pre-tRNA by RNase R, whereas extension of the stem results in the formation of a product terminating downstream at the new mature 3′-end. In addition, the 3′-terminal CCA sequence and the discriminator residue influence the ability of RNase R to stop at the mature 3′-end. RNase R-mediated generation of the mature 3′-end prefers a sequence of RCCN at the 3′ terminus of tRNA. Variations of this sequence may cause RNase R to trim further and remove terminal CA residues from the mature 3′-end. Therefore, M. genitalium RNase R can precisely remove the 3′-trailer of a tRNA precursor by recognizing features in the terminal domains of tRNA, a process requiring multiple RNases in most bacteria.Background: Mycoplasma genitalium lacks known ribonucleases for tRNA 3′-processing. The only identified exoribonuclease, RNase R, can carry out this function.Results: RNase R processes the tRNA 3′-end depending on the acceptor stem, discriminator, and CCA terminus.Conclusion: RNase R can process tRNA by recognizing features within the tRNA.Significance: M. genitalium may process tRNA 3′-end employing a unique single-step exonucleolytic pathway. Mycoplasma genitalium is expected to metabolize RNA using unique pathways because its minimal genome encodes very few ribonucleases. In this work, we report that the only exoribonuclease identified in M. genitalium, RNase R, is able to remove tRNA 3′-trailers and generate mature 3′-ends. Several sequence and structural features of a tRNA precursor determine its precise processing at the 3′-end by RNase R in a purified system. The aminoacyl-acceptor stem plays a major role in stopping RNase R digestion at the mature 3′-end. Disruption of the stem causes partial or complete degradation of the pre-tRNA by RNase R, whereas extension of the stem results in the formation of a product terminating downstream at the new mature 3′-end. In addition, the 3′-terminal CCA sequence and the discriminator residue influence the ability of RNase R to stop at the mature 3′-end. RNase R-mediated generation of the mature 3′-end prefers a sequence of RCCN at the 3′ terminus of tRNA. Variations of this sequence may cause RNase R to trim further and remove terminal CA residues from the mature 3′-end. Therefore, M. genitalium RNase R can precisely remove the 3′-trailer of a tRNA precursor by recognizing features in the terminal domains of tRNA, a process requiring multiple RNases in most bacteria. Background: Mycoplasma genitalium lacks known ribonucleases for tRNA 3′-processing. The only identified exoribonuclease, RNase R, can carry out this function. Results: RNase R processes the tRNA 3′-end depending on the acceptor stem, discriminator, and CCA terminus. Conclusion: RNase R can process tRNA by recognizing features within the tRNA. Significance: M. genitalium may process tRNA 3′-end employing a unique single-step exonucleolytic pathway." @default.
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• W2108791410 date "2012-07-01" @default.
• W2108791410 modified "2023-10-07" @default.
• W2108791410 title "Novel One-step Mechanism for tRNA 3′-End Maturation by the Exoribonuclease RNase R of Mycoplasma genitalium" @default.
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• W2108791410 doi "https://doi.org/10.1074/jbc.m111.324970" @default.
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