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• W2108177890 startingPage "1957" @default.
• W2108177890 abstract "Mycoplasma genitalium , a small bacterium having minimal genome size, has only one identified exoribonuclease, RNase R (MgR). We have purified MgR to homogeneity, and compared its RNA degradative properties to those of its Escherichia coli homologs RNase R (EcR) and RNase II (EcII). MgR is active on a number of substrates including oligoribonucleotides, poly(A), rRNA, and precursors to tRNA. Unlike EcR, which degrades rRNA and pre-tRNA without formation of intermediate products, MgR appears sensitive to certain RNA structural features and forms specific products from these stable RNA substrates. The 3′-ends of two MgR degradation products of 23S rRNA were mapped by RT-PCR to positions 2499 and 2553, each being 1 nucleotide downstream of a 2′- O -methylation site. The sensitivity of MgR to ribose methylation is further demonstrated by the degradation patterns of 16S rRNA and a synthetic methylated oligoribonucleotide. Remarkably, MgR removes the 3′-trailer sequence from a pre-tRNA, generating product with the mature 3′-end more efficiently than EcII does. In contrast, EcR degrades this pre-tRNA without the formation of specific products. Our results suggest that MgR shares some properties of both EcR and EcII and can carry out a broad range of RNA processing and degradative functions." @default.
• W2108177890 created "2016-06-24" @default.
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• W2108177890 date "2007-09-13" @default.
• W2108177890 modified "2023-10-07" @default.
• W2108177890 title "Exoribonuclease R in <i>Mycoplasma genitalium</i> can carry out both RNA processing and degradative functions and is sensitive to RNA ribose methylation" @default.
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• W2108177890 doi "https://doi.org/10.1261/rna.706207" @default.
• W2108177890 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2040080" @default.
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