| Autor: |
Lalonde MS; Department of Biomedical Science, Florida Atlantic University, Boca Raton, FL 33431, USA., Zuo Y, Zhang J, Gong X, Wu S, Malhotra A, Li Z |
| Jazyk: |
angličtina |
| Zdroj: |
RNA (New York, N.Y.) [RNA] 2007 Nov; Vol. 13 (11), pp. 1957-68. Date of Electronic Publication: 2007 Sep 13. |
| DOI: |
10.1261/rna.706207 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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