RtcB is the RNA ligase component of an Escherichia coli RNA repair operon Journal Article
| Authors: | Tanaka, N.; Shuman, S. |
| Article Title: | RtcB is the RNA ligase component of an Escherichia coli RNA repair operon |
| Abstract: | RNA 2′,3′-cyclic phosphate ends play important roles in RNA metabolism as substrates for RNA ligases during tRNA restriction-repair and tRNA splicing. Diverse bacteria from multiple phyla encode a two-component RNA repair cassette, comprising Pnkp (polynucleotide kinase-phosphatase-ligase) and Hen1 (RNA 3′-terminal ribose 2′-O-methyltransferase), that heals and then seals broken tRNAs with 2′,3′-cyclic phosphate and 5′-OH ends. The Pnkp-Hen1 repair operon is absent in the majority of bacterial species, thereby raising the prospect that other RNA repair systems might be extant. A candidate component is RNA 3′-phosphate cyclase, a widely distributed enzyme that transforms RNA 3′-monophosphate termini into 2′,3′-cyclic phosphates but cannot seal the ends it produces. Escherichia coli RNA cyclase (RtcA) is encoded in a σ54- regulated operon with RtcB, a protein of unknown function. Taking a cue from Pnkp-Hen1, we purified E. coli RtcB and tested it for RNA ligase activity. We report that RtcB per se seals broken tRNA-like stem-loop structures with 2′,3′-cyclic phosphate and 5′-OH ends to form a splice junction with a 2′-OH, 3′,5′-phosphodiester. We speculate that: (i) RtcB might afford bacteria a means to recover from stress-induced RNA damage; and (ii) RtcB homologs might catalyze tRNA repair or splicing reactions in archaea and eukarya. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc. |
| Keywords: | unclassified drug; sequence analysis; nonhuman; protein domain; protein function; genetic transcription; enzyme activity; enzyme substrate; rna; bacterial protein; e. coli; escherichia coli; nucleic acids; crystal structure; catalysis; rna structure; sequence homology; transfer rna; rna, transfer; enzyme specificity; enzymes; rna metabolism; polynucleotide 5' hydroxyl kinase; archaebacterium; rna ligase (atp); archaea; eukaryote; rna cleavage; transesterification; repair; rna splicing; escherichia coli proteins; rna, bacterial; ligases; ligase activity; rna repair; operon; bacteriology; bacterial rna; rna 3' phosphate cyclase; cyclases; cyclic phosphates; monophosphates; phosphodiesters; polynucleotides; rna ligase; bacterial species; eukarya; o-methyltransferase; repair system; rna metabolisms; splice junctions; splicing reactions; stem-loop structures; stress-induced; two-component; microorganism protein; protein rtcb; rna 3' terminal ribose 2' o methyltransferase; genetic organization; rna 3' end processing |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 286 |
| Issue: | 10 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 2011-03-11 |
| Start Page: | 7727 |
| End Page: | 7731 |
| Language: | English |
| DOI: | 10.1074/jbc.C111.219022 |
| PUBMED: | 21224389 |
| PROVIDER: | scopus |
| PMCID: | PMC3048659 |
| DOI/URL: | |
| Notes: | --- - "Export Date: 23 June 2011" - "CODEN: JBCHA" - "Source: Scopus" |
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