RtcB, a novel RNA ligase, can catalyze tRNA splicing and HAC1 mRNA splicing in vivo Journal Article
| Authors: | Tanaka, N.; Meineke, B.; Shuman, S. |
| Article Title: | RtcB, a novel RNA ligase, can catalyze tRNA splicing and HAC1 mRNA splicing in vivo |
| Abstract: | RtcB enzymes are novel RNA ligases that join 2′,3′-cyclic phosphate and 5′-OH ends. The phylogenetic distribution of RtcB points to its candidacy as a tRNA splicing/repair enzyme. Here we show that Escherichia coli RtcB is competent and sufficient for tRNA splicing in vivo by virtue of its ability to complement growth of yeast cells that lack the endogenous "healing/sealing-type" tRNA ligase Trl1. RtcB also protects yeast trl1Δ cells against a fungal ribotoxin that incises the anticodon loop of cellular tRNAs. Moreover, RtcB can replace Trl1 as the catalyst of HAC1 mRNA splicing during the unfolded protein response. Thus, RtcB is a bona fide RNA repair enzyme with broad physiological actions. Biochemical analysis of RtcB highlights the uniqueness of its active site and catalytic mechanism. Our findings draw attention to tRNA ligase as a promising drug target. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc. |
| Keywords: | unclassified drug; nonhuman; dna repair; introns; in vivo study; rna; molecular sequence data; messenger rna; saccharomyces cerevisiae; escherichia coli; base sequence; in-vivo; yeast; saccharomyces cerevisiae proteins; catalysis; nucleic acid conformation; transfer rna; rna, transfer; basic-leucine zipper transcription factors; catalytic domain; repressor proteins; catalyst; enzymes; yeast cell; rna ligase (atp); fungus growth; anticodon; rna splicing; escherichia coli proteins; fungal gene; ligases; unfolded protein response; catalysts; active site; cyclic phosphates; rna ligase; protein rtcb; drug targets; anticodon loop; biochemical analysis; catalytic mechanisms; phylogenetic distribution; repair enzymes; protein trl1; hac1 gene; amino acyl-trna synthetases |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 286 |
| Issue: | 35 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 2011-09-02 |
| Start Page: | 30253 |
| End Page: | 30257 |
| Language: | English |
| DOI: | 10.1074/jbc.C111.274597 |
| PROVIDER: | scopus |
| PMCID: | PMC3162383 |
| PUBMED: | 21757685 |
| DOI/URL: | |
| Notes: | --- - "Export Date: 3 October 2011" - "CODEN: JBCHA" - "Source: Scopus" |
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