An RNA ligase from Deinococcus radiodurans Journal Article
| Authors: | Martins, A.; Shuman, S. |
| Article Title: | An RNA ligase from Deinococcus radiodurans |
| Abstract: | Although DNA repair pathways have been the focus of much attention, there is an emerging appreciation that distinct pathways exist to maintain or manipulate RNA structure in response to breakage events. Here we identify an RNA ligase (DraRnl) from the radiation-resistant bacterium Deinococcus radiodurans. DraRnl seals 3′-OH/5′-PO4 RNA nicks in either a duplex RNA or an RNA: DNA hybrid, but it cannot seal 3′-OH/5′-PO 4 DNA nicks. The specificity of DraRnl arises from a requirement for RNA on the 3′-OH side of the nick. DraRnl is a 342-amino acid monomeric protein with a distinctive structure composed of a C-terminal adenylyltransferase domain linked to an N-terminal module that resembles the OB-fold of phenylalanyl-tRNA synthetases. RNA sealing activity was abolished by mutation of the predicted lysine adenylylation site (Lys-165) in the C-terminal domain and was reduced by an order of magnitude by deletion of the N-terminal OB module. Our findings highlight the existence of an RNA repair capacity in bacteria and support the hypothesis that contemporary DNA ligases, RNA ligases, and RNA capping enzymes evolved by the fusion of ancillary effector domains to an ancestral catalytic module involved in RNA repair. |
| Keywords: | mutation; nonhuman; protein domain; proteins; dna repair; carboxy terminal sequence; dose-response relationship, drug; enzyme activity; bacteria (microorganisms); rna; dna; amino acid sequence; molecular sequence data; sequence homology, amino acid; amino terminal sequence; recombinant proteins; alternative splicing; radiosensitivity; base sequence; protein structure, tertiary; catalysis; amino acids; protein folding; rna structure; enzyme specificity; enzyme substrate complex; centrifugation, density gradient; rna metabolism; lysine; rna ligase (atp); hydrogen-ion concentration; amino acid motifs; electrophoresis, polyacrylamide gel; enzyme conformation; rna repair; bacteria; glycerol; deinococcus radiodurans; deinococcus; bacterial rna; rna ligase; monomers; catalytic modules; cations; phocidae; priority journal; article; dna liganase; radiation-resistant bacterium |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 279 |
| Issue: | 49 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 2004-12-03 |
| Start Page: | 50654 |
| End Page: | 50661 |
| Language: | English |
| DOI: | 10.1074/jbc.M407657200 |
| PROVIDER: | scopus |
| PUBMED: | 15333634 |
| DOI/URL: | |
| Notes: | J. Biol. Chem. -- Cited By (since 1996):25 -- Export Date: 16 June 2014 -- CODEN: JBCHA -- Source: Scopus |
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