ArticleRNA (New York, N.Y.)2007
The C-terminal domain of T4 RNA ligase 1 confers specificity for tRNA repair.
Article in RNA (New York, N.Y.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Systematic mapping of bacteriophage gene essentiality with HIDEN-SEQ.Nature microbiology · 2026Article
- Biochemical and structural insights into a 5' to 3' RNA ligase reveal a potential role in tRNA ligation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Kinetic and structural insights into the requirement of fungal tRNA ligase for a 2'-phosphate end.RNA (New York, N.Y.) · 2024Article
- Two Novel Bacteriophage Species Against Hybrid Intestinal PathogenicPHAGE (New Rochelle, N.Y.) · 2024Article
- Characterisation and engineering of a thermophilic RNA ligase from Palaeococcus pacificus.Nucleic acids research · 2024Article
- Genetic and Functional Analyses of Archaeal ATP-Dependent RNA Ligase in C/D Box sRNA Circularization and Ribosomal RNA Processing.Frontiers in molecular biosciences · 2022Article
- Structure and two-metal mechanism of fungal tRNA ligase.Nucleic acids research · 2019Article
- Two-metal versus one-metal mechanisms of lysine adenylylation by ATP-dependent and NADProceedings of the National Academy of Sciences of the United States of America · 2017Article
- RNA damage in biological conflicts and the diversity of responding RNA repair systems.Nucleic acids research · 2016Review
- Structural and mutational analysis of archaeal ATP-dependent RNA ligase identifies amino acids required for RNA binding and catalysis.Nucleic acids research · 2016Article
- Structure and two-metal mechanism of a eukaryal nick-sealing RNA ligase.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Characterization of a novel eukaryal nick-sealing RNA ligase from Naegleria gruberi.RNA (New York, N.Y.) · 2015Article
- Effects of 3'-OH and 5'-PO4 base mispairs and damaged base lesions on the fidelity of nick sealing by Deinococcus radiodurans RNA ligase.Journal of bacteriology · 2014Article
- Kinetic mechanism of nick sealing by T4 RNA ligase 2 and effects of 3'-OH base mispairs and damaged base lesions.RNA (New York, N.Y.) · 2013Article
- The structure of the C-terminal domain of the largest editosome interaction protein and its role in promoting RNA binding by RNA-editing ligase L2.Nucleic acids research · 2012Article
- The adenylyltransferase domain of bacterial Pnkp defines a unique RNA ligase family.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- DNA ligases: progress and prospects.The Journal of biological chemistry · 2009Review
- Archaeal RNA ligase is a homodimeric protein that catalyzes intramolecular ligation of single-stranded RNA and DNA.Nucleic acids research · 2008Article
- The structure of an archaeal homodimeric ligase which has RNA circularization activity.Protein science : a publication of the Protein Society · 2008Article
- RNA repair: an antidote to cytotoxic eukaryal RNA damage.Molecular cell · 2008Article
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4 authors.
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Abstract
T4 RNA ligase 1 (Rnl1) is a tRNA repair enzyme that thwarts a tRNA-damaging host response to virus infection. The 374-aa Rnl1 protein consists of an N-terminal nucleotidyltransferase domain fused to a unique C-terminal domain composed of 10 alpha helices. We exploited an in vitro tRNA splicing system to demonstrate that Rnl1 has an inherent specificity for sealing tRNA with a break in the anticodon loop. The tRNA specificity is imparted by the C domain, any deletion of which caused the broken tRNA to be sealed as poorly as the linear intron in vitro and also abolished Rnl1 tRNA splicing activity in vivo. Deletion analysis demarcated Rnl1-(1-254) as a minimal catalytic domain of Rnl1, capable of all chemical steps of the nonspecific RNA ligation reaction. Alanine scanning of the N domain identified Ser103, Leu104, Lys117, and Ser118 as important for pRNA ligation in vitro and tRNA repair in vivo.
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