Bacteriophage T4 RNA ligase 2 (gp24.1) exemplifies a family of RNA ligases found in all phylogenetic domains Journal Article
| Authors: | Ho, C. K.; Shuman, S. |
| Article Title: | Bacteriophage T4 RNA ligase 2 (gp24.1) exemplifies a family of RNA ligases found in all phylogenetic domains |
| Abstract: | RNA ligases participate in repair, splicing, and editing pathways that either reseal broken RNAs or alter their primary structure. Bacteriophage T4 RNA ligase (gp63) is the best-studied member of this class of enzymes, which includes yeast tRNA ligase and trypanosome RNA-editing ligases. Here, we identified another RNA ligase from the bacterial domain-a second RNA ligase (Rnl2) encoded by phage T4. Purified Rnl2 (gp24.1) catalyzes intramolecular and intermolecular RNA strand joining through ligase-adenylate and RNA-adenylate intermediates. Mutational analysis identifies amino acids required for the ligase-adenylation or phosphodiester synthesis steps of the ligation reaction. The catalytic residues of Rnl2 are located within nucleotidyl transferase motifs I, IV, and V that are conserved in DNA ligases and RNA capping enzymes. Rnl2 has scant amino acid similarity to T4 gp63. Rather, Rnl2 exemplifies a distinct ligase family, defined by variant motifs, that includes the trypanosome-editing ligases and a group of putative RNA ligases encoded by eukaryotic viruses (baculoviruses and an entomopoxvirus) and many species of archaea. These findings have implications for the evolution of covalent nucleotidyl transferases and virus-host dynamics based on RNA restriction and repair. |
| Keywords: | controlled study; unclassified drug; mutation; nonhuman; protein domain; protein motif; dna repair; molecular dynamics; dose-response relationship, drug; enzyme activity; mutational analysis; bacteria (microorganisms); dna; molecular evolution; amino acid sequence; molecular sequence data; eukaryota; recombinant proteins; species difference; protein structure, tertiary; catalysis; adenosine triphosphate; protein family; polydeoxyribonucleotide synthase; catalytic domain; synthesis; rna ligase (atp); archaea; hydrogen-ion concentration; imidazoles; amino acid motifs; viral proteins; phylogeny; adenosine phosphate; adenylation; nucleotidyltransferase; ester derivative; rna capping; rna ligase; rna purification; polynucleotide ligases; bacteriophage t4; amino acid derivative; rna ligase 2; priority journal; article; unidentified bacteriophage; polynucleotide adenylyltransferase; unidentified entomopoxvirus |
| Journal Title: | Proceedings of the National Academy of Sciences of the United States of America |
| Volume: | 99 |
| Issue: | 20 |
| ISSN: | 0027-8424 |
| Publisher: | National Academy of Sciences |
| Date Published: | 2002-10-01 |
| Start Page: | 12709 |
| End Page: | 12714 |
| Language: | English |
| DOI: | 10.1073/pnas.192184699 |
| PUBMED: | 12228725 |
| PROVIDER: | scopus |
| PMCID: | PMC130525 |
| DOI/URL: | |
| Notes: | Export Date: 14 November 2014 -- Source: Scopus |
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