ArticleProtein science : a publication of the Protein Society2008
The structure of an archaeal homodimeric ligase which has RNA circularization activity.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 33 citations in OpenAlex.
- Article
- Circular RNAs in Archaea.Advances in experimental medicine and biology · 2025Review
- Characterisation and engineering of a thermophilic RNA ligase from Palaeococcus pacificus.Nucleic acids research · 2024Article
- Direct adenylation from 5'-OH-terminated oligonucleotides by a fusion enzyme containing Pfu RNA ligase and T4 polynucleotide kinase.Nucleic acids research · 2022Article
- 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
- Caveat mutator: alanine substitutions for conserved amino acids in RNA ligase elicit unexpected rearrangements of the active site for lysine adenylylation.Nucleic acids research · 2020Article
- Structure and two-metal mechanism of fungal tRNA ligase.Nucleic acids research · 2019Article
- Biotechnology of extremely thermophilic archaea.FEMS microbiology reviews · 2018Review
- High-throughput sequencing reveals circular substrates for an archaeal RNA ligase.RNA biology · 2017Article
- 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
- Archaeal RNA ligase from thermoccocus kodakarensis for template dependent ligation.RNA biology · 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
- Three-dimensional structure model and predicted ATP interaction rewiring of a deviant RNA ligase 2.BMC structural biology · 2015Article
- Characterization of a novel eukaryal nick-sealing RNA ligase from Naegleria gruberi.RNA (New York, N.Y.) · 2015Article
- RNA circularization strategies in vivo and in vitro.Nucleic acids research · 2015Review
- Archaeal Nucleic Acid Ligases and Their Potential in Biotechnology.Archaea (Vancouver, B.C.) · 2015Review
- 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
- Structure-function analysis of Methanobacterium thermoautotrophicum RNA ligase - engineering a thermostable ATP independent enzyme.BMC molecular biology · 2012Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The genome of Pyrococcus abyssi contains two open reading frames encoding proteins which had been previously predicted to be DNA ligases, Pab2002 and Pab1020. We show that while the former is indeed a DNA ligase, Pab1020 had no effect on the substrate deoxyoligo-ribonucleotides tested. Instead, Pab1020 catalyzes the nucleotidylation of oligo-ribonucleotides in an ATP-dependent reaction, suggesting that it is an RNA ligase. We have solved the structure of Pab1020 in complex with the ATP analog AMPPNP by single-wavelength anomalous dispersion (SAD), elucidating a structure with high structural similarity to the catalytic domains of two RNA ligases from the bacteriophage T4. Additional carboxy-terminal domains are also present, and one of these mediates contacts with a second protomer, which is related by noncrystallographic symmetry, generating a homodimeric structure. These C-terminal domains are terminated by short domain swaps which themselves end within 5 A of the active sites of the partner molecules. Additionally, we show that the protein is indeed capable of circularizing RNA molecules in an ATP-dependent reaction. These structural and biochemical results provide an insight into the potential physiological roles of Pab1020.
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