ArticleProceedings of the National Academy of Sciences of the United States of America2012
Molecular basis of bacterial protein Hen1 activating the ligase activity of bacterial protein Pnkp for RNA repair.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 20 citations in OpenAlex.
- HENMT1: an RNA methyltransferase in biology and disease.Journal of Zhejiang University. Science. B · 2026Review
- CRAFT: a web-integrated cavity prediction tool based on flow transfer algorithm.Journal of cheminformatics · 2024Article
- 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
- Structures of ATP-bound DNA ligase D in a closed domain conformation reveal a network of amino acid and metal contacts to the ATP phosphates.The Journal of biological chemistry · 2019Article
- 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
- Characterization of Runella slithyformis HD-Pnk, a Bifunctional DNA/RNA End-Healing Enzyme Composed of an N-Terminal 2',3'-Phosphoesterase HD Domain and a C-Terminal 5'-OH Polynucleotide Kinase Domain.Journal of bacteriology · 2017Article
- 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
- Reconstitution and structure of a bacterial Pnkp1-Rnl-Hen1 RNA repair complex.Nature communications · 2015Article
- Structures of bacterial polynucleotide kinase in a michaelis complex with nucleoside triphosphate (NTP)-Mg2+ and 5'-OH RNA and a mixed substrate-product complex with NTP-Mg2+ and a 5'-phosphorylated oligonucleotide.Journal of bacteriology · 2014Article
- Article
- Structural and biochemical analysis of the phosphate donor specificity of the polynucleotide kinase component of the bacterial pnkp•hen1 RNA repair system.Biochemistry · 2013Article
- Structure and mechanism of the 2',3' phosphatase component of the bacterial Pnkp-Hen1 RNA repair system.Nucleic acids research · 2013Article
- Structure and mechanism of the polynucleotide kinase component of the bacterial Pnkp-Hen1 RNA repair system.RNA (New York, N.Y.) · 2012Article
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6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Ribotoxins cleave essential RNAs for cell killing in vivo, and the bacterial polynucleotide kinase-phosphatase (Pnkp)/hua enhancer 1 (Hen1) complex has been shown to repair ribotoxin-cleaved RNAs in vitro. Bacterial Pnkp/Hen1 is distinguished from other RNA repair systems by performing 3'-terminal 2'-O-methylation during RNA repair, which prevents the repaired RNA from repeated cleavage at the same site. To ensure the opportunity of 2'-O-methylation by bacterial Hen1 during RNA repair and, therefore, maintain the quality of the repaired RNA, Pnkp/Hen1 has evolved to require the participation of Hen1 in RNA ligation, because Pnkp alone is unable to carry out the reaction despite possessing all signature motifs of an RNA ligase. However, the precise role of Hen1 in RNA ligation is unknown. Here, we present the crystal structure of an active RNA ligase consisting of the C-terminal half of Pnkp (Pnkp-C) and the N-terminal half of Hen1 (Hen1-N) from Clostridium thermocellum. The structure reveals that the N-terminal domain of Clostridium thermocellum (Cth) Hen1, shaped like a left hand, grabs the flexible insertion module of CthPnkp and locks its conformation via further interaction with the C-terminal addition module of CthPnkp. Formation of the CthPnkp-C/Hen1-N heterodimer creates a ligation pocket with a width for two strands of RNA, depth for two nucleotides, and the adenosine monophosphate (AMP)-binding pocket at the bottom. The structure, combined with functional analyses, provides insight into the mechanism of how Hen1 activates the RNA ligase activity of Pnkp for RNA repair.
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