ReviewBiochimica et biophysica acta2008
Determinants of substrate specificity in RNA-dependent nucleotidyl transferases.
Review in Biochimica et biophysica acta, 2008. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed.
- Article
- Protein-primed DNA homopolymer synthesis by an antiviral reverse transcriptase.bioRxiv : the preprint server for biology · 2025Article
- TRAMP assembly alters the conformation and RNA binding of Mtr4 and Trf4-Air2.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Birth of a poly(A) tail: mechanisms and control of mRNA polyadenylation.FEBS open bio · 2023Review
- Proteomic Analysis Reveals Differential Protein Expression Induced by Inhibition of Prolyl Oligopeptidase in Filarial Parasites.The protein journal · 2022Article
- Functions and mechanisms of RNA tailing by metazoan terminal nucleotidyltransferases.Wiley interdisciplinary reviews. RNA · 2021Review
- Polyadenylation and nuclear export of mRNAs.The Journal of biological chemistry · 2019Review
- Terminal nucleotidyl transferases (TENTs) in mammalian RNA metabolism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- The role of sequence context, nucleotide pool balance and stress in 2'-deoxynucleotide misincorporation in viral, bacterial and mammalian RNA.Nucleic acids research · 2016Article
- Uridylation of RNA Hairpins by Tailor Confines the Emergence of MicroRNAs in Drosophila.Molecular cell · 2015Article
- Structural basis for the activation of the C. elegans noncanonical cytoplasmic poly(A)-polymerase GLD-2 by GLD-3.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Characterization of Three Mycobacterium spp. with Potential Use in Bioremediation by Genome Sequencing and Comparative Genomics.Genome biology and evolution · 2015Article
- Crystal structure of human poly(A) polymerase gamma reveals a conserved catalytic core for canonical poly(A) polymerases.Journal of molecular biology · 2014Article
- The nucleic acid-binding domain and translational repression activity of a Xenopus terminal uridylyl transferase.The Journal of biological chemistry · 2013Article
- The novel poly(A) polymerase Star-PAP is a signal-regulated switch at the 3'-end of mRNAs.Advances in biological regulation · 2013Review
- Structure and function of the polymerase core of TRAMP, a RNA surveillance complex.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- tRNA nucleotidyltransferases: ancient catalysts with an unusual mechanism of polymerization.Cellular and molecular life sciences : CMLS · 2010Review
- Chain termination and inhibition of mammalian poly(A) polymerase by modified ATP analogues.Biochemical pharmacology · 2010Article
- On the role of a conserved, potentially helix-breaking residue in the tRNA-binding alpha-helix of archaeal CCA-adding enzymes.RNA (New York, N.Y.) · 2008Article
- Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Poly(A) polymerases were identified almost 50 years ago as enzymes that add multiple AMP residues to the 3' ends of primer RNAs without use of a template from ATP as cosubstrate and with release of pyrophosphate. Based on sequence homology of a signature motif in the catalytic domain, poly(A) polymerases were later found to belong to a superfamily of nucleotidyl transferases acting on a very diverse array of substrates. Enzymes belonging to the superfamily can add from single nucleotides of AMP, CMP or UMP to RNA, antibiotics and proteins but also homopolymers of many hundred residues to the 3' ends of RNA molecules. The recently reported structures of several nucleotidyl transferases facilitate the study of the catalytic mechanisms of these very diverse enzymes. Numerous structures of CCA-adding enzymes have now revealed all steps in the formation of a CCA tail at the 3' end of tRNAs. In addition, structures of poly(A) polymerases and uridylyl transferases are now available as binary and ternary complexes with incoming nucleotide and RNA primer. Some of these proteins undergo significant conformational changes after substrate binding. This is proposed to be an indication for an induced fit mechanism that drives substrate selection and leads to catalysis. Insights from recent structures of ternary complexes indicate an important role for the primer molecule in selecting the incoming nucleotide.
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Registered trials
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