ArticleThe Journal of biological chemistry2013
The nucleic acid-binding domain and translational repression activity of a Xenopus terminal uridylyl transferase.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Review
- Decoding RNA-Protein Interactions: Methodological Advances and Emerging Challenges.Advanced genetics (Hoboken, N.J.) · 2025Review
- Structural insights into a unique preference for 3' terminal guanine of mirtron in Drosophila TUTase tailor.Nucleic acids research · 2019Article
- The role of 3' end uridylation in RNA metabolism and cellular physiology.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- RNA uridylation and decay in plants.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Global pairwise RNA interaction landscapes reveal core features of protein recognition.Nature communications · 2018Article
- Nucleotide specificity of the human terminal nucleotidyltransferase Gld2 (TUT2).RNA (New York, N.Y.) · 2016Article
- Hormonal stimulation of starfish oocytes induces partial degradation of the 3' termini of cyclin B mRNAs with oligo(U) tails, followed by poly(A) elongation.RNA (New York, N.Y.) · 2016Article
- The new (dis)order in RNA regulation.Cell communication and signaling : CCS · 2016Review
- Protein-RNA networks revealed through covalent RNA marks.Nature methods · 2015Article
- Structural plasticity of Cid1 provides a basis for its distributive RNA terminal uridylyl transferase activity.Nucleic acids research · 2015Article
- Improved crystallization and diffraction of caffeine-induced death suppressor protein 1 (Cid1).Acta crystallographica. Section F, Structural biology communications · 2015Article
- Article
- A critical switch in the enzymatic properties of the Cid1 protein deciphered from its product-bound crystal structure.Nucleic acids research · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Terminal uridylyl transferases (TUTs) catalyze the addition of uridines to the 3' ends of RNAs and are implicated in the regulation of both messenger RNAs and microRNAs. To better understand how TUTs add uridines to RNAs, we focused on a putative TUT from Xenopus laevis, XTUT7. We determined that XTUT7 catalyzed the addition of uridines to RNAs. Mutational analysis revealed that a truncated XTUT7 enzyme, which contained solely the nucleotidyl transferase and poly(A) polymerase-associated domains, was sufficient for catalytic activity. XTUT7 activity decreased upon removal of the CCHC zinc finger domains and a short segment of basic amino acids (the basic region). This basic region bound nucleic acids in vitro. We also demonstrated that XTUT7 repressed translation of a polyadenylated RNA, to which it added a distinct number of uridines. We generated a predicted structure of the XTUT7 catalytic core that indicated histidine 1269 was likely important for uridine specificity. Indeed, mutation of histidine 1269 broadened the nucleotide specificity of XTUT7 and abolished XTUT7-dependent translational repression. Our data reveal key aspects of how XTUT7 adds uridines to RNAs, highlight the role of the basic region, illustrate that XTUT7 can repress translation, and identify an amino acid important for uridine specificity.
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