ArticleNature communications2023
Mechanism of U6 snRNA oligouridylation by human TUT1.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- Epigenetic regulation of humoral immunity: molecular mechanisms, diseases and therapeutic targets.Signal transduction and targeted therapy · 2026Review
- TUT1-catalyzed U6 snRNA 3'-end maturation is essential for RNA splicing and stem cell survival.EMBO reports · 2026Article
- 2'-O-methylation-dependent installation of NNature communications · 2026Article
- RNA Tailing by Nucleotidyltransferases in Plants: Mechanisms, Functions, and Biological Significance.Plants (Basel, Switzerland) · 2026Review
- Widespread mono- and oligoadenylation direct small noncoding RNA maturation versus degradation fates.The EMBO journal · 2026Article
- Structures and mechanisms of U6 snRNA mNature communications · 2025Article
- The poly(A) polymerase Star-PAP is regulated by stably associated phosphoinositide messengers.The Journal of biological chemistry · 2025Article
- A guide to the biogenesis and functions of endogenous small non-coding RNAs in animals.Nature reviews. Molecular cell biology · 2025Review
- Cryo-EM structure of human TUT1:U6 snRNA complex.Nucleic acids research · 2025Article
- Genome-wide association study identifies novel susceptible loci and evaluation of polygenic risk score for chronic obstructive pulmonary disease in a Taiwanese population.BMC genomics · 2024Article
- Identification and Expression Analysis of the Nucleotidyl Transferase Protein (NTP) Family in Soybean (International journal of molecular sciences · 2024Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
U6 snRNA is a catalytic RNA responsible for pre-mRNA splicing reactions and undergoes various post-transcriptional modifications during its maturation process. The 3'-oligouridylation of U6 snRNA by the terminal uridylyltransferase, TUT1, provides the Lsm-binding site in U6 snRNA for U4/U6 di-snRNP formation and this ensures pre-mRNA splicing. Here, we present the crystal structure of human TUT1 (hTUT1) complexed with U6 snRNA, representing the post-uridylation of U6 snRNA by hTUT1. The N-terminal ZF-RRM and catalytic palm clamp the single-stranded AUA motif between the 5'-short stem and the 3'-telestem of U6 snRNA, and the ZF-RRM specifically recognizes the AUA motif. The ZF and the fingers hold the telestem, and the 3'-end of U6 snRNA is placed in the catalytic pocket of the palm for oligouridylation. The oligouridylation of U6 snRNA depends on the internal four-adenosine tract in the 5'-part of the telestem of U6 snRNA, and hTUT1 adds uridines until the internal adenosine tract can form base-pairs with the 3'-oligouridine tract. Together, the recognition of the specific structure and sequence of U6 snRNA by the multi-domain TUT1 protein and the intrinsic sequence and structure of U6 snRNA ensure the oligouridylation of U6 snRNA.
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