ArticleProtein & cell2011
hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA.
Article in Protein & cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 44 citations in OpenAlex.
- NBS1 dePARylation by NUDT16 is critical for DNA double-strand break repair.Molecular and cellular biochemistry · 2025Article
- Aptamer-based assay for high-throughput substrate profiling of RNA decapping enzymes.Nucleic acids research · 2024Article
- TIRR regulates mRNA export and association with P-bodies in response to DNA damage.Nucleic acids research · 2024Article
- Application of Mammalian Nudix Enzymes to Capped RNA Analysis.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Mammalian Nudt15 hydrolytic and binding activity on methylated guanosine mononucleotides.European biophysics journal : EBJ · 2023Article
- Synthesis and Evaluation of Diguanosine Cap Analogs Modified at the C8-Position by Suzuki-Miyaura Cross-Coupling: Discovery of 7-Methylguanosine-Based Molecular Rotors.The Journal of organic chemistry · 2023Article
- m7G regulator-mediated molecular subtypes and tumor microenvironment in kidney renal clear cell carcinoma.Frontiers in pharmacology · 2022Article
- Insight into the Binding and Hydrolytic Preferences of hNudt16 Based on Nucleotide Diphosphate Substrates.International journal of molecular sciences · 2021Article
- Structural analyses of NudT16-ADP-ribose complexes direct rational design of mutants with improved processing of poly(ADP-ribosyl)ated proteins.Scientific reports · 2019Article
- Tumor suppressor PNRC1 blocks rRNA maturation by recruiting the decapping complex to the nucleolus.The EMBO journal · 2018Article
- Mechanism of 53BP1 activity regulation by RNA-binding TIRR and a designer protein.Nature structural & molecular biology · 2018Article
- Hydrolytic activity of human Nudt16 enzyme on dinucleotide cap analogs and short capped oligonucleotides.RNA (New York, N.Y.) · 2018Article
- NUDT expression is predictive of prognosis in patients with clear cell renal cell carcinoma.Oncology letters · 2017Article
- The ApaH-like phosphatase TbALPH1 is the major mRNA decapping enzyme of trypanosomes.PLoS pathogens · 2017Article
- New insights into decapping enzymes and selective mRNA decay.Wiley interdisciplinary reviews. RNA · 2017Review
- Two-headed tetraphosphate cap analogs are inhibitors of the Dcp1/2 RNA decapping complex.RNA (New York, N.Y.) · 2016Article
- Structural Basis for the Specificity of Human NUDT16 and Its Regulation by Inosine Monophosphate.PloS one · 2015Article
- Crystal structure of herpes simplex virus 2 gD bound to nectin-1 reveals a conserved mode of receptor recognition.Journal of virology · 2014Article
- Substrate ambiguity among the nudix hydrolases: biologically significant, evolutionary remnant, or both?Cellular and molecular life sciences : CMLS · 2013Article
- Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4.Nature structural & molecular biology · 2013Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human NUDT16 (hNUDT16) is a decapping enzyme initially identified as the human homolog to the Xenopus laevis X29. As a metalloenzyme, hNUDT16 relies on divalent cations for its cap-hydrolysis activity to remove m⁷GDP and m²²⁷GDP from RNAs. Metal also determines substrate specificity of the enzyme. So far, only U8 small nucleolar RNA (snoRNA) has been identified as the substrate of hNUDT16 in the presence of Mg²(+). Here we demonstrate that besides U8, hNUDT16 can also actively cleave the m⁷GDP cap from mRNAs in the presence of Mg²(+) or Mn²(+). We further show that hNUDT16 does not preferentially recognize U8 or mRNA substrates by our cross-inhibition and quantitative decapping assays. In addition, our mutagenesis analysis identifies several key residues involved in hydrolysis and confirms the key role of the REXXEE motif in catalysis. Finally an investigation into the subcellular localization of hNUDT16 revealed its abundance in both cytoplasm and nucleus. These findings extend the substrate spectrum of hNUDT16 beyond snoRNAs to also include mRNA, demonstrating the pleiotropic decapping activity of hNUDT16.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.