ArticleJournal of molecular biology2013
In human pseudouridine synthase 1 (hPus1), a C-terminal helical insert blocks tRNA from binding in the same orientation as in the Pus1 bacterial homologue TruA, consistent with their different target selectivities.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 38 citations in OpenAlex.
- The pseudouridine synthase PUSL1 modifies U39 of mitochondrial tRNAs and is linked to human neurological phenotypes.Nucleic acids research · 2026Article
- Quantitative analysis of small RNA pseudouridylation reveals interplay of PUS enzymes in tRNA anticodon stem-loop.Nature communications · 2026Article
- Mechanistic insight into the pseudouridylation of RNA.RNA biology · 2025Review
- Myopathy, lactic acidosis and sideroblastic anemia syndrome 1 (MLASA1): clinical hallmarks in a large pedigree with a novelHaematologica · 2025Article
- The molecular basis of tRNA selectivity by human pseudouridine synthase 3.Molecular cell · 2024Article
- Decoding the 'Fifth' Nucleotide: Impact of RNA Pseudouridylation on Gene Expression and Human Disease.Molecular biotechnology · 2024Review
- Truncated protein isoforms generate diversity of protein localization and function in yeast.Cell systems · 2024Article
- Pseudouridine synthase 1 regulates erythropoiesis via transfer RNAs pseudouridylation and cytoplasmic translation.iScience · 2024Article
- FOXA1-dependent PUS1 regulates EIF3b stability in a non-enzymatic pathway mediating prostate cancer bone metastasis.International journal of biological sciences · 2024Article
- The structural basis of mRNA recognition and binding by yeast pseudouridine synthase PUS1.PloS one · 2023Article
- Pseudouridine synthases modify human pre-mRNA co-transcriptionally and affect pre-mRNA processing.Molecular cell · 2022Article
- Pseudouridines in RNAs: switching atoms means shifting paradigms.FEBS letters · 2021Review
- Long Non-Coding RNA Epigenetics.International journal of molecular sciences · 2021Review
- Regulation and Function of RNA Pseudouridylation in Human Cells.Annual review of genetics · 2020Review
- mRNA structure determines modification by pseudouridine synthase 1.Nature chemical biology · 2019Article
- Eukaryotic stand-alone pseudouridine synthases - RNA modifying enzymes and emerging regulators of gene expression?RNA biology · 2017Review
- Dual nature of pseudouridylation in U2 snRNA: Pus1p-dependent and Pus1p-independent activities in yeasts and higher eukaryotes.RNA (New York, N.Y.) · 2017Article
- Pseudouridine synthase 1 deficient mice, a model for Mitochondrial Myopathy with Sideroblastic Anemia, exhibit muscle morphology and physiology alterations.Scientific reports · 2016Article
- Clinical and molecular study in a long-surviving patient with MLASA syndrome due to novel PUS1 mutations.Neurogenetics · 2016Article
- Dye label interference with RNA modification reveals 5-fluorouridine as non-covalent inhibitor.Nucleic acids research · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Human pseudouridine (Ψ) synthase Pus1 (hPus1) modifies specific uridine residues in several non-coding RNAs: tRNA, U2 spliceosomal RNA, and steroid receptor activator RNA. We report three structures of the catalytic core domain of hPus1 from two crystal forms, at 1.8Å resolution. The structures are the first of a mammalian Ψ synthase from the set of five Ψ synthase families common to all kingdoms of life. hPus1 adopts a fold similar to bacterial Ψ synthases, with a central antiparallel β-sheet flanked by helices and loops. A flexible hinge at the base of the sheet allows the enzyme to open and close around an electropositive active-site cleft. In one crystal form, a molecule of Mes [2-(N-morpholino)ethane sulfonic acid] mimics the target uridine of an RNA substrate. A positively charged electrostatic surface extends from the active site towards the N-terminus of the catalytic domain, suggesting an extensive binding site specific for target RNAs. Two α-helices C-terminal to the core domain, but unique to hPus1, extend along the back and top of the central β-sheet and form the walls of the RNA binding surface. Docking of tRNA to hPus1 in a productive orientation requires only minor conformational changes to enzyme and tRNA. The docked tRNA is bound by the electropositive surface of the protein employing a completely different binding mode than that seen for the tRNA complex of the Escherichia coli homologue TruA.
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