Evidence map›Paper›PMID 33290549›Full record

ArticleNucleic acids research2021

Structural basis for the substrate specificity and catalytic features of pseudouridine kinase from Arabidopsis thaliana.

Sang-Hoon Kim, Claus-Peter Witte, Sangkee Rhee

Open access · goldAbstract readComparative Study
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.7field-weighted citation impact, top 32% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Screening of flavor-enhancing yeast and its role in fig fermentation.Frontiers in bioengineering and biotechnology · 2026
    Article
  3. Article
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  8. Article
  9. Structure Characterization ofFrontiers in microbiology · 2022
    Article
  10. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

Sang-Hoon KimDepartment of Agricultural Biotechnology, Seoul National University, Seoul, Korea.
Claus-Peter WitteDepartment of Molecular Nutrition and Biochemistry of Plants, Leibniz University Hannover, Hannover, Germany.
Sangkee RheeDepartment of Agricultural Biotechnology, Seoul National University, Seoul, Korea.
Seoul National University · KRLeibniz University Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA modifications can regulate the stability of RNAs, mRNA-protein interactions, and translation efficiency. Pseudouridine is a prevalent RNA modification, and its metabolic fate after RNA turnover was recently characterized in eukaryotes, in the plant Arabidopsis thaliana. Here, we present structural and biochemical analyses of PSEUDOURIDINE KINASE from Arabidopsis (AtPUKI), the enzyme catalyzing the first step in pseudouridine degradation. AtPUKI, a member of the PfkB family of carbohydrate kinases, is a homodimeric α/β protein with a protruding small β-strand domain, which serves simultaneously as dimerization interface and dynamic substrate specificity determinant. AtPUKI has a unique nucleoside binding site specifying the binding of pseudourine, in particular at the nucleobase, by multiple hydrophilic interactions, of which one is mediated by a loop from the small β-strand domain of the adjacent monomer. Conformational transition of the dimerized small β-strand domains containing active site residues is required for substrate specificity. These dynamic features explain the higher catalytic efficiency for pseudouridine over uridine. Both substrates bind well (similar Km), but only pseudouridine is turned over efficiently. Our studies provide an example for structural and functional divergence in the PfkB family and highlight how AtPUKI avoids futile uridine phosphorylation which in vivo would disturb pyrimidine homeostasis.

Indexed as

Adenosine KinaseAmino Acid SequenceArabidopsisArabidopsis ProteinsBinding SitesCatalysisCatalytic DomainConsensus SequenceCrystallography, X-RayMagnesiumModels, MolecularPhosphotransferases (Alcohol Group Acceptor)Protein ConformationPseudouridineSequence AlignmentSequence Homology, Amino AcidAdenosine KinaseArabidopsis ProteinsMagnesiumPhosphotransferases (Alcohol Group Acceptor)Pseudouridineribokinase

Identifiers

PMID33290549
PMCPMC7797080
OpenAlexW3113108658

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.