ArticlePloS one2014
Structure-function relationship of a plant NCS1 member--homology modeling and mutagenesis identified residues critical for substrate specificity of PLUTO, a nucleobase transporter from Arabidopsis.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 34 citations in OpenAlex.
- Characterization of Nucleobase Cation Symporter 1 (NCS1) Localized to the Plastids of Nicotiana tabacum.Genes to cells : devoted to molecular & cellular mechanisms · 2026Article
- Advances and opportunities for computational interrogation of plant proteins.The Plant journal : for cell and molecular biology · 2026Review
- Degradation of FATTY ACID EXPORT PROTEIN1 by RHOMBOID-LIKE PROTEASE11 contributes to cold tolerance in Arabidopsis.The Plant cell · 2024Article
- The last two transmembrane helices in the APC-type FurE transporter act as an intramolecular chaperone essential for concentrative ER-exit.Microbial cell (Graz, Austria) · 2024Article
- A newly identified glycosyltransferase AsRCOM provides resistance to purple curl leaf disease in agave.BMC genomics · 2023Article
- Structure of cytosine transport protein CodB provides insight into nucleobase-cation symporter 1 mechanism.The EMBO journal · 2022Article
- The importance of thiamine (vitamin BThe Journal of biological chemistry · 2020Review
- Genetic analysis of tomato root colonization by arbuscular mycorrhizal fungi.Annals of botany · 2019Article
- Pyrimidine Salvage: Physiological Functions and Interaction with Chloroplast Biogenesis.Plant physiology · 2019Article
- Recent developments in nucleobase cation symporter-1 (NCS1) family transport proteins from bacteria, archaea, fungi and plants.Journal of biosciences · 2018Review
- Allantoin transport protein, PucI, from Bacillus subtilis: evolutionary relationships, amplified expression, activity and specificity.Microbiology (Reading, England) · 2016Article
- The solute specificity profiles of nucleobase cation symporter 1 (NCS1) from Zea mays and Setaria viridis illustrate functional flexibility.Protoplasma · 2016Article
- Histidine 352 (His352) and tryptophan 355 (Trp355) are essential for flax UGT74S1 glucosylation activity toward secoisolariciresinol.PloS one · 2015Article
- Molecular mechanism of ligand recognition by membrane transport protein, Mhp1.The EMBO journal · 2014Article
- Structural comparison, substrate specificity, and inhibitor binding of AGPase small subunit from monocot and dicot: present insight and future potential.BioMed research international · 2014Article
- Nucleobase and nucleoside transport and integration into plant metabolism.Frontiers in plant science · 2014Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plastidic uracil salvage is essential for plant growth and development. So far, PLUTO, the plastidic nucleobase transporter from Arabidopsis thaliana is the only known uracil importer at the inner plastidic membrane which represents the permeability barrier of this organelle. We present the first homology model of PLUTO, the sole plant NCS1 member from Arabidopsis based on the crystal structure of the benzyl hydantoin transporter MHP1 from Microbacterium liquefaciens and validated by molecular dynamics simulations. Polar side chains of residues Glu-227 and backbones of Val-145, Gly-147 and Thr-425 are proposed to form the binding site for the three PLUTO substrates uracil, adenine and guanine. Mutational analysis and competition studies identified Glu-227 as an important residue for uracil and to a lesser extent for guanine transport. A differential response in substrate transport was apparent with PLUTO double mutants E227Q G147Q and E227Q T425A, both of which most strongly affected adenine transport, and in V145A G147Q, which markedly affected guanine transport. These differences could be explained by docking studies, showing that uracil and guanine exhibit a similar binding mode whereas adenine binds deep into the catalytic pocket of PLUTO. Furthermore, competition studies confirmed these results. The present study defines the molecular determinants for PLUTO substrate binding and demonstrates key differences in structure-function relations between PLUTO and other NCS1 family members.
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