ArticlePloS one2014
Archaeal Tuc1/Ncs6 homolog required for wobble uridine tRNA thiolation is associated with ubiquitin-proteasome, translation, and RNA processing system homologs.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 23 papers.
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23 citing papers in PubMed, 38 citations in OpenAlex.
- Evolutionary conservation of ubiquitin-like protein urmylation as revealed by URM1 gene shuffle from archaea to yeast.Communications biology · 2025Article
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- Ncs2* mediates in vivo virulence of pathogenic yeast through sulphur modification of cytoplasmic transfer RNA.Nucleic acids research · 2023Article
- Insights into the Lysine Acetylome of the HaloarchaeonAntioxidants (Basel, Switzerland) · 2023Article
- The thiolation of uridine 34 in tRNA, which controls protein translation, depends on a [4Fe-4S] cluster in the archaeum Methanococcus maripaludis.Scientific reports · 2023Article
- Learning from the Invaders: What Viruses Teach Us about RNA-Based Regulation in Microbes.Microorganisms · 2022Article
- Small Proteins in Archaea, a Mainly Unexplored World.Journal of bacteriology · 2022Review
- The first apicoplast tRNA thiouridylase plays a vital role in the growth ofFrontiers in cellular and infection microbiology · 2022Article
- Biosynthesis and Degradation of Sulfur Modifications in tRNAs.International journal of molecular sciences · 2021Review
- Natural variations of SLG1 confer high-temperature tolerance in indica rice.Nature communications · 2020Article
- An ancient type of MnmA protein is an iron-sulfur cluster-dependent sulfurtransferase for tRNA anticodons.RNA (New York, N.Y.) · 2020Article
- Rhodanese-Like Domain Protein UbaC and Its Role in Ubiquitin-Like Protein Modification and Sulfur Mobilization in Archaea.Journal of bacteriology · 2019Article
- Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA.Microorganisms · 2018Review
- Recent Advances in Our Understanding of the Biosynthesis of Sulfur Modifications in tRNAs.Frontiers in microbiology · 2018Article
- Nonredox thiolation in tRNA occurring via sulfur activation by a [4Fe-4S] cluster.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Biosynthesis of Sulfur-Containing tRNA Modifications: A Comparison of Bacterial, Archaeal, and Eukaryotic Pathways.Biomolecules · 2017Review
- Toward Time-Resolved Analysis of RNA Metabolism in Archaea Using 4-Thiouracil.Frontiers in microbiology · 2017Article
- A [3Fe-4S] cluster is required for tRNA thiolation in archaea and eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Mechanistic insight into protein modification and sulfur mobilization activities of noncanonical E1 and associated ubiquitin-like proteins of Archaea.The FEBS journal · 2016Article
Corrections and comments
- Erratum issued
Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
While cytoplasmic tRNA 2-thiolation protein 1 (Tuc1/Ncs6) and ubiquitin-related modifier-1 (Urm1) are important in the 2-thiolation of 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) at wobble uridines of tRNAs in eukaryotes, the biocatalytic roles and properties of Ncs6/Tuc1 and its homologs are poorly understood. Here we present the first report of an Ncs6 homolog of archaea (NcsA of Haloferax volcanii) that is essential for maintaining cellular pools of thiolated tRNA(Lys)UUU and for growth at high temperature. When purified from Hfx. volcanii, NcsA was found to be modified at Lys204 by isopeptide linkage to polymeric chains of the ubiquitin-fold protein SAMP2. The ubiquitin-activating E1 enzyme homolog of archaea (UbaA) was required for this covalent modification. Non-covalent protein partners that specifically associated with NcsA were also identified including UbaA, SAMP2, proteasome activating nucleotidase (PAN)-A/1, translation elongation factor aEF-1α and a β-CASP ribonuclease homolog of the archaeal cleavage and polyadenylation specificity factor 1 family (aCPSF1). Together, our study reveals that NcsA is essential for growth at high temperature, required for formation of thiolated tRNA(Lys)UUU and intimately linked to homologs of ubiquitin-proteasome, translation and RNA processing systems.
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