ArticleProceedings of the National Academy of Sciences of the United States of America2011
E1- and ubiquitin-like proteins provide a direct link between protein conjugation and sulfur transfer in archaea.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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.
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.
Who cites it
68 citing papers in PubMed, 87 citations in OpenAlex.
- Protein modification by a eukaryotic-like ubiquitin-related modifier in the hyperthermophilic archaeonmSystems · 2025Article
- Article
- Review
- Molecular basis for thiocarboxylation and release of Urm1 by its E1-activating enzyme Uba4.Nucleic acids research · 2024Article
- Article
- Article
- MoaE Is Involved in Response to Oxidative Stress inInternational journal of molecular sciences · 2023Article
- Backbone NMR resonance assignment of the intrinsically disordered UBact protein from Nitrospira nitrosa.Biomolecular NMR assignments · 2022Article
- Small Proteins in Archaea, a Mainly Unexplored World.Journal of bacteriology · 2022Review
- Sulfur modification in natural RNA and therapeutic oligonucleotides.RSC chemical biology · 2021Review
- Functional elucidation of TfuA in peptide backbone thioamidation.Nature chemical biology · 2021Article
- Urm1: A Non-Canonical UBL.Biomolecules · 2021Review
- DRJAMM Is Involved in the Oxidative Resistance inFrontiers in microbiology · 2021Article
- The Archaeal Proteome Project advances knowledge about archaeal cell biology through comprehensive proteomics.Nature communications · 2020Article
- Rhodanese-Like Domain Protein UbaC and Its Role in Ubiquitin-Like Protein Modification and Sulfur Mobilization in Archaea.Journal of bacteriology · 2019Article
- Assays for ubiquitin-like protein ligation and proteasome function in archaea.Methods in enzymology · 2019Article
- Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.Emerging topics in life sciences · 2018Article
- Molecular Factors of Hypochlorite Tolerance in the Hypersaline Archaeon Haloferax volcanii.Genes · 2018Article
- Methionine Sulfoxide Reductases of Archaea.Antioxidants (Basel, Switzerland) · 2018Review
- The Uba4 domain interplay is mediated via a thioester that is critical for tRNA thiolation through Urm1 thiocarboxylation.Nucleic acids research · 2018Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Based on our recent work with Haloferax volcanii, ubiquitin-like (Ubl) proteins (SAMP1 and SAMP2) are known to be covalently attached to proteins in archaea. Here, we investigated the enzymes required for the formation of these Ubl-protein conjugates (SAMPylation) and whether this system is linked to sulfur transfer. Markerless in-frame deletions were generated in H. volcanii target genes. The mutants were examined for: (i) the formation of Ubl protein conjugates, (ii) growth under various conditions, including those requiring the synthesis of the sulfur-containing molybdenum cofactor (MoCo), and (iii) the thiolation of tRNA. With this approach we found that UbaA of the E1/MoeB/ThiF superfamily was required for the formation of both SAMP1- and SAMP2-protein conjugates. In addition, UbaA, SAMP1, and MoaE (a homolog of the large subunit of molybdopterin synthase) were essential for MoCo-dependent dimethyl sulfoxide reductase activity, suggesting that these proteins function in MoCo-biosynthesis. UbaA and SAMP2 were also crucial for optimal growth at high temperature and the thiolation of tRNA. Based on these results, we propose a working model for archaea in which the E1-like UbaA can activate multiple Ubl SAMPs for protein conjugation as well as for sulfur transfer. In sulfur transfer, SAMP1 and SAMP2 appear specific for MoCo biosynthesis and the thiolation of tRNA, respectively. Overall, this study provides a fundamental insight into the diverse cellular functions of the Ubl system.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.