ArticleThe FEBS journal2016
Mechanistic insight into protein modification and sulfur mobilization activities of noncanonical E1 and associated ubiquitin-like proteins of Archaea.
Article in The FEBS journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 25 citations in OpenAlex.
- Protein modification by a eukaryotic-like ubiquitin-related modifier in the hyperthermophilic archaeonmSystems · 2025Article
- Molecular choreography of E1 enzymes in ubiquitin-like protein cascades: New insights into dynamics and specificity.The Journal of biological chemistry · 2025Review
- Molecular basis for thiocarboxylation and release of Urm1 by its E1-activating enzyme Uba4.Nucleic acids research · 2024Article
- Article
- Insights into the Lysine Acetylome of the HaloarchaeonAntioxidants (Basel, Switzerland) · 2023Article
- E2/E3-independent ubiquitin-like protein conjugation by Urm1 is directly coupled to cysteine persulfidation.The EMBO journal · 2022Article
- Acute Myeloid Leukemia-Related Proteins Modified by Ubiquitin and Ubiquitin-like Proteins.International journal of molecular sciences · 2022Review
- Urm1: A Non-Canonical UBL.Biomolecules · 2021Review
- Multidomain ribosomal protein trees and the planctobacterial origin of neomura (eukaryotes, archaebacteria).Protoplasma · 2020Review
- Rhodanese-Like Domain Protein UbaC and Its Role in Ubiquitin-Like Protein Modification and Sulfur Mobilization in Archaea.Journal of bacteriology · 2019Article
- Article
- 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
- Methionine Sulfoxide Reductases of Archaea.Antioxidants (Basel, Switzerland) · 2018Review
- Rpn11-mediated ubiquitin processing in an ancestral archaeal ubiquitination system.Nature communications · 2018Article
- The Uba4 domain interplay is mediated via a thioester that is critical for tRNA thiolation through Urm1 thiocarboxylation.Nucleic acids research · 2018Article
- Article
- High expression of ubiquitin-conjugating enzyme E2A predicts poor prognosis in hepatocellular carcinoma.Oncology letters · 2018Article
- Methionine Sulfoxide Reductase A (MsrA) and Its Function in Ubiquitin-Like Protein Modification inmBio · 2017Article
- Structural Insight into Ubiquitin-Like Protein Recognition and Oligomeric States of JAMM/MPNStructure (London, England : 1993) · 2017Article
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12 authors at 3 institutions in 1 country.
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Abstract
Here we provide the first detailed biochemical study of a noncanonical E1-like enzyme with broad specificity for cognate ubiquitin-like (Ubl) proteins that mediates Ubl protein modification and sulfur mobilization to form molybdopterin and thiolated tRNA. Isothermal titration calorimetry and in vivo analyses proved useful in discovering that environmental conditions, ATP binding, and Ubl type controlled the mechanism of association of the Ubl protein with its cognate E1-like enzyme (SAMP and UbaA of the archaeon Haloferax volcanii, respectively). Further analysis revealed that ATP hydrolysis triggered the formation of thioester and peptide bonds within the Ubl:E1-like complex. Importantly, the thioester was an apparent precursor to Ubl protein modification but not sulfur mobilization. Comparative modeling to MoeB/ThiF guided the discovery of key residues within the adenylation domain of UbaA that were needed to bind ATP as well as residues that were specifically needed to catalyze the downstream reactions of sulfur mobilization and/or Ubl protein modification. UbaA was also found to be Ubl-automodified at lysine residues required for early (ATP binding) and late (sulfur mobilization) stages of enzyme activity revealing multiple layers of autoregulation. Cysteine residues, distinct from the canonical E1 'active site' cysteine, were found important in UbaA function supporting a model that this noncanonical E1 is structurally flexible in its active site to allow Ubl~adenylate, Ubl~E1-like thioester and cysteine persulfide(s) intermediates to form.
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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.