ArticleProtein science : a publication of the Protein Society2013
Crystal structure of the dimer of two essential Salmonella typhimurium proteins, YgjD & YeaZ and calorimetric evidence for the formation of a ternary YgjD-YeaZ-YjeE complex.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 37 citations in OpenAlex.
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- Catalytic and regulatory basis of tRNA tNature communications · 2026Article
- Impairing protein-protein interactions in an essential tRNA modification complex: An innovative antimicrobial strategy against Pseudomonas aeruginosa.Journal of peptide science : an official publication of the European Peptide Society · 2025Article
- Structures of KEOPS bound to tRNA reveal functional roles of the kinase Bud32.Nature communications · 2024Article
- Molecular basis of A. thaliana KEOPS complex in biosynthesizing tRNA t6A.Nucleic acids research · 2024Article
- New Insights into the Biological Functions of Essential TsaB/YeaZ Protein inAntibiotics (Basel, Switzerland) · 2024Article
- Conservation and Diversification of tRNA tInternational journal of molecular sciences · 2022Review
- The structural and functional workings of KEOPS.Nucleic acids research · 2021Review
- Comparative Genomic Analysis of the DUF34 Protein Family Suggests Role as a Metal Ion Chaperone or Insertase.Biomolecules · 2021Article
- Structure of a reaction intermediate mimic in t6A biosynthesis bound in the active site of the TsaBD heterodimer from Escherichia coli.Nucleic acids research · 2021Article
- Molecular basis for t6A modification in human mitochondria.Nucleic acids research · 2020Article
- Conformational communication mediates the reset step in t6A biosynthesis.Nucleic acids research · 2019Article
- Structure-function analysis of Sua5 protein reveals novel functional motifs required for the biosynthesis of the universal tRNA (New York, N.Y.) · 2018Article
- The structure of the TsaB/TsaD/TsaE complex reveals an unexpected mechanism for the bacterial t6A tRNA-modification.Nucleic acids research · 2018Article
- Structure and mechanism of a bacterial t6A biosynthesis system.Nucleic acids research · 2018Article
- Proteomic analysis of the human KEOPS complex identifies C14ORF142 as a core subunit homologous to yeast Gon7.Nucleic acids research · 2017Article
- Structural and functional characterization of KEOPS dimerization by Pcc1 and its role in t6A biosynthesis.Nucleic acids research · 2016Article
- Biochemical evidence for relaxed substrate specificity of Nα-acetyltransferase (Rv3420c/rimI) of Mycobacterium tuberculosis.Scientific reports · 2016Article
- Crystal structures of the Gon7/Pcc1 and Bud32/Cgi121 complexes provide a model for the complete yeast KEOPS complex.Nucleic acids research · 2015Article
- The ATP-mediated formation of the YgjD-YeaZ-YjeE complex is required for the biosynthesis of tRNA t6A in Escherichia coli.Nucleic acids research · 2015Article
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8 authors at 3 institutions in 1 country.
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Abstract
YgjD from COG0533 is amongst a small group of highly conserved proteins present in all three domains of life. Various roles and biochemical functions (including sialoprotease and endonuclease activities) have been ascribed to YgjD and orthologs, the most recent, however, is involvement in the post transcriptional modification of certain tRNAs by formation of N6-threonyl-adenosine (t⁶A) at position 37. In bacteria, YgjD is essential and along with YeaZ, YjeE, and YrdC has been shown to be 'necessary and sufficient' for the tRNA modification. To further define interactions and possible roles for some of this set of proteins we have undertaken structural and biochemical studies. We show that formation of the previously reported heterodimer of YgjD-YeaZ involves ordering of the C-terminal region of YeaZ which extends along the surface of YgjD in the crystal structure. ATPγS or AMP is observed in YgjD while no nucleotide is bound on YeaZ. ITC experiments reveal previously unreported binary and ternary complexes which can be nucleotide dependent. The stoichiometry of the YeaZ-YgjD complex is 1:1 with a K(D) of 0.3 µM. YgjD and YjeE interact only in the presence of ATP, while YjeE binds to YgjD-YeaZ in the presence of ATP or ADP with a K(D) of 6 µM. YgjD doesn't bind the precursors of t⁶A, threonine, and bicarbonate. These results show a more complex set of interactions than previously thought, which may have a regulatory role. The understanding gained should help in deriving inhibitors of these essential proteins that might have potential as antibacterial drugs.
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