ArticleBiomolecules2017
QueF-Like, a Non-Homologous Archaeosine Synthase from the Crenarchaeota.
Article in Biomolecules, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Biosynthesis and function of 7-deazaguanine derivatives in bacteria and phages.Microbiology and molecular biology reviews : MMBR · 2024Review
- Four additional natural 7-deazaguanine derivatives in phages and how to make them.Nucleic acids research · 2023Article
- Article
- Archaeosine Modification of Archaeal tRNA: Role in Structural Stabilization.Journal of bacteriology · 2020Article
- Identification of a radical SAM enzyme involved in the synthesis of archaeosine.Nature chemical biology · 2019Article
- 7-Deazaguanine modifications protect phage DNA from host restriction systems.Nature communications · 2019Article
- Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA.Microorganisms · 2018Review
- Effects of Heterologous tRNA Modifications on the Production of Proteins Containing Noncanonical Amino Acids.Bioengineering (Basel, Switzerland) · 2018Article
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5 authors at 2 institutions in 1 country.
Funding
Abstract
Archaeosine (G⁺) is a structurally complex modified nucleoside ubiquitous to the Archaea, where it is found in the D-loop of virtually all archaeal transfer RNA (tRNA). Its unique structure, which includes a formamidine group that carries a formal positive charge, and location in the tRNA, led to the proposal that it serves a key role in stabilizing tRNA structure. Although G⁺ is limited to the Archaea, it is structurally related to the bacterial modified nucleoside queuosine, and the two share homologous enzymes for the early steps of their biosynthesis. In the Euryarchaeota, the last step of the archaeosine biosynthetic pathway involves the amidation of a nitrile group on an archaeosine precursor to give formamidine, a reaction catalyzed by the enzyme Archaeosine Synthase (ArcS). Most Crenarchaeota lack ArcS, but possess two proteins that inversely distribute with ArcS and each other, and are implicated in G⁺ biosynthesis. Here, we describe biochemical studies of one of these, the protein QueF-like (QueF-L) from
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