6p78
queuine lyase from Clostridium spiroforme bound to SAM and queuine
Structural highlights
FunctionPublication Abstract from PubMedQueuosine (Q) is a complex tRNA modification widespread in eukaryotes and bacteria that contributes to the efficiency and accuracy of protein synthesis. Eukaryotes are not capable of Q synthesis and rely on salvage of the queuine base (q) as a Q precursor. While many bacteria are capable of Q de novo synthesis, salvage of the prokaryotic Q precursors preQ0 and preQ1 also occurs. With the exception of Escherichia coli YhhQ, shown to transport preQ0 and preQ1, the enzymes and transporters involved in Q salvage and recycling have not been well described. We discovered and characterized 2 Q salvage pathways present in many pathogenic and commensal bacteria. The first, found in the intracellular pathogen Chlamydia trachomatis, uses YhhQ and tRNA guanine transglycosylase (TGT) homologs that have changed substrate specificities to directly salvage q, mimicking the eukaryotic pathway. The second, found in bacteria from the gut flora such as Clostridioides difficile, salvages preQ1 from q through an unprecedented reaction catalyzed by a newly defined subgroup of the radical-SAM enzyme family. The source of q can be external through transport by members of the energy-coupling factor (ECF) family or internal through hydrolysis of Q by a dedicated nucleosidase. This work reinforces the concept that hosts and members of their associated microbiota compete for the salvage of Q precursors micronutrients. Discovery of novel bacterial queuine salvage enzymes and pathways in human pathogens.,Yuan Y, Zallot R, Grove TL, Payan DJ, Martin-Verstraete I, Sepic S, Balamkundu S, Neelakandan R, Gadi VK, Liu CF, Swairjo MA, Dedon PC, Almo SC, Gerlt JA, de Crecy-Lagard V Proc Natl Acad Sci U S A. 2019 Sep 17;116(38):19126-19135. doi:, 10.1073/pnas.1909604116. Epub 2019 Sep 3. PMID:31481610[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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