Discovery of novel bacterial queuine salvage enzymes and pathways in human pathogens
In: Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2019, 116 (38), pp.19126-19135. ⟨10.1073/pnas.1909604116⟩ Proceedings of the National Academy of Sciences of the United States of America, 2019, 116 (38), pp.19126-19135. ⟨10.1073/pnas.1909604116⟩; (2019)
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Queuosine (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 preQ 0 and preQ 1 also occurs. With the exception of Escherichia coli YhhQ, shown to transport preQ 0 and preQ 1 , 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 preQ 1 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.
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Discovery of novel bacterial queuine salvage enzymes and pathways in human pathogens
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| Autor/in / Beteiligte Person: | Payan, Daniel J. ; Šepić, Sara ; Almo, Steven C. ; Valérie de Crécy-Lagard ; Dedon, Peter C. ; Gerlt, John A. ; Gadi, Vinod ; Swairjo, Manal A. ; Martin-Verstraete, Isabelle ; Yuan, Yifeng ; Balamkundu, Seetharamsing ; Neelakandan, Ramesh ; Chuan Fa Liu ; Zallot, Rémi ; Grove, Tyler L. ; University of Florida [Gainesville] (UF) ; University of Illinois at Urbana-Champaign [Urbana] ; University of Illinois System ; Albert Einstein College of Medicine [New York] ; Pathogénèse des Bactéries Anaérobies / Pathogenesis of Bacterial Anaerobes (PBA (U-Pasteur_6)) ; Institut Pasteur [Paris]-Université Paris Diderot - Paris 7 (UPD7) ; Singapore-MIT Alliance for Research and Technology (SMART) ; Massachusetts Institute of Technology (MIT) ; San Diego State University (SDSU) ; This work was funded by the National Institutes of Health (R01 GM70641 to V.d.C. L. ; P01 GM118303 to J.A.G. and S.C.A. ; U54-GM093342 to J.A.G. and S.C.A. ; R21-AI133329 to T.L.G. and S.C.A. ; U54-GM094662 to S.C.A. ; GM110588 to M.A.S.), the Price Family Foundation (S.C.A.), and the California Metabolic Research Foundation (M.A.S.). ; We acknowledge the Albert Einstein Anaerobic Structural and Functional Genomics Resource (http://www.nysgxrc.org/psi3/anaerobic.html). We thank Martin I. H. McLauglin and Wilfred A. van der Donk for providing the guidance and the plasmid isc-pBADCDF for in vivo maturation of metalloenzymes. The LC-MS analyses were performed by Furong Sun at the Mass Spectrometry Laboratory, a Service Facility from the School of Chemical Sciences at University of Illinois at Urbana–Champaign. The Einstein Crystallographic Core X-Ray diffraction facility is supported by NIH Shared Instrumentation Grant S10 OD020068. This research used resources of the Advanced Photon Source, a US Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Argonne National Laboratory under Contract No. DE-AC02-06CH11357. Use of the Lilly Research Laboratories Collaborative Access Team (LRL-CAT) beamline at Sector 31 of the Advanced Photon Source was provided by Eli Lilly Company, which operates the facility. ; Institut Pasteur [Paris] (IP)-Université Paris Diderot - Paris 7 (UPD7) ; University of Florida [Gainesville] ; Albert Einstein College of Medicine ; Alliance, Singapore-MIT ; National University of Singapore (NUS) |
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| Quelle: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2019, 116 (38), pp.19126-19135. ⟨10.1073/pnas.1909604116⟩ Proceedings of the National Academy of Sciences of the United States of America, 2019, 116 (38), pp.19126-19135. ⟨10.1073/pnas.1909604116⟩; (2019) |
| Veröffentlichung: | Proceedings of the National Academy of Sciences, 2019 |
| Medientyp: | unknown |
| ISSN: | 0027-8424 (print) ; 1091-6490 (print) |
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