Show simple item record Tillault, Anne-Sophie Fourmann, Jean-Baptiste Loegler, Christine Wieden, Hans-Joachim Wieden-Kothe, Ute Charpentier, Bruno 2019-06-02T21:09:10Z 2019-06-02T21:09:10Z 2015
dc.identifier.citation Tillault, A., Fourmann, J., Loegler, C., Wieden, H.-J., Kothe, U., & Charpentier, B. (2015). Contribution of two conserved histidines to the dual activity of archaeal RNA guide-dependent and -independent pseudouridine synthase Cbf5. RNA, 21(7), 1233-1239. doi: 10.1261/rna.051425.115 en_US
dc.description Sherpa Romeo green journal. Open access article. Creative Commons Attribution-NonCommercial 4.0 International LIcense (CC BY-NC 4.0) applies en_US
dc.description.abstract In all organisms, several distinct stand-alone pseudouridine synthase (PUS) family enzymes are expressed to isomerizeuridine into pseudouridine (Ψ) by specific recognition of RNAs. In addition, Ψs are generated in Archaea and Eukaryotes by PUS enzymes which are organized as ribonucleoprotein particles (RNP)—the box H/ACA s/snoRNPs. For this modification system, a unique TruB-like catalytic PUS subunit is associated with various RNA guides which specifically target and secure substrate RNAs by base-pairing. The archaeal Cbf5 PUS displays the special feature of exhibiting both RNA guide-dependent and -independent activities. Structures of substrate-bound TruB and H/ACA sRNP revealed the importance of histidines in positioning the target uridine in the active site. To analyze the respective role of H60 and H77, we have generated variants carrying alanine substitutions at these positions. The impact of the mutations was analyzed for unguided modifications U55 in tRNA and U2603 in 23S rRNA, and for activity of the box H/ACA Pab91 sRNP enzyme. H77 (H43 in TruB), but not H60, appeared to be crucial for the RNA guide-independent activity. In contrast to earlier suggestions, H60 was found to be noncritical for the activity of the H/ACA sRNP, but contributes together with H77 to the full activity of H/ACA sRNPs. The data suggest that a similar catalytic process was conserved in the two divergent pseudouridylation systems. en_US
dc.language.iso en_US en_US
dc.publisher Cold Spring Harbor Laboratory Press en_US
dc.subject Archaea en_US
dc.subject Cbf5 en_US
dc.subject H/ACA sRNP en_US
dc.subject RNA modification en_US
dc.subject Pseudouridine en_US
dc.subject.lcsh Pseudouridine--Research
dc.subject.lcsh RNA--Research
dc.title Contribution of two conserved histidines to the dual activity of archael RNA guide-dependent and -independent pseudouridine synthase Cbf5 en_US
dc.type Article en_US
dc.publisher.faculty Arts and Science en_US
dc.publisher.department Department of Chemistry and Biochemistry en_US
dc.description.peer-review Yes en_US
dc.publisher.institution Bipole de l'Université de Lorraine en_US
dc.publisher.institution University of Lethbridge en_US

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