Contribution of two conserved histidines to the dual activity of archael RNA guide-dependent and -independent pseudouridine synthase Cbf5

Simple item page
dc.contributor.authorTillault, Anne-Sophie
dc.contributor.authorFourmann, Jean-Baptiste
dc.contributor.authorLoegler, Christine
dc.contributor.authorWieden, Hans-Joachim
dc.contributor.authorWieden-Kothe, Ute
dc.contributor.authorCharpentier, Bruno
dc.date.accessioned2019-06-02T21:09:10Z
dc.date.available2019-06-02T21:09:10Z
dc.date.issued2015
dc.descriptionSherpa Romeo green journal. Open access article. Creative Commons Attribution-NonCommercial 4.0 International LIcense (CC BY-NC 4.0) appliesen_US
dc.description.abstractIn 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.description.peer-reviewYesen_US
dc.identifier.citationTillault, 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.051425.115en_US
dc.identifier.urihttps://hdl.handle.net/10133/5383
dc.language.isoen_USen_US
dc.publisherCold Spring Harbor Laboratory Pressen_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.publisher.institutionBipole de l'Université de Lorraineen_US
dc.publisher.institutionUniversity of Lethbridgeen_US
dc.publisher.urlhttps://dx.doi.org/10.1261/rna.051425.115
dc.subjectArchaeaen_US
dc.subjectCbf5en_US
dc.subjectH/ACA sRNPen_US
dc.subjectRNA modificationen_US
dc.subjectPseudouridineen_US
dc.subject.lcshPseudouridine--Research
dc.subject.lcshRNA--Research
dc.titleContribution of two conserved histidines to the dual activity of archael RNA guide-dependent and -independent pseudouridine synthase Cbf5en_US
dc.typeArticleen_US
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
Wieden-contribution-of-two.pdf
Size:
422.23 KB
Format:
Adobe Portable Document Format
Description:
Download
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
1.75 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Wieden, Hans-Joachim
Wieden-Kothe, Ute