Show simple item record Kamalampeta, Rajashekhar Wieden-Kothe, Ute 2017-07-13T22:48:00Z 2017-07-13T22:48:00Z 2012
dc.identifier.citation Kamalampeta, R., & Kothe, U. (2012). Archael proteins Nop 10 and Gar 1 increase the catalytic activity of Cbf5 in pseudouridylating tRNA. Scientific Reports, 2, 663. doi:10.1038/srep00663 en_US
dc.description Sherpa Romeo green journal. Open access article. Creative Commons Attribution 4.0 International License (CC BY 4.0) applies en_US
dc.description.abstract Cbf5 is a pseudouridine synthase that usually acts in a guide RNA-dependent manner as part of H/ACA small ribonucleoproteins; however archaeal Cbf5 can also act independently of guide RNA in modifying uridine 55 in tRNA. This guide-independent activity of Cbf5 is enhanced by proteins Nop10 and Gar1 which are also found in H/ACA small ribonucleoproteins. Here, we analyzed the specific contribution of Nop10 and Gar1 for Cbf5-catalyzed pseudouridylation of tRNA. Interestingly, both Nop10 and Gar1 not only increase Cbf5’s affinity for tRNA, but they also directly enhance Cbf5’s catalytic activity by increasing the kcat of the reaction. In contrast to the guide RNA-dependent reaction, Gar1 is not involved in product release after tRNA modification. These results in conjunction with structural information suggest that Nop10 and Gar1 stabilize Cbf5 in its active conformation; we hypothesize that this might also be true for guide-RNA dependent pseudouridine formation by Cbf5. en_US
dc.language.iso en_US en_US
dc.publisher Nature Publishing Group en_US
dc.subject Cbf5 en_US
dc.subject Nop10 en_US
dc.subject Gar1 en_US
dc.subject Pseudouridylation en_US
dc.subject Catalytic activity en_US
dc.subject Archaeal en_US
dc.subject Pseudouridine formation en_US
dc.subject tRNA modification en_US
dc.subject.lcsh Transfer RNA
dc.subject.lcsh Pseudouridine
dc.subject.lcsh Catalysis
dc.title Archael proteins Nop10 and Gar1 increase the catalytic activity of Cbf5 in pseudouridylating tRNA 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 University of Lethbridge en_US

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