Archael proteins Nop10 and Gar1 increase the catalytic activity of Cbf5 in pseudouridylating tRNA
Date
2012
Authors
Kamalampeta, Rajashekhar
Wieden-Kothe, Ute
Journal Title
Journal ISSN
Volume Title
Publisher
Nature Publishing Group
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.
Description
Sherpa Romeo green journal. Open access article. Creative Commons Attribution 4.0 International License (CC BY 4.0) applies
Keywords
Cbf5 , Nop10 , Gar1 , Pseudouridylation , Catalytic activity , Archaeal , Pseudouridine formation , tRNA modification
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