Insights into the evolutionary conserved regulation of Rio ATPase activity
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Eukaryotic ribosome biogenesis is a complex dynamic process which requires the action of numerous ribosome assembly factors. Among them, the eukaryotic Rio protein family members (Rio1, Rio2 and Rio3) belong to an ancient conserved atypical protein kinase/ ATPase family required for the maturation of the small ribosomal subunit (SSU). Recent structure-function analyses suggested an ATPase-dependent role of the Rio proteins to regulate their dynamic association with the nascent pre-SSU. However, the evolutionary origin of this feature and the detailed molecular mechanism that allows controlled activation of the catalytic activity remained to be determined. In this work we provide functional evidence showing a conserved role of the archaeal Rio proteins for the synthesis of the SSU in archaea. Moreover, we unravel a conserved RNA-dependent regulation of the Rio ATPases, which in the case of Rio2 involves, at least, helix 30 of the SSU rRNA and the P-loop lysine within the shared RIO domain. Together, our study suggests a ribosomal RNA-mediated regulatory mechanism enabling the appropriate stimulation of Rio2 catalytic activity and subsequent release of Rio2 from the nascent pre- 40S particle. Based on our findings we propose a unified release mechanism for the Rio proteins.
Knüppel , R , Christensen , R , Gray , F C , Esser , D , Strauss , D , Medenbach , J , Siebers , B , MacNeill , S A , LaRonde , N & Ferreira-Cerca , S 2018 , ' Insights into the evolutionary conserved regulation of Rio ATPase activity ' Nucleic Acids Research , vol. 46 , no. 3 , pp. 1441-1456 . https://doi.org/10.1093/nar/gkx1236
Nucleic Acids Research
Copright The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact firstname.lastname@example.org
DescriptionWork in the MacNeill laboratory was funded by Forskningsrådet for Natur og Univers (FNU) [sagsnr. 272-05-0446]; Scottish Universities Life Sciences Alliance (SULSA).
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