A novel double kink-turn module in euryarchaeal RNase P RNAs

Nucleic Acids Research
Lien B LaiVenkat Gopalan

Abstract

RNase P is primarily responsible for the 5΄ maturation of transfer RNAs (tRNAs) in all domains of life. Archaeal RNase P is a ribonucleoprotein made up of one catalytic RNA and five protein cofactors including L7Ae, which is known to bind the kink-turn (K-turn), an RNA structural element that causes axial bending. However, the number and location of K-turns in archaeal RNase P RNAs (RPRs) are unclear. As part of an integrated approach, we used native mass spectrometry to assess the number of L7Ae copies that bound the RPR and site-specific hydroxyl radical-mediated footprinting to localize the K-turns. Mutagenesis of each of the putative K-turns singly or in combination decreased the number of bound L7Ae copies, and either eliminated or changed the L7Ae footprint on the mutant RPRs. In addition, our results support an unprecedented 'double K-turn' module in type A and type M archaeal RPR variants.

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Citations

Nov 18, 2017·Nucleic Acids Research·Zainab AhdashArgyris Politis
Oct 4, 2017·RNA·Venkat GopalanAndrey S Krasilnikov
Jan 1, 2018·Quarterly Reviews of Biophysics·Lin Huang, David M J Lilley
Jun 15, 2019·Nature Communications·Futang WanMing Lei
May 4, 2018·Nucleic Acids Research·Anna PerederinaAndrey S Krasilnikov
Apr 24, 2018·FEMS Microbiology Reviews·Béatrice Clouet-d'OrvalLisa-Katharina Maier
Nov 3, 2021·Chemical Reviews·Dalton T SnyderVicki H Wysocki

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Methods Mentioned

BETA
footprinting
pull-down
in vitro transcription

Software Mentioned

ImageQuant
MjaRPR
Assemble
PfuRPR

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