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The translational NTPase OLA1 is an RNA binding protein
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Date
2023
Authors
Semmelrock, Jessica
University of Lethbridge. Faculty of Arts and Science
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Publisher
Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry
Abstract
With ribosome-dependent protein synthesis being essential to life, previously overlooked components of the ribosome regulome can potentially become novel therapeutic targets. Obg-like ATPase 1 (OLA1) – or YchF in bacteria – is among several universally conserved guanosine nucleotide-dependent molecular switches, called GTPases, that interact with the ribosome throughout its life cycle and provide an important fitness advantage. However, OLA1’s exact cellular role and molecular mechanism of action are poorly understood. Structural modelling reveals that OLA1 can form a tRNA-bound complex in the ribosomal A site, overall mimicking the structure of the Elongation Factor-Tu ternary complex (EF-Tu•GTP•aminoacyl tRNA) and several other translational GTPases. Using electrophoretic mobility shift assays (EMSAs) and nitrocellulose filtration, I reveal that human OLA1 can bind tRNA independent of the ribosome. Integration of these results with previous studies suggests a role for OLA1 in ribosome maintenance.
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Keywords
Translation , Ribosome , RNA , YchF , OLA1 , GTPase , Binding proteins