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Interrogation of RNA-protein interaction dynamics in bacterial growth.

Accepted version
Peer-reviewed

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Authors

Monti, Mie 
Herman, Reyme 
Mancini, Leonardo 
Capitanchik, Charlotte 
Davey, Karen 

Abstract

Characterising RNA-protein interaction dynamics is fundamental to understand how bacteria respond to their environment. In this study, we have analysed the dynamics of 91% of the Escherichia coli expressed proteome and the RNA-interaction properties of 271 RNA-binding proteins (RBPs) at different growth phases. We find that 68% of RBPs differentially bind RNA across growth phases and characterise 17 previously unannotated proteins as bacterial RBPs including YfiF, a ncRNA-binding protein. While these new RBPs are mostly present in Proteobacteria, two of them are orthologs of human mitochondrial proteins associated with rare metabolic disorders. Moreover, we reveal novel RBP functions for proteins such as the chaperone HtpG, a new stationary phase tRNA-binding protein. For the first time, the dynamics of the bacterial RBPome have been interrogated, showcasing how this approach can reveal the function of uncharacterised proteins and identify critical RNA-protein interactions for cell growth which could inform new antimicrobial therapies.

Description

Keywords

E. coli, Functional Screening, Proteomics, RBPome, iCLIP

Journal Title

Mol Syst Biol

Conference Name

Journal ISSN

1744-4292
1744-4292

Volume Title

Publisher

Springer Science and Business Media LLC
Sponsorship
Wellcome Trust (110071/Z/15/Z)
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