Role of Escherichia coli YbeY, a highly conserved protein, in rRNA processing
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Author(s)
Davies, Bryan W.
Koehrer, Caroline
Jacob, Asha I.
Simmons, Lyle A.
Zhu, Jianyu
Aleman, Lourdes M.
RajBhandary, Uttam L.
Walker, Graham C.
Date Issued
September 2010
Journal
Molecular Microbiology
Publisher
Wiley-Blackwell Pubishers
Citation
Davies, Bryan W. et al. “Role of Escherichia Coli YbeY, a Highly Conserved Protein, in rRNA Processing.” Molecular Microbiology 78.2 (2010): 506–518. Web.
Version
Author's final manuscript
Abstract
The UPF0054 protein family is highly conserved with homologues present in nearly every sequenced bacterium. In some bacteria, the respective gene is essential, while in others its loss results in a highly pleiotropic phenotype. Despite detailed structural studies, a cellular role for this protein family has remained unknown. We report here that deletion of the Escherichia coli homologue, YbeY, causes striking defects that affect ribosome activity, translational fidelity and ribosome assembly. Mapping of 16S, 23S and 5S rRNA termini reveals that YbeY influences the maturation of all three rRNAs, with a particularly strong effect on maturation at both the 5′- and 3′-ends of 16S rRNA as well as maturation of the 5′-termini of 23S and 5S rRNAs. Furthermore, we demonstrate strong genetic interactions between ybeY and rnc (encoding RNase III), ybeY and rnr (encoding RNase R), and ybeY and pnp (encoding PNPase), further suggesting a role for YbeY in rRNA maturation. Mutation of highly conserved amino acids in YbeY, allowed the identification of two residues (H114, R59) that were found to have a significant effect in vivo. We discuss the implications of these findings for rRNA maturation and ribosome assembly in bacteria.
Description
available in PMC 2011 October 1.
MIT Department
Massachusetts Institute of Technology. Department of Biology
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Creative Commons Attribution-Noncommercial-Share Alike 3.0
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DOI of Published Version
https://doi.org/10.1111/j.1365-2958.2010.07351.x
