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Structure of the $\textit{Escherichia coli}$ ProQ RNA chaperone protein

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Gonzalez, G 
Maslen, SL 
Skehel, JM 
Holmqvist, E 


The protein ProQ has recently been identified as a global RNA chaperone in Salmonella, and a similar role is anticipated for its numerous homologues in divergent bacterial species. We report the solution structure of Escherichia coli ProQ, revealing an N-terminal FinO-like domain, a C-terminal domain that unexpectedly has a Tudor-domain fold commonly found in eukaryotes, and an elongated bridging intra-domain linker that is flexible but nonetheless incompressible. Structure based sequence analysis suggests that the Tudor domain was acquired through horizontal gene transfer and gene fusion to the ancestral FinO-like domain. Through a combination of biochemical and biophysical approaches, we have mapped putative RNA binding surfaces on all three domains of ProQ and modelled the protein's conformation in the apo and RNA-bound forms. Taken together, these data suggest how the FinO, Tudor and linker domains of ProQ cooperate to recognise complex RNA structures and serve to promote RNA-mediated regulation.



FinO, RNA chaperone, protein-RNA interactions, regulatory RNA, riboregulation

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Cold Spring Harbor
Wellcome Trust (094229/Z/10/Z)
Wellcome Trust (200873/Z/16/Z)
G.M.G. was supported by a Gates Cambridge Scholarship. B.F.L., G.M.G., and S.W.H. are supported by the Wellcome Trust.