| Autor: |
Gonzalez, G, Hardwick, S, Maslen, SL, Skehel, JM, Holmqvist, E, Vogel, J, Bateman, A, Luisi, B, Broadhurst, RW |
| Přispěvatelé: |
Hardwick, Steven [0000-0001-9246-1864], Luisi, Ben [0000-0003-1144-9877], Broadhurst, Bill [0000-0002-0264-4593], Apollo - University of Cambridge Repository |
| Jazyk: |
angličtina |
| Rok vydání: |
2017 |
| Předmět: |
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| DOI: |
10.17863/cam.9242 |
| Popis: |
The protein ProQ has recently been identified as a global RNA chaperone in $\textit{Salmonella}$, and a similar role is anticipated for its numerous homologues in divergent bacterial species. We report the solution structure of $\textit{Escherichia coli}$ 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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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