| Autor: |
Grecia M, Gonzalez, Steven W, Hardwick, Sarah L, Maslen, J Mark, Skehel, Erik, Holmqvist, Jörg, Vogel, Alex, Bateman, Ben F, Luisi, R William, Broadhurst |
| Rok vydání: |
2016 |
| Předmět: |
|
| Zdroj: |
RNA (New York, N.Y.). 23(5) |
| ISSN: |
1469-9001 |
| Popis: |
The protein ProQ has recently been identified as a global small noncoding RNA-binding protein in Salmonella, and a similar role is anticipated for its numerous homologs 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 intradomain 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 modeled 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 recognize complex RNA structures and serve to promote RNA-mediated regulation. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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