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Structure of the Escherichia coli ProQ RNA-binding protein.
Gonzalez, Grecia M Hardwick, Steven W Maslen, Sarah L Skehel, J Mark Holmqvist, Erik Bateman, Alex Luisi, Ben F Broadhurst, R William
Gonzalez, Grecia M
Hardwick, Steven W
Maslen, Sarah L
Skehel, J Mark
Holmqvist, Erik
Bateman, Alex
Luisi, Ben F
Broadhurst, R William
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2017-05
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Abstract
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.
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Structure of the Escherichia coli ProQ RNA-binding protein. 2017, 23 (5):696-711 RNA
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en
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1469-9001