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Structure of the Escherichia coli ProQ RNA-binding protein.


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.

SUBMITTER: Gonzalez GM 

PROVIDER: S-EPMC5393179 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature

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Structure of the <i>Escherichia coli</i> ProQ RNA-binding protein.

Gonzalez Grecia M GM   Hardwick Steven W SW   Maslen Sarah L SL   Skehel J Mark JM   Holmqvist Erik E   Vogel Jörg J   Bateman Alex A   Luisi Ben F BF   Broadhurst R William RW  

RNA (New York, N.Y.) 20170213 5


The protein ProQ has recently been identified as a global small noncoding RNA-binding protein in <i>Salmonella</i>, and a similar role is anticipated for its numerous homologs in divergent bacterial species. We report the solution structure of <i>Escherichia coli</i> 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  ...[more]

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