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Structure of the Escherichia coli ProQ RNA-binding protein
Univ Cambridge, Dept Biochem, Cambridge CB2 1GA, England..
Univ Cambridge, Dept Biochem, Cambridge CB2 1GA, England..
MRC Lab Mol Biol, Cambridge CB2 0QH, England..
MRC Lab Mol Biol, Cambridge CB2 0QH, England..
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2017 (English)In: RNA: A publication of the RNA Society, ISSN 1355-8382, E-ISSN 1469-9001, Vol. 23, no 5, 696-711 p.Article in journal (Refereed) Published
Abstract [en]

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 call 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.

Place, publisher, year, edition, pages
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT , 2017. Vol. 23, no 5, 696-711 p.
Keyword [en]
protein-RNA interactions, regulatory RNA, riboregulation, FinO, ProQ, RNA chaperone
National Category
Basic Medicine
Identifiers
URN: urn:nbn:se:uu:diva-322710DOI: 10.1261/rna.060343.116ISI: 000400123100009PubMedID: 28193673OAI: oai:DiVA.org:uu-322710DiVA: diva2:1100915
Funder
Wellcome trust
Available from: 2017-05-29 Created: 2017-05-29 Last updated: 2017-05-29Bibliographically approved

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