Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
AuthorsGonzalez, Grecia M
Hardwick, Steven W
Maslen, Sarah L
Skehel, J Mark
Luisi, Ben F
Broadhurst, R William
MetadataShow full item record
AbstractThe 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.
CitationStructure of the Escherichia coli ProQ RNA-binding protein. 2017, 23 (5):696-711 RNA
AffiliationHelmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.
JournalRNA (New York, N.Y.)
The following license files are associated with this item:
- Creative Commons
Except where otherwise noted, this item's license is described as http://creativecommons.org/licenses/by-nc-sa/4.0/
- Determinants of RNA recognition by the FinO domain of the Escherichia coli ProQ protein.
- Authors: Stein EM, Kwiatkowska J, Basczok MM, Gravel CM, Berry KE, Olejniczak M
- Issue date: 2020 Jul 27
- Genetic identification of the functional surface for RNA binding by Escherichia coli ProQ.
- Authors: Pandey S, Gravel CM, Stockert OM, Wang CD, Hegner CL, LeBlanc H, Berry KE
- Issue date: 2020 May 7
- Solution structure and RNA-binding of a minimal ProQ-homolog from Legionella pneumophila (Lpp1663).
- Authors: Immer C, Hacker C, Wöhnert J
- Issue date: 2020 Dec
- Biochemical and genetic dissection of the RNA-binding surface of the FinO domain of Escherichia coli ProQ.
- Authors: Stein EM, Wang S, Dailey KG, Gravel CM, Wang S, Olejniczak M, Berry KE
- Issue date: 2023 Nov
- ProQ is an RNA chaperone that controls ProP levels in Escherichia coli.
- Authors: Chaulk SG, Smith Frieday MN, Arthur DC, Culham DE, Edwards RA, Soo P, Frost LS, Keates RA, Glover JN, Wood JM
- Issue date: 2011 Apr 19