Structural highlights
Function
[PROQ_ECO45] RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism.
Publication Abstract from PubMed
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.
Structure of the Escherichia coli ProQ RNA-binding protein.,Gonzalez GM, Hardwick SW, Maslen SL, Skehel JM, Holmqvist E, Vogel J, Bateman A, Luisi BF, Broadhurst RW RNA. 2017 May;23(5):696-711. doi: 10.1261/rna.060343.116. Epub 2017 Feb 13. PMID:28193673[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gonzalez GM, Hardwick SW, Maslen SL, Skehel JM, Holmqvist E, Vogel J, Bateman A, Luisi BF, Broadhurst RW. Structure of the Escherichia coli ProQ RNA-binding protein. RNA. 2017 May;23(5):696-711. doi: 10.1261/rna.060343.116. Epub 2017 Feb 13. PMID:28193673 doi:http://dx.doi.org/10.1261/rna.060343.116
