In:
RNA, Cold Spring Harbor Laboratory, Vol. 23, No. 5 ( 2017-05), p. 696-711
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.
Type of Medium:
Online Resource
ISSN:
1355-8382
,
1469-9001
DOI:
10.1261/rna.060343.116
Language:
English
Publisher:
Cold Spring Harbor Laboratory
Publication Date:
2017
detail.hit.zdb_id:
1475737-0
SSG:
12
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