2.50
Hdl Handle:
http://hdl.handle.net/10033/621016
Title:
Structure of the Escherichia coli ProQ RNA-binding protein.
Authors:
Gonzalez, Grecia M; Hardwick, Steven W; Maslen, Sarah L; Skehel, J Mark; Holmqvist, Erik; Vogel, Jörg; Bateman, Alex; Luisi, Ben F; Broadhurst, R William
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.
Affiliation:
Helmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.
Citation:
Structure of the Escherichia coli ProQ RNA-binding protein. 2017, 23 (5):696-711 RNA
Journal:
RNA (New York, N.Y.)
Issue Date:
May-2017
URI:
http://hdl.handle.net/10033/621016
DOI:
10.1261/rna.060343.116
PubMed ID:
28193673
Type:
Article
Language:
en
ISSN:
1469-9001
Appears in Collections:
Publications of the AG (ESME)

Full metadata record

DC FieldValue Language
dc.contributor.authorGonzalez, Grecia Men
dc.contributor.authorHardwick, Steven Wen
dc.contributor.authorMaslen, Sarah Len
dc.contributor.authorSkehel, J Marken
dc.contributor.authorHolmqvist, Eriken
dc.contributor.authorVogel, Jörgen
dc.contributor.authorBateman, Alexen
dc.contributor.authorLuisi, Ben Fen
dc.contributor.authorBroadhurst, R Williamen
dc.date.accessioned2017-07-21T08:29:01Z-
dc.date.available2017-07-21T08:29:01Z-
dc.date.issued2017-05-
dc.identifier.citationStructure of the Escherichia coli ProQ RNA-binding protein. 2017, 23 (5):696-711 RNAen
dc.identifier.issn1469-9001-
dc.identifier.pmid28193673-
dc.identifier.doi10.1261/rna.060343.116-
dc.identifier.urihttp://hdl.handle.net/10033/621016-
dc.description.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.en
dc.language.isoenen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.mesh3' Untranslated Regionsen
dc.subject.meshBinding Sitesen
dc.subject.meshEscherichia coli Proteinsen
dc.subject.meshHost Factor 1 Proteinen
dc.subject.meshModels, Molecularen
dc.subject.meshNuclear Magnetic Resonance, Biomolecularen
dc.subject.meshProtein Domainsen
dc.subject.meshRNA-Binding Proteinsen
dc.titleStructure of the Escherichia coli ProQ RNA-binding protein.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.en
dc.identifier.journalRNA (New York, N.Y.)en

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