Publication
Title
Hfq binding changes the structure of **Escherichia coli** small noncoding RNAs OxyS and RprA, which are involved in the riboregulation of rpoS
Author
Abstract
OxyS and RprA are two small noncoding RNAs (sRNAs) that modulate the expression of rpoS, encoding an alternative sigma factor that activates transcription of multiple Escherichia coli stress-response genes. While RprA activates rpoS for translation, OxyS down-regulates the transcript. Crucially, the RNA binding protein Hfq is required for both sRNAs to function, although the specific role played by Hfq remains unclear. We have investigated RprA and OxyS interactions with Hfq using biochemical and biophysical approaches. In particular, we have obtained the molecular envelopes of the HfqsRNA complexes using small-angle scattering methods, which reveal key molecular details. These data indicate that Hfq does not substantially change shape upon complex formation, whereas the sRNAs do. We link the impact of Hfq binding, and the sRNA structural changes induced, to transcript stability with respect to RNase E degradation. In light of these findings, we discuss the role of Hfq in the opposing regulatory functions played by RprA and OxyS in rpoS regulation.
Language
English
Source (journal)
RNA / RNA Society. - New York, N.Y., 1995, currens
Publication
New York, N.Y. : 2013
ISSN
1355-8382
1469-9001 [online]
DOI
10.1261/RNA.034595.112
Volume/pages
19 :8 (2013) , p. 1089-1104
ISI
000321834600007
Full text (Publisher's DOI)
Full text (publisher's version - intranet only)
UAntwerpen
Faculty/Department
Research group
Project info
Determination of subunit composition and architecture of supramolecular and biological complexes using mass spectrometry coupled with ion mobility spectroscopy and allied techniques.
Publication type
Subject
Affiliation
Publications with a UAntwerp address
External links
Web of Science
Record
Identifier
Creation 14.11.2013
Last edited 25.05.2022
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