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Hfq binding changes the structure of Escherichia coli small noncoding RNAs OxyS and RprA, which are involved in the riboregulation of rpoS

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Hfq binding changes the structure of Escherichia coli small noncoding RNAs OxyS and RprA, which are involved in the riboregulation of rpoS. / Henderson, Charlotte; Vincent, H.; Casamento, A.; Stone, Carlanne; Phillips, Jack; Cary, Peter; Sobott, F.; Gowers, Darren; Taylor, James E.; Callaghan, Anastasia.

In: RNA, Vol. 19, No. 8, 08.2013, p. 1089-1104.

Research output: Contribution to journalArticlepeer-review

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Henderson, Charlotte ; Vincent, H. ; Casamento, A. ; Stone, Carlanne ; Phillips, Jack ; Cary, Peter ; Sobott, F. ; Gowers, Darren ; Taylor, James E. ; Callaghan, Anastasia. / Hfq binding changes the structure of Escherichia coli small noncoding RNAs OxyS and RprA, which are involved in the riboregulation of rpoS. In: RNA. 2013 ; Vol. 19, No. 8. pp. 1089-1104.

Bibtex

@article{811ec4efc09d4aa5bf0f5cc90b3a6a8f,
title = "Hfq binding changes the structure of Escherichia coli small noncoding RNAs OxyS and RprA, which are involved in the riboregulation of rpoS",
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 Hfq–sRNA 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.",
keywords = "APC-PAID, RCUK, BBSRC",
author = "Charlotte Henderson and H. Vincent and A. Casamento and Carlanne Stone and Jack Phillips and Peter Cary and F. Sobott and Darren Gowers and Taylor, {James E.} and Anastasia Callaghan",
note = "{\textcopyright} 2013; Published by Cold Spring Harbor Laboratory Press for the RNA Society",
year = "2013",
month = aug,
doi = "10.1261/rna.034595.112",
language = "English",
volume = "19",
pages = "1089--1104",
journal = "RNA",
issn = "1355-8382",
publisher = "Cold Spring Harbor Laboratory Press",
number = "8",

}

RIS

TY - JOUR

T1 - Hfq binding changes the structure of Escherichia coli small noncoding RNAs OxyS and RprA, which are involved in the riboregulation of rpoS

AU - Henderson, Charlotte

AU - Vincent, H.

AU - Casamento, A.

AU - Stone, Carlanne

AU - Phillips, Jack

AU - Cary, Peter

AU - Sobott, F.

AU - Gowers, Darren

AU - Taylor, James E.

AU - Callaghan, Anastasia

N1 - © 2013; Published by Cold Spring Harbor Laboratory Press for the RNA Society

PY - 2013/8

Y1 - 2013/8

N2 - 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 Hfq–sRNA 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.

AB - 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 Hfq–sRNA 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.

KW - APC-PAID

KW - RCUK

KW - BBSRC

U2 - 10.1261/rna.034595.112

DO - 10.1261/rna.034595.112

M3 - Article

VL - 19

SP - 1089

EP - 1104

JO - RNA

JF - RNA

SN - 1355-8382

IS - 8

ER -

ID: 224206