Skip to content
Back to outputs

The low-resolution solution structure of Vibrio cholerae Hfq in complex with Qrr1 sRNA

Research output: Contribution to journalArticle

Standard

The low-resolution solution structure of Vibrio cholerae Hfq in complex with Qrr1 sRNA. / Vincent, H.; Henderson, Charlotte; Stone, C.; Cary, Peter; Gowers, Darren; Sobott, F.; Taylor, James E.; Callaghan, Anastasia.

In: Nucleic Acids Research, Vol. 40, No. 17, 2012, p. 8698-8710.

Research output: Contribution to journalArticle

Harvard

APA

Vancouver

Author

Vincent, H. ; Henderson, Charlotte ; Stone, C. ; Cary, Peter ; Gowers, Darren ; Sobott, F. ; Taylor, James E. ; Callaghan, Anastasia. / The low-resolution solution structure of Vibrio cholerae Hfq in complex with Qrr1 sRNA. In: Nucleic Acids Research. 2012 ; Vol. 40, No. 17. pp. 8698-8710.

Bibtex

@article{bc9c6cbaa4c2469bbb3d8cc7afd811b4,
title = "The low-resolution solution structure of Vibrio cholerae Hfq in complex with Qrr1 sRNA",
abstract = "In Vibrio cholerae, the RNA binding protein and chaperone Hfq (VcHfq) facilitates the pairing of the quorum regulatory RNA (Qrr) small regulatory RNAs (sRNAs) to the 5′ untranslated regions of the mRNAs for a number of global regulators that modulate the expression of virulence genes. This Qrr-mediated sRNA circuit is an attractive antimicrobial target, but characterization at the molecular level is required for this to be realized. Here, we investigate the interactions between VcHfq and the Qrr sRNAs using a variety of biochemical and biophysical techniques. We show that the ring-shaped VcHfq hexamer binds the Qrrs with 1:1 stoichiometry through its proximal face, and the molecular envelope of the VcHfq-Qrr complex is experimentally determined from small angle scattering data to present the first structural glimpse of a Hfq-sRNA complex. This structure reveals that the VcHfq protein does not change shape on complex formation but the RNA does, suggesting that a chaperone role for VcHfq is a critical part of the VcHfq-Qrr interaction. Overall, these studies enhance our understanding of VcHfq-Qrr interactions.",
author = "H. Vincent and Charlotte Henderson and C. Stone and Peter Cary and Darren Gowers and F. Sobott and Taylor, {James E.} and Anastasia Callaghan",
year = "2012",
doi = "10.1093/nar/gks582",
language = "English",
volume = "40",
pages = "8698--8710",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "17",

}

RIS

TY - JOUR

T1 - The low-resolution solution structure of Vibrio cholerae Hfq in complex with Qrr1 sRNA

AU - Vincent, H.

AU - Henderson, Charlotte

AU - Stone, C.

AU - Cary, Peter

AU - Gowers, Darren

AU - Sobott, F.

AU - Taylor, James E.

AU - Callaghan, Anastasia

PY - 2012

Y1 - 2012

N2 - In Vibrio cholerae, the RNA binding protein and chaperone Hfq (VcHfq) facilitates the pairing of the quorum regulatory RNA (Qrr) small regulatory RNAs (sRNAs) to the 5′ untranslated regions of the mRNAs for a number of global regulators that modulate the expression of virulence genes. This Qrr-mediated sRNA circuit is an attractive antimicrobial target, but characterization at the molecular level is required for this to be realized. Here, we investigate the interactions between VcHfq and the Qrr sRNAs using a variety of biochemical and biophysical techniques. We show that the ring-shaped VcHfq hexamer binds the Qrrs with 1:1 stoichiometry through its proximal face, and the molecular envelope of the VcHfq-Qrr complex is experimentally determined from small angle scattering data to present the first structural glimpse of a Hfq-sRNA complex. This structure reveals that the VcHfq protein does not change shape on complex formation but the RNA does, suggesting that a chaperone role for VcHfq is a critical part of the VcHfq-Qrr interaction. Overall, these studies enhance our understanding of VcHfq-Qrr interactions.

AB - In Vibrio cholerae, the RNA binding protein and chaperone Hfq (VcHfq) facilitates the pairing of the quorum regulatory RNA (Qrr) small regulatory RNAs (sRNAs) to the 5′ untranslated regions of the mRNAs for a number of global regulators that modulate the expression of virulence genes. This Qrr-mediated sRNA circuit is an attractive antimicrobial target, but characterization at the molecular level is required for this to be realized. Here, we investigate the interactions between VcHfq and the Qrr sRNAs using a variety of biochemical and biophysical techniques. We show that the ring-shaped VcHfq hexamer binds the Qrrs with 1:1 stoichiometry through its proximal face, and the molecular envelope of the VcHfq-Qrr complex is experimentally determined from small angle scattering data to present the first structural glimpse of a Hfq-sRNA complex. This structure reveals that the VcHfq protein does not change shape on complex formation but the RNA does, suggesting that a chaperone role for VcHfq is a critical part of the VcHfq-Qrr interaction. Overall, these studies enhance our understanding of VcHfq-Qrr interactions.

U2 - 10.1093/nar/gks582

DO - 10.1093/nar/gks582

M3 - Article

VL - 40

SP - 8698

EP - 8710

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 17

ER -

ID: 172895