New insight into the structure and function of Hfq C-terminus

Valeria Militello, Federica Piccirilli, Veronique Arluison, Véronique Arluison, Sergio Marco, Aziz Taghbalout, Sylvain Trépout, Emilie Fortas, Antoine Malabirade

Risultato della ricerca: Article

17 Citazioni (Scopus)

Abstract

Accumulating evidence indicates that RNA metabolism components assemble into supramolecular cellular structures to mediate functional compartmentalization within the cytoplasmic membrane of the bacterial cell. This cellular compartmentalization could play important roles in the processes of RNA degradation and maturation. These components include Hfq, the RNA chaperone protein, which is involved in the post-transcriptional control of protein synthesis mainly by the virtue of its interactions with several small regulatory ncRNAs (sRNA). The Escherichia coli Hfq is structurally organized into two domains. An N-terminal domain that folds as strongly bent β-sheets within individual protomers to assemble into a typical toroidal hexameric ring. A C-terminal flexible domain that encompasses approximately one-third of the protein seems intrinsically unstructured. RNA-binding function of Hfq mainly lies within its N-terminal core, whereas the function of the flexible domain remains controversial and largely unknown. In the present study, we demonstrate that the Hfq-C-terminal region (CTR) has an intrinsic property to self-assemble into long amyloid-like fibrillar structures in vitro. We show that normal localization of Hfq within membrane-associated coiled structures in vivo requires this C-terminal domain. This finding establishes for the first time a function for the hitherto puzzling CTR, with a plausible central role in RNA transactions.
Lingua originaleEnglish
pagine (da-a)1-9
Numero di pagine9
RivistaBioscience Reports
Volume35
Stato di pubblicazionePublished - 2015

Fingerprint

RNA
Proteins
RNA Stability
Protein Subunits
Membranes
Cellular Structures
Amyloid
Metabolism
Escherichia coli
Cell Membrane
Degradation
beta-Strand Protein Conformation
In Vitro Techniques

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Cell Biology
  • Molecular Biology
  • Biochemistry

Cita questo

Militello, V., Piccirilli, F., Arluison, V., Arluison, V., Marco, S., Taghbalout, A., ... Malabirade, A. (2015). New insight into the structure and function of Hfq C-terminus. Bioscience Reports, 35, 1-9.

New insight into the structure and function of Hfq C-terminus. / Militello, Valeria; Piccirilli, Federica; Arluison, Veronique; Arluison, Véronique; Marco, Sergio; Taghbalout, Aziz; Trépout, Sylvain; Fortas, Emilie; Malabirade, Antoine.

In: Bioscience Reports, Vol. 35, 2015, pag. 1-9.

Risultato della ricerca: Article

Militello, V, Piccirilli, F, Arluison, V, Arluison, V, Marco, S, Taghbalout, A, Trépout, S, Fortas, E & Malabirade, A 2015, 'New insight into the structure and function of Hfq C-terminus', Bioscience Reports, vol. 35, pagg. 1-9.
Militello, Valeria ; Piccirilli, Federica ; Arluison, Veronique ; Arluison, Véronique ; Marco, Sergio ; Taghbalout, Aziz ; Trépout, Sylvain ; Fortas, Emilie ; Malabirade, Antoine. / New insight into the structure and function of Hfq C-terminus. In: Bioscience Reports. 2015 ; Vol. 35. pagg. 1-9.
@article{c91dcd89f16f41c6a33fb9c6d6e99c73,
title = "New insight into the structure and function of Hfq C-terminus",
abstract = "Accumulating evidence indicates that RNA metabolism components assemble into supramolecular cellular structures to mediate functional compartmentalization within the cytoplasmic membrane of the bacterial cell. This cellular compartmentalization could play important roles in the processes of RNA degradation and maturation. These components include Hfq, the RNA chaperone protein, which is involved in the post-transcriptional control of protein synthesis mainly by the virtue of its interactions with several small regulatory ncRNAs (sRNA). The Escherichia coli Hfq is structurally organized into two domains. An N-terminal domain that folds as strongly bent β-sheets within individual protomers to assemble into a typical toroidal hexameric ring. A C-terminal flexible domain that encompasses approximately one-third of the protein seems intrinsically unstructured. RNA-binding function of Hfq mainly lies within its N-terminal core, whereas the function of the flexible domain remains controversial and largely unknown. In the present study, we demonstrate that the Hfq-C-terminal region (CTR) has an intrinsic property to self-assemble into long amyloid-like fibrillar structures in vitro. We show that normal localization of Hfq within membrane-associated coiled structures in vivo requires this C-terminal domain. This finding establishes for the first time a function for the hitherto puzzling CTR, with a plausible central role in RNA transactions.",
keywords = "Amyloid fibrils; Cellular compartmentalization; Post-transcriptional regulation; Ribonucleic acid (RNA) processing and degradation; Small non-coding ribonucleic acid (RNA); Sub-membrane macromolecular assembly; Biophysics; Biochemistry; Molecular Biology; Cell Biology",
author = "Valeria Militello and Federica Piccirilli and Veronique Arluison and V{\'e}ronique Arluison and Sergio Marco and Aziz Taghbalout and Sylvain Tr{\'e}pout and Emilie Fortas and Antoine Malabirade",
year = "2015",
language = "English",
volume = "35",
pages = "1--9",
journal = "Bioscience Reports",
issn = "0144-8463",
publisher = "Portland Press Ltd.",

}

TY - JOUR

T1 - New insight into the structure and function of Hfq C-terminus

AU - Militello, Valeria

AU - Piccirilli, Federica

AU - Arluison, Veronique

AU - Arluison, Véronique

AU - Marco, Sergio

AU - Taghbalout, Aziz

AU - Trépout, Sylvain

AU - Fortas, Emilie

AU - Malabirade, Antoine

PY - 2015

Y1 - 2015

N2 - Accumulating evidence indicates that RNA metabolism components assemble into supramolecular cellular structures to mediate functional compartmentalization within the cytoplasmic membrane of the bacterial cell. This cellular compartmentalization could play important roles in the processes of RNA degradation and maturation. These components include Hfq, the RNA chaperone protein, which is involved in the post-transcriptional control of protein synthesis mainly by the virtue of its interactions with several small regulatory ncRNAs (sRNA). The Escherichia coli Hfq is structurally organized into two domains. An N-terminal domain that folds as strongly bent β-sheets within individual protomers to assemble into a typical toroidal hexameric ring. A C-terminal flexible domain that encompasses approximately one-third of the protein seems intrinsically unstructured. RNA-binding function of Hfq mainly lies within its N-terminal core, whereas the function of the flexible domain remains controversial and largely unknown. In the present study, we demonstrate that the Hfq-C-terminal region (CTR) has an intrinsic property to self-assemble into long amyloid-like fibrillar structures in vitro. We show that normal localization of Hfq within membrane-associated coiled structures in vivo requires this C-terminal domain. This finding establishes for the first time a function for the hitherto puzzling CTR, with a plausible central role in RNA transactions.

AB - Accumulating evidence indicates that RNA metabolism components assemble into supramolecular cellular structures to mediate functional compartmentalization within the cytoplasmic membrane of the bacterial cell. This cellular compartmentalization could play important roles in the processes of RNA degradation and maturation. These components include Hfq, the RNA chaperone protein, which is involved in the post-transcriptional control of protein synthesis mainly by the virtue of its interactions with several small regulatory ncRNAs (sRNA). The Escherichia coli Hfq is structurally organized into two domains. An N-terminal domain that folds as strongly bent β-sheets within individual protomers to assemble into a typical toroidal hexameric ring. A C-terminal flexible domain that encompasses approximately one-third of the protein seems intrinsically unstructured. RNA-binding function of Hfq mainly lies within its N-terminal core, whereas the function of the flexible domain remains controversial and largely unknown. In the present study, we demonstrate that the Hfq-C-terminal region (CTR) has an intrinsic property to self-assemble into long amyloid-like fibrillar structures in vitro. We show that normal localization of Hfq within membrane-associated coiled structures in vivo requires this C-terminal domain. This finding establishes for the first time a function for the hitherto puzzling CTR, with a plausible central role in RNA transactions.

KW - Amyloid fibrils; Cellular compartmentalization; Post-transcriptional regulation; Ribonucleic acid (RNA) processing and degradation; Small non-coding ribonucleic acid (RNA); Sub-membrane macromolecular assembly; Biophysics; Biochemistry; Molecular Biology;

UR - http://hdl.handle.net/10447/227552

UR - http://www.bioscirep.org/bsr/035/e190/035e190.pdf

M3 - Article

VL - 35

SP - 1

EP - 9

JO - Bioscience Reports

JF - Bioscience Reports

SN - 0144-8463

ER -