Nouvelles perspectives concernant la structure et la fonction du domaine carboxyl terminal de Hfq

Autor: Fortas, Emilie, Piccirilli, Federica, Malabirade, Antoine, Militello, Valeria, Trépout, Sylvain, Marco, Sergio, Taghbalout, Aziz, Arluison, Véronique
Přispěvatelé: Laboratoire Léon Brillouin (LLB - UMR 12), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay, Department of Physics - University of Palermo, Università degli studi di Palermo - University of Palermo, Université Paris-Sud - Paris 11 (UP11), Chimie, Modélisation et Imagerie pour la Biologie [Orsay], Institut de Chimie du CNRS (INC)-Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Curie [Paris], University of Connecticut (UCONN), Université Paris Diderot - Paris 7 (UPD7), CNRS, CEA, National Institute of Health [grant number R37 GM060632], Université Paris Diderot, Université Paris Sud, European Project: 223431,EC:FP7:HEALTH,FP7-HEALTH-2007-B,DIVINOCELL(2009), Malabirade, Antoine, Exploiting Gram-negative cell division targets in the test tube to obtain anti-microbial compounds - DIVINOCELL - - EC:FP7:HEALTH2009-03-01 - 2013-08-31 - 223431 - VALID, Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Université Paris-Sud - Paris 11 (UP11)-Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)
Jazyk: angličtina
Rok vydání: 2015
Předmět:
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
[SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
[SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biophysics
sub-membrane macromolecular assembly
[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Molecular biology
[SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry
Molecular Biology/Molecular biology
cellular compartmentalization
[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biophysics
amyloid fibrils
small non-coding ribonucleic acid (RNA)
ribonucleic acid (RNA) processing and degradation
[SDV.BBM] Life Sciences [q-bio]/Biochemistry
Molecular Biology
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
post-transcriptional regulation
Zdroj: Bioscience Reports
Bioscience Reports, Portland Press, 2015, 112, pp.531-9. ⟨10.1042/BSR20140128⟩
Bioscience Reports, 2015, 112, pp.531-9. ⟨10.1042/BSR20140128⟩
ISSN: 0144-8463
1573-4935
DOI: 10.1042/BSR20140128⟩
Popis: International audience; 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 com-partmentalization 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.
Databáze: OpenAIRE
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