Nouvelles perspectives concernant la structure et la fonction du domaine carboxyl terminal de Hfq
| Autor: | Sylvain Trépout, Emilie Fortas, Antoine Malabirade, Sergio Marco, Valeria Militello, Aziz Taghbalout, Federica Piccirilli, Véronique Arluison |
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| Přispěvatelé: | Laboratoire Léon Brillouin (LLB - UMR 12), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Università degli studi di Palermo - University of Palermo, Université Paris-Sud - Paris 11 (UP11), Chimie, Modélisation et Imagerie pour la Biologie [Orsay], 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), 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), Fortas, E, Piccirilli, F, Malabirade, A, Militello, V, Trepout, S, Marco, S, Taghbalout, A, Arluison, V |
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
IDP
intrinsically-disordered proteins lcsh:Life lcsh:QR1-502 sub-membrane macromolecular assembly Plasma protein binding sRNA small non-coding RNA Biochemistry lcsh:Microbiology amyloid fibrils Protein biosynthesis 0303 health sciences [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] Escherichia coli Proteins 030302 biochemistry & molecular biology HfqCTRp Hfq C-terminal peptide FTIR Fourier transform infrared spectroscopy NTR N-terminal region Compartmentalization (psychology) Cell biology [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biophysics RNA Bacterial small non-coding ribonucleic acid (RNA) FSD Fourier self-deconvolution Transfer RNA Amyloid fibril Protein Binding Biophysics Biology Host Factor 1 Protein 03 medical and health sciences Escherichia coli ThT thioflavin T [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Protein Structure Quaternary ncRNA regulatory non-coding RNA Post-transcriptional regulation Molecular Biology 030304 developmental biology Original Paper C-terminus RNA [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology Cell Biology cellular compartmentalization WT wild-type Protein Structure Tertiary lcsh:QH501-531 CTR Hfq C-terminal region ribonucleic acid (RNA) processing and degradation Biophysic post-transcriptional regulation |
| Zdroj: | Bioscience Reports, Vol 35, Iss 2, p e00190 (2015) Bioscience Reports Bioscience Reports, 2015, 112, pp.531-9. ⟨10.1042/BSR20140128⟩ |
| ISSN: | 1573-4935 0144-8463 |
| DOI: | 10.1042/BSR20140128⟩ |
| Popis: | 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. We showed that Hfq C-terminal region (CTR) has an intrinsic property to self-assemble into amyloid-like fibrils. This region is required for cellular assembly of Hfq into membrane-associated coiled structures. The work establishes a new function for this naturally unstructured Hfq domain. |
| Databáze: | OpenAIRE |
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