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Bacterial RNA Degradosomes: Molecular Machines under Tight Control.
Tejada-Arranz, Alejandro; de Crécy-Lagard, Valérie; de Reuse, Hilde.
Affiliation
  • Tejada-Arranz A; Helicobacter Pathogenesis Unit, Department of Microbiology, Institut Pasteur, Paris, France; Université Paris Diderot, Sorbonne Paris Cité, Paris, France.
  • de Crécy-Lagard V; Department of Microbiology and Cell Science, University of Florida, Gainesville, FL, USA; University of Florida Genetics Institute, Gainesville, FL, USA.
  • de Reuse H; Helicobacter Pathogenesis Unit, Department of Microbiology, Institut Pasteur, Paris, France. Electronic address: hdereuse@pasteur.fr.
Trends Biochem Sci ; 45(1): 42-57, 2020 01.
Article in En | MEDLINE | ID: mdl-31679841
ABSTRACT
Bacterial RNA degradosomes are multienzyme molecular machines that act as hubs for post-transcriptional regulation of gene expression. The ribonuclease activities of these complexes require tight regulation, as they are usually essential for cell survival while potentially destructive. Recent studies have unveiled a wide variety of regulatory mechanisms including autoregulation, post-translational modifications, and protein compartmentalization. Recently, the subcellular organization of bacterial RNA degradosomes was found to present similarities with eukaryotic messenger ribonucleoprotein (mRNP) granules, membraneless compartments that are also involved in mRNA and protein storage and/or mRNA degradation. In this review, we present the current knowledge on the composition and targets of RNA degradosomes, the most recent developments regarding the regulation of these machineries, and their similarities with the eukaryotic mRNP granules.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Polyribonucleotide Nucleotidyltransferase / RNA, Bacterial / RNA Helicases / Endoribonucleases / Multienzyme Complexes Language: En Journal: Trends Biochem Sci Year: 2020 Type: Article Affiliation country: France

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Polyribonucleotide Nucleotidyltransferase / RNA, Bacterial / RNA Helicases / Endoribonucleases / Multienzyme Complexes Language: En Journal: Trends Biochem Sci Year: 2020 Type: Article Affiliation country: France