Crucial Role of the C-Terminal Domain of Hfq Protein in Genomic Instability

G-rich DNA repeats that can form G-quadruplex structures are prevalent in bacterial genomes and are frequently associated with regulatory regions of genes involved in virulence, antigenic variation, and antibiotic resistance. These sequences are also inherently mutagenic and can lead to changes affe...

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Main Authors: Virali J. Parekh, Frank Wien, Wilfried Grange, Thomas A. De Long, Véronique Arluison, Richard R. Sinden
Format: Article
Language:English
Published: MDPI AG 2020-10-01
Series:Microorganisms
Subjects:
Online Access:https://www.mdpi.com/2076-2607/8/10/1598
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author Virali J. Parekh
Frank Wien
Wilfried Grange
Thomas A. De Long
Véronique Arluison
Richard R. Sinden
author_facet Virali J. Parekh
Frank Wien
Wilfried Grange
Thomas A. De Long
Véronique Arluison
Richard R. Sinden
author_sort Virali J. Parekh
collection DOAJ
description G-rich DNA repeats that can form G-quadruplex structures are prevalent in bacterial genomes and are frequently associated with regulatory regions of genes involved in virulence, antigenic variation, and antibiotic resistance. These sequences are also inherently mutagenic and can lead to changes affecting cell survival and adaptation. Transcription of the G-quadruplex-forming repeat (G<sub>3</sub>T)<sub>n</sub> in <i>E. coli</i>, when mRNA comprised the G-rich strand, promotes G-quadruplex formation in DNA and increases rates of deletion of G-quadruplex-forming sequences. The genomic instability of G-quadruplex repeats may be a source of genetic variability that can influence alterations and evolution of bacteria. The DNA chaperone Hfq is involved in the genetic instability of these G-quadruplex sequences. Inactivation of the <i>hfq</i> gene decreases the genetic instability of G-quadruplex, demonstrating that the genomic instability of this regulatory element can be influenced by the <i>E. coli</i> highly pleiotropic Hfq protein, which is involved in small noncoding RNA regulation pathways, and DNA organization and packaging. We have shown previously that the protein binds to and stabilizes these sequences, increasing rates of their genomic instability. Here, we extend this analysis to characterize the role of the C-terminal domain of Hfq protein in interaction with G-quadruplex structures. This allows to better understand the function of this specific region of the Hfq protein in genomic instability.
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spelling doaj.art-3513b0ab13a14f6eba9748022402cdbd2023-11-20T17:28:09ZengMDPI AGMicroorganisms2076-26072020-10-01810159810.3390/microorganisms8101598Crucial Role of the C-Terminal Domain of Hfq Protein in Genomic InstabilityVirali J. Parekh0Frank Wien1Wilfried Grange2Thomas A. De Long3Véronique Arluison4Richard R. Sinden5Laboratory of DNA Structure and Mutagenesis, Department of Biology, Chemistry and Health Sciences, South Dakota School of Mines and Technology, Rapid City, SD 57701, USASynchrotron SOLEIL, 91192 Gif-sur-Yvette, FranceInstitut de Physique et Chimie des Matériaux de Strasbourg (IPCMS), Département d’Optique ultrarapide et de Nanophotonique (DON), 23, rue du Loess, BP 43, CEDEX 2, 67034 Strasbourg, FranceLaboratory of DNA Structure and Mutagenesis, Department of Biology, Chemistry and Health Sciences, South Dakota School of Mines and Technology, Rapid City, SD 57701, USAUFR Sciences du vivant–Université de Paris, F-75006 Paris, FranceLaboratory of DNA Structure and Mutagenesis, Department of Biology, Chemistry and Health Sciences, South Dakota School of Mines and Technology, Rapid City, SD 57701, USAG-rich DNA repeats that can form G-quadruplex structures are prevalent in bacterial genomes and are frequently associated with regulatory regions of genes involved in virulence, antigenic variation, and antibiotic resistance. These sequences are also inherently mutagenic and can lead to changes affecting cell survival and adaptation. Transcription of the G-quadruplex-forming repeat (G<sub>3</sub>T)<sub>n</sub> in <i>E. coli</i>, when mRNA comprised the G-rich strand, promotes G-quadruplex formation in DNA and increases rates of deletion of G-quadruplex-forming sequences. The genomic instability of G-quadruplex repeats may be a source of genetic variability that can influence alterations and evolution of bacteria. The DNA chaperone Hfq is involved in the genetic instability of these G-quadruplex sequences. Inactivation of the <i>hfq</i> gene decreases the genetic instability of G-quadruplex, demonstrating that the genomic instability of this regulatory element can be influenced by the <i>E. coli</i> highly pleiotropic Hfq protein, which is involved in small noncoding RNA regulation pathways, and DNA organization and packaging. We have shown previously that the protein binds to and stabilizes these sequences, increasing rates of their genomic instability. Here, we extend this analysis to characterize the role of the C-terminal domain of Hfq protein in interaction with G-quadruplex structures. This allows to better understand the function of this specific region of the Hfq protein in genomic instability.https://www.mdpi.com/2076-2607/8/10/1598genomic instabilityquadruplexDNA-directed mutagenesisnucleoidbacterial chromatin
spellingShingle Virali J. Parekh
Frank Wien
Wilfried Grange
Thomas A. De Long
Véronique Arluison
Richard R. Sinden
Crucial Role of the C-Terminal Domain of Hfq Protein in Genomic Instability
Microorganisms
genomic instability
quadruplex
DNA-directed mutagenesis
nucleoid
bacterial chromatin
title Crucial Role of the C-Terminal Domain of Hfq Protein in Genomic Instability
title_full Crucial Role of the C-Terminal Domain of Hfq Protein in Genomic Instability
title_fullStr Crucial Role of the C-Terminal Domain of Hfq Protein in Genomic Instability
title_full_unstemmed Crucial Role of the C-Terminal Domain of Hfq Protein in Genomic Instability
title_short Crucial Role of the C-Terminal Domain of Hfq Protein in Genomic Instability
title_sort crucial role of the c terminal domain of hfq protein in genomic instability
topic genomic instability
quadruplex
DNA-directed mutagenesis
nucleoid
bacterial chromatin
url https://www.mdpi.com/2076-2607/8/10/1598
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