Identification and characterization of the Hfq bacterial amyloid region DNA interactions

Nucleic acid amyloid proteins interactions have been observed in the past few years. These interactions often promote protein aggregation. Nevertheless, molecular basis and physiological consequences of these interactions are still poorly understood. Additionally, it is unknown whether the nucleic a...

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Autores principales:	Florian Turbant, Omar El Hamoui, David Partouche, Christophe Sandt, Florent Busi, Frank Wien, Véronique Arluison
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Bacterial amyloid Functional amyloid DNA:protein fibrils DNA induced protein fibrillation Bacterial adaptation Biochemistry QD415-436 Genetics QH426-470
Acceso en línea:	https://doaj.org/article/7ce0e048d2cf4331a00540d7f6517ab8
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spelling	oai:doaj.org-article:7ce0e048d2cf4331a00540d7f6517ab82021-11-12T04:50:00ZIdentification and characterization of the Hfq bacterial amyloid region DNA interactions2667-160310.1016/j.bbadva.2021.100029https://doaj.org/article/7ce0e048d2cf4331a00540d7f6517ab82021-01-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2667160321000284https://doaj.org/toc/2667-1603Nucleic acid amyloid proteins interactions have been observed in the past few years. These interactions often promote protein aggregation. Nevertheless, molecular basis and physiological consequences of these interactions are still poorly understood. Additionally, it is unknown whether the nucleic acid promotes the formation of self-assembly due to direct interactions or indirectly via sequences surrounding the amyloid region. Here we focus our attention on a bacterial amyloid, Hfq. This protein is a pleiotropic bacterial regulator that mediates many aspects of nucleic acids metabolism. The protein notably mediates mRNA stability and translation efficiency by using stress-related small non coding regulatory RNA. In addition, Hfq, thanks to its amyloid C-terminal region, binds and compacts DNA. A combination of experimental methodologies, including synchrotron radiation circular dichroism (SRCD), gel shift assay and infrared (FTIR) spectroscopy have been used to probe the interaction of Hfq C-terminal region with DNA. We clearly identify important amino acids in this region involved in DNA binding and polymerization properties. This allows to understand better how this bacterial amyloid interacts with DNA. Possible functional consequence to answer to stresses are discussed.Florian TurbantOmar El HamouiDavid PartoucheChristophe SandtFlorent BusiFrank WienVéronique ArluisonElsevierarticleBacterial amyloidFunctional amyloidDNA:protein fibrilsDNA induced protein fibrillationBacterial adaptationBiochemistryQD415-436GeneticsQH426-470ENBBA Advances, Vol 1, Iss , Pp 100029- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Bacterial amyloid Functional amyloid DNA:protein fibrils DNA induced protein fibrillation Bacterial adaptation Biochemistry QD415-436 Genetics QH426-470
spellingShingle	Bacterial amyloid Functional amyloid DNA:protein fibrils DNA induced protein fibrillation Bacterial adaptation Biochemistry QD415-436 Genetics QH426-470 Florian Turbant Omar El Hamoui David Partouche Christophe Sandt Florent Busi Frank Wien Véronique Arluison Identification and characterization of the Hfq bacterial amyloid region DNA interactions
description	Nucleic acid amyloid proteins interactions have been observed in the past few years. These interactions often promote protein aggregation. Nevertheless, molecular basis and physiological consequences of these interactions are still poorly understood. Additionally, it is unknown whether the nucleic acid promotes the formation of self-assembly due to direct interactions or indirectly via sequences surrounding the amyloid region. Here we focus our attention on a bacterial amyloid, Hfq. This protein is a pleiotropic bacterial regulator that mediates many aspects of nucleic acids metabolism. The protein notably mediates mRNA stability and translation efficiency by using stress-related small non coding regulatory RNA. In addition, Hfq, thanks to its amyloid C-terminal region, binds and compacts DNA. A combination of experimental methodologies, including synchrotron radiation circular dichroism (SRCD), gel shift assay and infrared (FTIR) spectroscopy have been used to probe the interaction of Hfq C-terminal region with DNA. We clearly identify important amino acids in this region involved in DNA binding and polymerization properties. This allows to understand better how this bacterial amyloid interacts with DNA. Possible functional consequence to answer to stresses are discussed.
format	article
author	Florian Turbant Omar El Hamoui David Partouche Christophe Sandt Florent Busi Frank Wien Véronique Arluison
author_facet	Florian Turbant Omar El Hamoui David Partouche Christophe Sandt Florent Busi Frank Wien Véronique Arluison
author_sort	Florian Turbant
title	Identification and characterization of the Hfq bacterial amyloid region DNA interactions
title_short	Identification and characterization of the Hfq bacterial amyloid region DNA interactions
title_full	Identification and characterization of the Hfq bacterial amyloid region DNA interactions
title_fullStr	Identification and characterization of the Hfq bacterial amyloid region DNA interactions
title_full_unstemmed	Identification and characterization of the Hfq bacterial amyloid region DNA interactions
title_sort	identification and characterization of the hfq bacterial amyloid region dna interactions
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/7ce0e048d2cf4331a00540d7f6517ab8
work_keys_str_mv	AT florianturbant identificationandcharacterizationofthehfqbacterialamyloidregiondnainteractions AT omarelhamoui identificationandcharacterizationofthehfqbacterialamyloidregiondnainteractions AT davidpartouche identificationandcharacterizationofthehfqbacterialamyloidregiondnainteractions AT christophesandt identificationandcharacterizationofthehfqbacterialamyloidregiondnainteractions AT florentbusi identificationandcharacterizationofthehfqbacterialamyloidregiondnainteractions AT frankwien identificationandcharacterizationofthehfqbacterialamyloidregiondnainteractions AT veroniquearluison identificationandcharacterizationofthehfqbacterialamyloidregiondnainteractions
_version_	1718431178906664960

Identification and characterization of the Hfq bacterial amyloid region DNA interactions

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