Mammalian histones facilitate antimicrobial synergy by disrupting the bacterial proton gradient and chromosome organization

Histones have a role in antimicrobial defense. Here, the authors show that the histone H2A and the antimicrobial peptide LL-37 exert synergistic effects by enhancing bacterial membrane pores and enabling H2A entry into the bacterial cytoplasm, where it reorganizes DNA and inhibits transcription.

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Autores principales:	Tory Doolin, Henry M. Amir, Leora Duong, Rachel Rosenzweig, Lauren A. Urban, Marta Bosch, Albert Pol, Steven P. Gross, Albert Siryaporn
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b32d941bdfe447b68dbe6452c3da533c
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spelling	oai:doaj.org-article:b32d941bdfe447b68dbe6452c3da533c2021-12-02T18:49:29ZMammalian histones facilitate antimicrobial synergy by disrupting the bacterial proton gradient and chromosome organization10.1038/s41467-020-17699-z2041-1723https://doaj.org/article/b32d941bdfe447b68dbe6452c3da533c2020-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-17699-zhttps://doaj.org/toc/2041-1723Histones have a role in antimicrobial defense. Here, the authors show that the histone H2A and the antimicrobial peptide LL-37 exert synergistic effects by enhancing bacterial membrane pores and enabling H2A entry into the bacterial cytoplasm, where it reorganizes DNA and inhibits transcription.Tory DoolinHenry M. AmirLeora DuongRachel RosenzweigLauren A. UrbanMarta BoschAlbert PolSteven P. GrossAlbert SiryapornNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Tory Doolin Henry M. Amir Leora Duong Rachel Rosenzweig Lauren A. Urban Marta Bosch Albert Pol Steven P. Gross Albert Siryaporn Mammalian histones facilitate antimicrobial synergy by disrupting the bacterial proton gradient and chromosome organization
description	Histones have a role in antimicrobial defense. Here, the authors show that the histone H2A and the antimicrobial peptide LL-37 exert synergistic effects by enhancing bacterial membrane pores and enabling H2A entry into the bacterial cytoplasm, where it reorganizes DNA and inhibits transcription.
format	article
author	Tory Doolin Henry M. Amir Leora Duong Rachel Rosenzweig Lauren A. Urban Marta Bosch Albert Pol Steven P. Gross Albert Siryaporn
author_facet	Tory Doolin Henry M. Amir Leora Duong Rachel Rosenzweig Lauren A. Urban Marta Bosch Albert Pol Steven P. Gross Albert Siryaporn
author_sort	Tory Doolin
title	Mammalian histones facilitate antimicrobial synergy by disrupting the bacterial proton gradient and chromosome organization
title_short	Mammalian histones facilitate antimicrobial synergy by disrupting the bacterial proton gradient and chromosome organization
title_full	Mammalian histones facilitate antimicrobial synergy by disrupting the bacterial proton gradient and chromosome organization
title_fullStr	Mammalian histones facilitate antimicrobial synergy by disrupting the bacterial proton gradient and chromosome organization
title_full_unstemmed	Mammalian histones facilitate antimicrobial synergy by disrupting the bacterial proton gradient and chromosome organization
title_sort	mammalian histones facilitate antimicrobial synergy by disrupting the bacterial proton gradient and chromosome organization
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/b32d941bdfe447b68dbe6452c3da533c
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Mammalian histones facilitate antimicrobial synergy by disrupting the bacterial proton gradient and chromosome organization

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