The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding

ParA is an ATPase involved in the segregation of newly replicated DNA in bacteria. Here, structures of a ParA filament bound to DNA and of ParA in various nucleotide states offer insight into its conformational changes upon DNA binding and filament assembly, including the basis for ParA’s cooperativ...

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Autores principales:	Alexandra V. Parker, Daniel Mann, Svetomir B. Tzokov, Ling C. Hwang, Julien R. C. Bergeron
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/d781f34ba46640b4959372762e0f69a3
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spelling	oai:doaj.org-article:d781f34ba46640b4959372762e0f69a32021-12-02T16:35:07ZThe structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding10.1038/s41467-021-25429-22041-1723https://doaj.org/article/d781f34ba46640b4959372762e0f69a32021-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25429-2https://doaj.org/toc/2041-1723ParA is an ATPase involved in the segregation of newly replicated DNA in bacteria. Here, structures of a ParA filament bound to DNA and of ParA in various nucleotide states offer insight into its conformational changes upon DNA binding and filament assembly, including the basis for ParA’s cooperative binding to DNA.Alexandra V. ParkerDaniel MannSvetomir B. TzokovLing C. HwangJulien R. C. BergeronNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Alexandra V. Parker Daniel Mann Svetomir B. Tzokov Ling C. Hwang Julien R. C. Bergeron The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding
description	ParA is an ATPase involved in the segregation of newly replicated DNA in bacteria. Here, structures of a ParA filament bound to DNA and of ParA in various nucleotide states offer insight into its conformational changes upon DNA binding and filament assembly, including the basis for ParA’s cooperative binding to DNA.
format	article
author	Alexandra V. Parker Daniel Mann Svetomir B. Tzokov Ling C. Hwang Julien R. C. Bergeron
author_facet	Alexandra V. Parker Daniel Mann Svetomir B. Tzokov Ling C. Hwang Julien R. C. Bergeron
author_sort	Alexandra V. Parker
title	The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding
title_short	The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding
title_full	The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding
title_fullStr	The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding
title_full_unstemmed	The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding
title_sort	structure of the bacterial dna segregation atpase filament reveals the conformational plasticity of para upon dna binding
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/d781f34ba46640b4959372762e0f69a3
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The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding

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