Examination of the roles of a conserved motif in the PriA helicase in structure-specific DNA unwinding and processivity.

DNA replication complexes (replisomes) frequently encounter barriers that can eject them prematurely from the genome. To avoid the lethality of incomplete DNA replication that arises from these events, bacteria have evolved "DNA replication restart" mechanisms to reload replisomes onto aba...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Alexander T Duckworth, Tricia A Windgassen, James L Keck
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/5580c6f10c3a463886ed0e2cb386b665
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:5580c6f10c3a463886ed0e2cb386b665
record_format	dspace
spelling	oai:doaj.org-article:5580c6f10c3a463886ed0e2cb386b6652021-12-02T20:08:48ZExamination of the roles of a conserved motif in the PriA helicase in structure-specific DNA unwinding and processivity.1932-620310.1371/journal.pone.0255409https://doaj.org/article/5580c6f10c3a463886ed0e2cb386b6652021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0255409https://doaj.org/toc/1932-6203DNA replication complexes (replisomes) frequently encounter barriers that can eject them prematurely from the genome. To avoid the lethality of incomplete DNA replication that arises from these events, bacteria have evolved "DNA replication restart" mechanisms to reload replisomes onto abandoned replication forks. The Escherichia coli PriA DNA helicase orchestrates this process by recognizing and remodeling replication forks and recruiting additional proteins that help to drive replisome reloading. We have identified a conserved sequence motif within a linker region of PriA that docks into a groove on the exterior of the PriA helicase domain. Alterations to the motif reduce the apparent processivity and attenuate structure-specific helicase activity in PriA, implicating the motif as a potential autoregulatory element in replication fork processing. The study also suggests that multiple PriA molecules may function in tandem to enhance DNA unwinding processivity, highlighting an unexpected similarity between PriA and other DNA helicases.Alexander T DuckworthTricia A WindgassenJames L KeckPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 7, p e0255409 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Alexander T Duckworth Tricia A Windgassen James L Keck Examination of the roles of a conserved motif in the PriA helicase in structure-specific DNA unwinding and processivity.
description	DNA replication complexes (replisomes) frequently encounter barriers that can eject them prematurely from the genome. To avoid the lethality of incomplete DNA replication that arises from these events, bacteria have evolved "DNA replication restart" mechanisms to reload replisomes onto abandoned replication forks. The Escherichia coli PriA DNA helicase orchestrates this process by recognizing and remodeling replication forks and recruiting additional proteins that help to drive replisome reloading. We have identified a conserved sequence motif within a linker region of PriA that docks into a groove on the exterior of the PriA helicase domain. Alterations to the motif reduce the apparent processivity and attenuate structure-specific helicase activity in PriA, implicating the motif as a potential autoregulatory element in replication fork processing. The study also suggests that multiple PriA molecules may function in tandem to enhance DNA unwinding processivity, highlighting an unexpected similarity between PriA and other DNA helicases.
format	article
author	Alexander T Duckworth Tricia A Windgassen James L Keck
author_facet	Alexander T Duckworth Tricia A Windgassen James L Keck
author_sort	Alexander T Duckworth
title	Examination of the roles of a conserved motif in the PriA helicase in structure-specific DNA unwinding and processivity.
title_short	Examination of the roles of a conserved motif in the PriA helicase in structure-specific DNA unwinding and processivity.
title_full	Examination of the roles of a conserved motif in the PriA helicase in structure-specific DNA unwinding and processivity.
title_fullStr	Examination of the roles of a conserved motif in the PriA helicase in structure-specific DNA unwinding and processivity.
title_full_unstemmed	Examination of the roles of a conserved motif in the PriA helicase in structure-specific DNA unwinding and processivity.
title_sort	examination of the roles of a conserved motif in the pria helicase in structure-specific dna unwinding and processivity.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/5580c6f10c3a463886ed0e2cb386b665
work_keys_str_mv	AT alexandertduckworth examinationoftherolesofaconservedmotifinthepriahelicaseinstructurespecificdnaunwindingandprocessivity AT triciaawindgassen examinationoftherolesofaconservedmotifinthepriahelicaseinstructurespecificdnaunwindingandprocessivity AT jameslkeck examinationoftherolesofaconservedmotifinthepriahelicaseinstructurespecificdnaunwindingandprocessivity
_version_	1718375124341620736

Examination of the roles of a conserved motif in the PriA helicase in structure-specific DNA unwinding and processivity.

Ejemplares similares