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...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2021-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0255409 |
| _version_ | 1818722397443850240 |
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| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-17T20:53:59Z |
| format | Article |
| id | doaj.art-5580c6f10c3a463886ed0e2cb386b665 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-17T20:53:59Z |
| publishDate | 2021-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-5580c6f10c3a463886ed0e2cb386b6652022-12-21T21:32:56ZengPublic Library of Science (PLoS)PLoS ONE1932-62032021-01-01167e025540910.1371/journal.pone.0255409Examination of the roles of a conserved motif in the PriA helicase in structure-specific DNA unwinding and processivity.Alexander T DuckworthTricia A WindgassenJames L KeckDNA 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.https://doi.org/10.1371/journal.pone.0255409 |
| spellingShingle | 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. PLoS ONE |
| title | 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_short | 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 |
| url | https://doi.org/10.1371/journal.pone.0255409 |
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