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研究保守基序在 PriA 解旋酶中对结构特异性 DNA 解旋和连续性的作用。

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

机构信息

Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI, United States of America.

Codexis Inc, Redwood City, CA, United States of America.

出版信息

PLoS One. 2021 Jul 30;16(7):e0255409. doi: 10.1371/journal.pone.0255409. eCollection 2021.

DOI:10.1371/journal.pone.0255409
PMID:34329356
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8323898/
Abstract

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.

摘要

DNA 复制复合物（复制体）经常会遇到障碍，这些障碍会导致它们过早地从基因组中弹出。为了避免因这些事件导致的不完全 DNA 复制的致命性，细菌已经进化出“DNA 复制重新启动”机制，以便将复制体重新加载到被放弃的复制叉上。大肠杆菌 PriA DNA 解旋酶通过识别和重塑复制叉并招募其他有助于驱动复制体重新加载的蛋白质来协调这个过程。我们已经在 PriA 的连接区中识别出一个保守的序列模体，该模体可以插入 PriA 解旋酶结构域外部的一个凹槽中。改变该模体可降低 PriA 的表观连续性和减弱结构特异性解旋酶活性，表明该模体可能是复制叉加工的潜在自调节元件。该研究还表明，多个 PriA 分子可能串联发挥作用以增强 DNA 解旋的连续性，这突出了 PriA 与其他 DNA 解旋酶之间出乎意料的相似性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/081a/8323898/5ac80050059a/pone.0255409.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/081a/8323898/28dfc474a3da/pone.0255409.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/081a/8323898/7d88709f4981/pone.0255409.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/081a/8323898/a9f98069307d/pone.0255409.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/081a/8323898/7a9d493e170b/pone.0255409.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/081a/8323898/ca0006cc2ac1/pone.0255409.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/081a/8323898/5ac80050059a/pone.0255409.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/081a/8323898/28dfc474a3da/pone.0255409.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/081a/8323898/7d88709f4981/pone.0255409.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/081a/8323898/a9f98069307d/pone.0255409.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/081a/8323898/7a9d493e170b/pone.0255409.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/081a/8323898/ca0006cc2ac1/pone.0255409.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/081a/8323898/5ac80050059a/pone.0255409.g006.jpg

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本文引用的文献

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Biochem J. 2020 Oct 16;477(19):3911-3922. doi: 10.1042/BCJ20200269.
2
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J Biol Chem. 2019 Feb 22;294(8):2801-2814. doi: 10.1074/jbc.RA118.006870. Epub 2018 Dec 28.
3
Structure-specific DNA replication-fork recognition directs helicase and replication restart activities of the PriA helicase.
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Proc Natl Acad Sci U S A. 2018 Sep 25;115(39):E9075-E9084. doi: 10.1073/pnas.1809842115. Epub 2018 Sep 10.
4
Mechanisms of bacterial DNA replication restart.细菌 DNA 复制重启动的机制。
Nucleic Acids Res. 2018 Jan 25;46(2):504-519. doi: 10.1093/nar/gkx1203.
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Transcription leads to pervasive replisome instability in bacteria.转录会导致细菌中普遍存在的复制体不稳定性。
Elife. 2017 Jan 16;6:e19848. doi: 10.7554/eLife.19848.
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An aromatic-rich loop couples DNA binding and ATP hydrolysis in the PriA DNA helicase.富含芳香族氨基酸的环将PriA DNA解旋酶中的DNA结合与ATP水解偶联起来。
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