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人类DNA解旋酶B在细胞同源重组中发挥作用，并在体外刺激Rad51介导的5'-3'异源双链延伸。

Human DNA helicase B functions in cellular homologous recombination and stimulates Rad51-mediated 5'-3' heteroduplex extension in vitro.

作者信息

Liu Hanjian, Yan Peijun, Fanning Ellen

机构信息

Department of Biological Sciences, Vanderbilt University, Nashville, Tennessee, United States of America.

出版信息

PLoS One. 2015 Jan 24;10(1):e0116852. doi: 10.1371/journal.pone.0116852. eCollection 2015.

DOI:10.1371/journal.pone.0116852
PMID:25617833
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4305318/
Abstract

Homologous recombination is involved in the repair of DNA damage and collapsed replication fork, and is critical for the maintenance of genomic stability. Its process involves a network of proteins with different enzymatic activities. Human DNA helicase B (HDHB) is a robust 5'-3' DNA helicase which accumulates on chromatin in cells exposed to DNA damage. HDHB facilitates cellular recovery from replication stress, but its role in DNA damage response remains unclear. Here we report that HDHB silencing results in reduced sister chromatid exchange, impaired homologous recombination repair, and delayed RPA late-stage foci formation induced by ionizing radiation. Ectopically expressed HDHB colocalizes with Rad51, Rad52, RPA, and ssDNA. In vitro, HDHB stimulates Rad51-mediated heteroduplex extension in 5'-3' direction. A helicase-defective mutant HDHB failed to promote this reaction. Our studies implicate HDHB promotes homologous recombination in vivo and stimulates 5'-3' heteroduplex extension during Rad51-mediated strand exchange in vitro.

摘要

同源重组参与DNA损伤修复和复制叉坍塌修复，对维持基因组稳定性至关重要。其过程涉及具有不同酶活性的蛋白质网络。人DNA解旋酶B（HDHB）是一种强大的5'-3' DNA解旋酶，在暴露于DNA损伤的细胞中会在染色质上积累。HDHB促进细胞从复制应激中恢复，但其在DNA损伤反应中的作用仍不清楚。在此我们报告，HDHB沉默导致姐妹染色单体交换减少、同源重组修复受损以及电离辐射诱导的RPA后期病灶形成延迟。异位表达的HDHB与Rad51、Rad52、RPA和单链DNA共定位。在体外，HDHB刺激Rad51介导的异源双链在5'-3'方向上延伸。解旋酶缺陷型突变体HDHB未能促进此反应。我们的研究表明，HDHB在体内促进同源重组，并在体外Rad51介导的链交换过程中刺激5'-3'异源双链延伸。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb2/4305318/3d4b526a2089/pone.0116852.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb2/4305318/4339b2b73dbb/pone.0116852.g001.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb2/4305318/1f3c2c6a4842/pone.0116852.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb2/4305318/495dab431a04/pone.0116852.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb2/4305318/3d4b526a2089/pone.0116852.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb2/4305318/4339b2b73dbb/pone.0116852.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb2/4305318/bf612afcbdc4/pone.0116852.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb2/4305318/cc04e6825e3c/pone.0116852.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb2/4305318/1f3c2c6a4842/pone.0116852.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb2/4305318/495dab431a04/pone.0116852.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb2/4305318/3d4b526a2089/pone.0116852.g006.jpg

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