Structural insights into DNA repair by RNase T--an exonuclease processing 3' end of structured DNA in repair pathways.

DNA repair mechanisms are essential for preservation of genome integrity. However, it is not clear how DNA are selected and processed at broken ends by exonucleases during repair pathways. Here we show that the DnaQ-like exonuclease RNase T is critical for Escherichia coli resistance to various DNA-...

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Autores principales: Yu-Yuan Hsiao, Woei-Horng Fang, Chia-Chia Lee, Yi-Ping Chen, Hanna S Yuan
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Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2014
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Acceso en línea:https://doaj.org/article/bb08ec8882724f25930b0f0b784c269c
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spelling oai:doaj.org-article:bb08ec8882724f25930b0f0b784c269c2021-11-18T05:37:33ZStructural insights into DNA repair by RNase T--an exonuclease processing 3' end of structured DNA in repair pathways.1544-91731545-788510.1371/journal.pbio.1001803https://doaj.org/article/bb08ec8882724f25930b0f0b784c269c2014-03-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24594808/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885DNA repair mechanisms are essential for preservation of genome integrity. However, it is not clear how DNA are selected and processed at broken ends by exonucleases during repair pathways. Here we show that the DnaQ-like exonuclease RNase T is critical for Escherichia coli resistance to various DNA-damaging agents and UV radiation. RNase T specifically trims the 3' end of structured DNA, including bulge, bubble, and Y-structured DNA, and it can work with Endonuclease V to restore the deaminated base in an inosine-containing heteroduplex DNA. Crystal structure analyses further reveal how RNase T recognizes the bulge DNA by inserting a phenylalanine into the bulge, and as a result the 3' end of blunt-end bulge DNA can be digested by RNase T. In contrast, the homodimeric RNase T interacts with the Y-structured DNA by a different binding mode via a single protomer so that the 3' overhang of the Y-structured DNA can be trimmed closely to the duplex region. Our data suggest that RNase T likely processes bulge and bubble DNA in the Endonuclease V-dependent DNA repair, whereas it processes Y-structured DNA in UV-induced and various other DNA repair pathways. This study thus provides mechanistic insights for RNase T and thousands of DnaQ-like exonucleases in DNA 3'-end processing.Yu-Yuan HsiaoWoei-Horng FangChia-Chia LeeYi-Ping ChenHanna S YuanPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 12, Iss 3, p e1001803 (2014)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
Yu-Yuan Hsiao
Woei-Horng Fang
Chia-Chia Lee
Yi-Ping Chen
Hanna S Yuan
Structural insights into DNA repair by RNase T--an exonuclease processing 3' end of structured DNA in repair pathways.
description DNA repair mechanisms are essential for preservation of genome integrity. However, it is not clear how DNA are selected and processed at broken ends by exonucleases during repair pathways. Here we show that the DnaQ-like exonuclease RNase T is critical for Escherichia coli resistance to various DNA-damaging agents and UV radiation. RNase T specifically trims the 3' end of structured DNA, including bulge, bubble, and Y-structured DNA, and it can work with Endonuclease V to restore the deaminated base in an inosine-containing heteroduplex DNA. Crystal structure analyses further reveal how RNase T recognizes the bulge DNA by inserting a phenylalanine into the bulge, and as a result the 3' end of blunt-end bulge DNA can be digested by RNase T. In contrast, the homodimeric RNase T interacts with the Y-structured DNA by a different binding mode via a single protomer so that the 3' overhang of the Y-structured DNA can be trimmed closely to the duplex region. Our data suggest that RNase T likely processes bulge and bubble DNA in the Endonuclease V-dependent DNA repair, whereas it processes Y-structured DNA in UV-induced and various other DNA repair pathways. This study thus provides mechanistic insights for RNase T and thousands of DnaQ-like exonucleases in DNA 3'-end processing.
format article
author Yu-Yuan Hsiao
Woei-Horng Fang
Chia-Chia Lee
Yi-Ping Chen
Hanna S Yuan
author_facet Yu-Yuan Hsiao
Woei-Horng Fang
Chia-Chia Lee
Yi-Ping Chen
Hanna S Yuan
author_sort Yu-Yuan Hsiao
title Structural insights into DNA repair by RNase T--an exonuclease processing 3' end of structured DNA in repair pathways.
title_short Structural insights into DNA repair by RNase T--an exonuclease processing 3' end of structured DNA in repair pathways.
title_full Structural insights into DNA repair by RNase T--an exonuclease processing 3' end of structured DNA in repair pathways.
title_fullStr Structural insights into DNA repair by RNase T--an exonuclease processing 3' end of structured DNA in repair pathways.
title_full_unstemmed Structural insights into DNA repair by RNase T--an exonuclease processing 3' end of structured DNA in repair pathways.
title_sort structural insights into dna repair by rnase t--an exonuclease processing 3' end of structured dna in repair pathways.
publisher Public Library of Science (PLoS)
publishDate 2014
url https://doaj.org/article/bb08ec8882724f25930b0f0b784c269c
work_keys_str_mv AT yuyuanhsiao structuralinsightsintodnarepairbyrnasetanexonucleaseprocessing3endofstructureddnainrepairpathways
AT woeihorngfang structuralinsightsintodnarepairbyrnasetanexonucleaseprocessing3endofstructureddnainrepairpathways
AT chiachialee structuralinsightsintodnarepairbyrnasetanexonucleaseprocessing3endofstructureddnainrepairpathways
AT yipingchen structuralinsightsintodnarepairbyrnasetanexonucleaseprocessing3endofstructureddnainrepairpathways
AT hannasyuan structuralinsightsintodnarepairbyrnasetanexonucleaseprocessing3endofstructureddnainrepairpathways
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