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Protease Activity of PprI Facilitates DNA Damage Response: Mn(2+)-Dependence and Substrate Sequence-Specificity of the Proteolytic Reaction
The extremophilic bacterium Deinococcus radiodurans exhibits an extraordinary resistance to ionizing radiation. Previous studies established that a protein named PprI, which exists only in the Deinococcus-Thermus family, acts as a general switch to orchestrate the expression of a number of DNA damag...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4374696/ https://www.ncbi.nlm.nih.gov/pubmed/25811789 http://dx.doi.org/10.1371/journal.pone.0122071 |
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author | Wang, Yunguang Xu, Qiang Lu, Huiming Lin, Lin Wang, Liangyan Xu, Hong Cui, Xianyan Zhang, Hui Li, Tingting Hua, Yuejin |
author_facet | Wang, Yunguang Xu, Qiang Lu, Huiming Lin, Lin Wang, Liangyan Xu, Hong Cui, Xianyan Zhang, Hui Li, Tingting Hua, Yuejin |
author_sort | Wang, Yunguang |
collection | PubMed |
description | The extremophilic bacterium Deinococcus radiodurans exhibits an extraordinary resistance to ionizing radiation. Previous studies established that a protein named PprI, which exists only in the Deinococcus-Thermus family, acts as a general switch to orchestrate the expression of a number of DNA damage response (DDR) proteins involved in cellular radio-resistance. Here we show that the regulatory mechanism of PprI depends on its Mn(2+)-dependent protease activity toward DdrO, a transcription factor that suppresses DDR genes’ expression. Recognition sequence-specificity around the PprI cleavage site is essential for DNA damage repair in vivo. PprI and DdrO mediate a novel DNA damage response pathway differing from the classic LexA-mediated SOS response system found in radiation-sensitive bacterium Escherichia coli. This PprI-mediated pathway in D. radiodurans is indispensable for its extreme radio-resistance and therefore its elucidation significantly advances our understanding of the DNA damage repair mechanism in this amazing organism. |
format | Online Article Text |
id | pubmed-4374696 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-43746962015-04-04 Protease Activity of PprI Facilitates DNA Damage Response: Mn(2+)-Dependence and Substrate Sequence-Specificity of the Proteolytic Reaction Wang, Yunguang Xu, Qiang Lu, Huiming Lin, Lin Wang, Liangyan Xu, Hong Cui, Xianyan Zhang, Hui Li, Tingting Hua, Yuejin PLoS One Research Article The extremophilic bacterium Deinococcus radiodurans exhibits an extraordinary resistance to ionizing radiation. Previous studies established that a protein named PprI, which exists only in the Deinococcus-Thermus family, acts as a general switch to orchestrate the expression of a number of DNA damage response (DDR) proteins involved in cellular radio-resistance. Here we show that the regulatory mechanism of PprI depends on its Mn(2+)-dependent protease activity toward DdrO, a transcription factor that suppresses DDR genes’ expression. Recognition sequence-specificity around the PprI cleavage site is essential for DNA damage repair in vivo. PprI and DdrO mediate a novel DNA damage response pathway differing from the classic LexA-mediated SOS response system found in radiation-sensitive bacterium Escherichia coli. This PprI-mediated pathway in D. radiodurans is indispensable for its extreme radio-resistance and therefore its elucidation significantly advances our understanding of the DNA damage repair mechanism in this amazing organism. Public Library of Science 2015-03-26 /pmc/articles/PMC4374696/ /pubmed/25811789 http://dx.doi.org/10.1371/journal.pone.0122071 Text en © 2015 Wang et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Wang, Yunguang Xu, Qiang Lu, Huiming Lin, Lin Wang, Liangyan Xu, Hong Cui, Xianyan Zhang, Hui Li, Tingting Hua, Yuejin Protease Activity of PprI Facilitates DNA Damage Response: Mn(2+)-Dependence and Substrate Sequence-Specificity of the Proteolytic Reaction |
title | Protease Activity of PprI Facilitates DNA Damage Response: Mn(2+)-Dependence and Substrate Sequence-Specificity of the Proteolytic Reaction |
title_full | Protease Activity of PprI Facilitates DNA Damage Response: Mn(2+)-Dependence and Substrate Sequence-Specificity of the Proteolytic Reaction |
title_fullStr | Protease Activity of PprI Facilitates DNA Damage Response: Mn(2+)-Dependence and Substrate Sequence-Specificity of the Proteolytic Reaction |
title_full_unstemmed | Protease Activity of PprI Facilitates DNA Damage Response: Mn(2+)-Dependence and Substrate Sequence-Specificity of the Proteolytic Reaction |
title_short | Protease Activity of PprI Facilitates DNA Damage Response: Mn(2+)-Dependence and Substrate Sequence-Specificity of the Proteolytic Reaction |
title_sort | protease activity of ppri facilitates dna damage response: mn(2+)-dependence and substrate sequence-specificity of the proteolytic reaction |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4374696/ https://www.ncbi.nlm.nih.gov/pubmed/25811789 http://dx.doi.org/10.1371/journal.pone.0122071 |
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