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Optimized enzymatic dual functions of PaPrx protein by proton irradiation
We investigated the effects of proton irradiation on the function and structure of the Pseudomonas aeruginosa peroxiredoxin (PaPrx). Polyacrylamide gel demonstrated that PaPrx proteins exposed to proton irradiation at several doses exhibited simultaneous formation of high molecular weight (HMW) comp...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3885114/ https://www.ncbi.nlm.nih.gov/pubmed/23753570 http://dx.doi.org/10.1093/jrr/rrt081 |
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author | Park, Chul-Hong Lee, Seung Sik Kim, Kye Ryung Jung, Myung Hwan Lee, Sang Yeol Cho, Eun Ju Singh, Sudhir Chung, Byung Yeoup |
author_facet | Park, Chul-Hong Lee, Seung Sik Kim, Kye Ryung Jung, Myung Hwan Lee, Sang Yeol Cho, Eun Ju Singh, Sudhir Chung, Byung Yeoup |
author_sort | Park, Chul-Hong |
collection | PubMed |
description | We investigated the effects of proton irradiation on the function and structure of the Pseudomonas aeruginosa peroxiredoxin (PaPrx). Polyacrylamide gel demonstrated that PaPrx proteins exposed to proton irradiation at several doses exhibited simultaneous formation of high molecular weight (HMW) complexes and fragmentation. Size-exclusion chromatography (SEC) analysis revealed that the number of fragments and very low molecular weight (LMW) structures increased as the proton irradiation dose increased. The peroxidase activity of irradiated PaPrx was preserved, and its chaperone activity was significantly increased by increasing the proton irradiation dose. The chaperone activity increased about 3–4 fold after 2.5 kGy proton irradiation, compared with that of non-irradiated PaPrx, and increased to almost the maximum activity after 10 kGy proton irradiation. We previously obtained functional switching in PaPrx proteins, by using gamma rays and electron beams as radiation sources, and found that the proteins exhibited increased chaperone activity but decreased peroxidase activity. Interestingly, in this study we newly found that proton irradiation could enhance both peroxidase and chaperone activities. Therefore, we can suggest proton irradiation as a novel protocol for conserved 2-Cys protein engineering. |
format | Online Article Text |
id | pubmed-3885114 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-38851142014-01-08 Optimized enzymatic dual functions of PaPrx protein by proton irradiation Park, Chul-Hong Lee, Seung Sik Kim, Kye Ryung Jung, Myung Hwan Lee, Sang Yeol Cho, Eun Ju Singh, Sudhir Chung, Byung Yeoup J Radiat Res Biology We investigated the effects of proton irradiation on the function and structure of the Pseudomonas aeruginosa peroxiredoxin (PaPrx). Polyacrylamide gel demonstrated that PaPrx proteins exposed to proton irradiation at several doses exhibited simultaneous formation of high molecular weight (HMW) complexes and fragmentation. Size-exclusion chromatography (SEC) analysis revealed that the number of fragments and very low molecular weight (LMW) structures increased as the proton irradiation dose increased. The peroxidase activity of irradiated PaPrx was preserved, and its chaperone activity was significantly increased by increasing the proton irradiation dose. The chaperone activity increased about 3–4 fold after 2.5 kGy proton irradiation, compared with that of non-irradiated PaPrx, and increased to almost the maximum activity after 10 kGy proton irradiation. We previously obtained functional switching in PaPrx proteins, by using gamma rays and electron beams as radiation sources, and found that the proteins exhibited increased chaperone activity but decreased peroxidase activity. Interestingly, in this study we newly found that proton irradiation could enhance both peroxidase and chaperone activities. Therefore, we can suggest proton irradiation as a novel protocol for conserved 2-Cys protein engineering. Oxford University Press 2014-01 2013-06-09 /pmc/articles/PMC3885114/ /pubmed/23753570 http://dx.doi.org/10.1093/jrr/rrt081 Text en © The Author 2013. Published by Oxford University Press on behalf of The Japan Radiation Research Society and Japanese Society for Therapeutic Radiology and Oncology. http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Biology Park, Chul-Hong Lee, Seung Sik Kim, Kye Ryung Jung, Myung Hwan Lee, Sang Yeol Cho, Eun Ju Singh, Sudhir Chung, Byung Yeoup Optimized enzymatic dual functions of PaPrx protein by proton irradiation |
title | Optimized enzymatic dual functions of PaPrx protein by proton irradiation |
title_full | Optimized enzymatic dual functions of PaPrx protein by proton irradiation |
title_fullStr | Optimized enzymatic dual functions of PaPrx protein by proton irradiation |
title_full_unstemmed | Optimized enzymatic dual functions of PaPrx protein by proton irradiation |
title_short | Optimized enzymatic dual functions of PaPrx protein by proton irradiation |
title_sort | optimized enzymatic dual functions of paprx protein by proton irradiation |
topic | Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3885114/ https://www.ncbi.nlm.nih.gov/pubmed/23753570 http://dx.doi.org/10.1093/jrr/rrt081 |
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