Cargando…
Callitriche cophocarpa (water starwort) proteome under chromate stress: evidence for induction of a quinone reductase
Chromate-induced physiological stress in a water-submerged macrophyte Callitriche cophocarpa Sendtn. (water starwort) was tested at the proteomic level. The oxidative stress status of the plant treated with 1 mM Cr(VI) for 3 days revealed stimulation of peroxidases whereas catalase and superoxide di...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5854755/ https://www.ncbi.nlm.nih.gov/pubmed/29332274 http://dx.doi.org/10.1007/s11356-017-1067-y |
_version_ | 1783306969993445376 |
---|---|
author | Kaszycki, Paweł Dubicka-Lisowska, Aleksandra Augustynowicz, Joanna Piwowarczyk, Barbara Wesołowski, Wojciech |
author_facet | Kaszycki, Paweł Dubicka-Lisowska, Aleksandra Augustynowicz, Joanna Piwowarczyk, Barbara Wesołowski, Wojciech |
author_sort | Kaszycki, Paweł |
collection | PubMed |
description | Chromate-induced physiological stress in a water-submerged macrophyte Callitriche cophocarpa Sendtn. (water starwort) was tested at the proteomic level. The oxidative stress status of the plant treated with 1 mM Cr(VI) for 3 days revealed stimulation of peroxidases whereas catalase and superoxide dismutase activities were similar to the control levels. Employing two-dimensional electrophoresis, comparative proteomics enabled to detect five differentiating proteins subjected to identification with mass spectrometry followed by an NCBI database search. Cr(VI) incubation led to induction of light harvesting chlorophyll a/b binding protein with a concomitant decrease of accumulation of ribulose bisphosphate carboxylase (RuBisCO). The main finding was, however, the identification of an NAD(P)H-dependent dehydrogenase FQR1, detectable only in Cr(VI)-treated plants. The FQR1 flavoenzyme is known to be responsive to oxidative stress and to act as a detoxification protein by protecting the cells against oxidative damage. It exhibits the in vitro quinone reductase activity and is capable of catalyzing two-electron transfer from NAD(P)H to several substrates, presumably including Cr(VI). The enhanced accumulation of FQR1 was chromate-specific since other stressful conditions, such as salt, temperature, and oxidative stresses, all failed to induce the protein. Zymographic analysis of chromate-treated Callitriche shoots showed a novel enzymatic protein band whose activity was attributed to the newly identified enzyme. We suggest that Cr(VI) phytoremediation with C. cophocarpa can be promoted by chromate reductase activity produced by the induced quinone oxidoreductase which might take part in Cr(VI) → Cr(III) bioreduction process and thus enable the plant to cope with the chromate-generated oxidative stress. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s11356-017-1067-y) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-5854755 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-58547552018-03-22 Callitriche cophocarpa (water starwort) proteome under chromate stress: evidence for induction of a quinone reductase Kaszycki, Paweł Dubicka-Lisowska, Aleksandra Augustynowicz, Joanna Piwowarczyk, Barbara Wesołowski, Wojciech Environ Sci Pollut Res Int Research Article Chromate-induced physiological stress in a water-submerged macrophyte Callitriche cophocarpa Sendtn. (water starwort) was tested at the proteomic level. The oxidative stress status of the plant treated with 1 mM Cr(VI) for 3 days revealed stimulation of peroxidases whereas catalase and superoxide dismutase activities were similar to the control levels. Employing two-dimensional electrophoresis, comparative proteomics enabled to detect five differentiating proteins subjected to identification with mass spectrometry followed by an NCBI database search. Cr(VI) incubation led to induction of light harvesting chlorophyll a/b binding protein with a concomitant decrease of accumulation of ribulose bisphosphate carboxylase (RuBisCO). The main finding was, however, the identification of an NAD(P)H-dependent dehydrogenase FQR1, detectable only in Cr(VI)-treated plants. The FQR1 flavoenzyme is known to be responsive to oxidative stress and to act as a detoxification protein by protecting the cells against oxidative damage. It exhibits the in vitro quinone reductase activity and is capable of catalyzing two-electron transfer from NAD(P)H to several substrates, presumably including Cr(VI). The enhanced accumulation of FQR1 was chromate-specific since other stressful conditions, such as salt, temperature, and oxidative stresses, all failed to induce the protein. Zymographic analysis of chromate-treated Callitriche shoots showed a novel enzymatic protein band whose activity was attributed to the newly identified enzyme. We suggest that Cr(VI) phytoremediation with C. cophocarpa can be promoted by chromate reductase activity produced by the induced quinone oxidoreductase which might take part in Cr(VI) → Cr(III) bioreduction process and thus enable the plant to cope with the chromate-generated oxidative stress. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s11356-017-1067-y) contains supplementary material, which is available to authorized users. Springer Berlin Heidelberg 2018-01-13 2018 /pmc/articles/PMC5854755/ /pubmed/29332274 http://dx.doi.org/10.1007/s11356-017-1067-y Text en © The Author(s) 2018 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Research Article Kaszycki, Paweł Dubicka-Lisowska, Aleksandra Augustynowicz, Joanna Piwowarczyk, Barbara Wesołowski, Wojciech Callitriche cophocarpa (water starwort) proteome under chromate stress: evidence for induction of a quinone reductase |
title | Callitriche cophocarpa (water starwort) proteome under chromate stress: evidence for induction of a quinone reductase |
title_full | Callitriche cophocarpa (water starwort) proteome under chromate stress: evidence for induction of a quinone reductase |
title_fullStr | Callitriche cophocarpa (water starwort) proteome under chromate stress: evidence for induction of a quinone reductase |
title_full_unstemmed | Callitriche cophocarpa (water starwort) proteome under chromate stress: evidence for induction of a quinone reductase |
title_short | Callitriche cophocarpa (water starwort) proteome under chromate stress: evidence for induction of a quinone reductase |
title_sort | callitriche cophocarpa (water starwort) proteome under chromate stress: evidence for induction of a quinone reductase |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5854755/ https://www.ncbi.nlm.nih.gov/pubmed/29332274 http://dx.doi.org/10.1007/s11356-017-1067-y |
work_keys_str_mv | AT kaszyckipaweł callitrichecophocarpawaterstarwortproteomeunderchromatestressevidenceforinductionofaquinonereductase AT dubickalisowskaaleksandra callitrichecophocarpawaterstarwortproteomeunderchromatestressevidenceforinductionofaquinonereductase AT augustynowiczjoanna callitrichecophocarpawaterstarwortproteomeunderchromatestressevidenceforinductionofaquinonereductase AT piwowarczykbarbara callitrichecophocarpawaterstarwortproteomeunderchromatestressevidenceforinductionofaquinonereductase AT wesołowskiwojciech callitrichecophocarpawaterstarwortproteomeunderchromatestressevidenceforinductionofaquinonereductase |