Identification of novel superoxide dismutase isoenzymes in the olive (Olea europaea L.) pollen
Abstract Background Among antioxidant enzymes, the superoxide dismutase (SOD) family is a major actor in catalysing the disproportionation of superoxide. Apart from its role as antioxidant, these enzymes have a role in cell signalling, and Cu,Zn-SOD proteins are also major pollen allergens. In order...
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BMC
2018-06-01
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Series: | BMC Plant Biology |
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Online Access: | http://link.springer.com/article/10.1186/s12870-018-1328-z |
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author | Adoración Zafra Antonio Jesús Castro Juan de Dios Alché |
author_facet | Adoración Zafra Antonio Jesús Castro Juan de Dios Alché |
author_sort | Adoración Zafra |
collection | DOAJ |
description | Abstract Background Among antioxidant enzymes, the superoxide dismutase (SOD) family is a major actor in catalysing the disproportionation of superoxide. Apart from its role as antioxidant, these enzymes have a role in cell signalling, and Cu,Zn-SOD proteins are also major pollen allergens. In order to deepen our understanding of the SOD isoenzymes present in olive pollen and to analyse the molecular variability of the pollen Cu,Zn-SOD family, we carried out biochemical, transcriptomic and localization studies of pollen grains from different olive cultivars and other allergenic species. Results Olive pollen showed a high rate of total SOD activity in all cultivars assayed, which did not correlate with pollen viability. Mass spectrometry analysis together with activity assays and Western blotting experiments enabled us to identify new forms of Cu,Zn-SOD enzyme (including chloroplastidic and peroxisomal forms) as well as differentially expressed Mn-, Fe- and Cu,Zn-SOD isoenzymes among the pollen of different olive cultivars and allergenic species. Ultrastructural localization of Cu,Zn-SOD revealed its plastidial localization in the pollen grain. We also identified the occurrence of a shorter form of one of the cytosolic Cu,Zn-SOD enzymes, likely as the result of alternative splicing. This shorter enzyme showed lower SOD activity as compared to the full length form. Conclusions The presence of multiple SOD isoenzymes in the olive pollen could be related to the need of finely tuning the ROS metabolism during the transition from its quiescent condition at maturity to a highly metabolically active state at germination. |
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language | English |
last_indexed | 2024-04-13T08:36:51Z |
publishDate | 2018-06-01 |
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series | BMC Plant Biology |
spelling | doaj.art-9486b15da1b9417ea5cee8c616fdea5e2022-12-22T02:54:04ZengBMCBMC Plant Biology1471-22292018-06-0118111610.1186/s12870-018-1328-zIdentification of novel superoxide dismutase isoenzymes in the olive (Olea europaea L.) pollenAdoración Zafra0Antonio Jesús Castro1Juan de Dios Alché2Plant Reproductive Biology Research Laboratory, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas (CSIC), Department of Biochemistry, Cell and Molecular Biology of PlantsPlant Reproductive Biology Research Laboratory, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas (CSIC), Department of Biochemistry, Cell and Molecular Biology of PlantsPlant Reproductive Biology Research Laboratory, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas (CSIC), Department of Biochemistry, Cell and Molecular Biology of PlantsAbstract Background Among antioxidant enzymes, the superoxide dismutase (SOD) family is a major actor in catalysing the disproportionation of superoxide. Apart from its role as antioxidant, these enzymes have a role in cell signalling, and Cu,Zn-SOD proteins are also major pollen allergens. In order to deepen our understanding of the SOD isoenzymes present in olive pollen and to analyse the molecular variability of the pollen Cu,Zn-SOD family, we carried out biochemical, transcriptomic and localization studies of pollen grains from different olive cultivars and other allergenic species. Results Olive pollen showed a high rate of total SOD activity in all cultivars assayed, which did not correlate with pollen viability. Mass spectrometry analysis together with activity assays and Western blotting experiments enabled us to identify new forms of Cu,Zn-SOD enzyme (including chloroplastidic and peroxisomal forms) as well as differentially expressed Mn-, Fe- and Cu,Zn-SOD isoenzymes among the pollen of different olive cultivars and allergenic species. Ultrastructural localization of Cu,Zn-SOD revealed its plastidial localization in the pollen grain. We also identified the occurrence of a shorter form of one of the cytosolic Cu,Zn-SOD enzymes, likely as the result of alternative splicing. This shorter enzyme showed lower SOD activity as compared to the full length form. Conclusions The presence of multiple SOD isoenzymes in the olive pollen could be related to the need of finely tuning the ROS metabolism during the transition from its quiescent condition at maturity to a highly metabolically active state at germination.http://link.springer.com/article/10.1186/s12870-018-1328-zAlternative splicingAmyloplastCu,Zn-SODFe-SODMn-SODOlive |
spellingShingle | Adoración Zafra Antonio Jesús Castro Juan de Dios Alché Identification of novel superoxide dismutase isoenzymes in the olive (Olea europaea L.) pollen BMC Plant Biology Alternative splicing Amyloplast Cu,Zn-SOD Fe-SOD Mn-SOD Olive |
title | Identification of novel superoxide dismutase isoenzymes in the olive (Olea europaea L.) pollen |
title_full | Identification of novel superoxide dismutase isoenzymes in the olive (Olea europaea L.) pollen |
title_fullStr | Identification of novel superoxide dismutase isoenzymes in the olive (Olea europaea L.) pollen |
title_full_unstemmed | Identification of novel superoxide dismutase isoenzymes in the olive (Olea europaea L.) pollen |
title_short | Identification of novel superoxide dismutase isoenzymes in the olive (Olea europaea L.) pollen |
title_sort | identification of novel superoxide dismutase isoenzymes in the olive olea europaea l pollen |
topic | Alternative splicing Amyloplast Cu,Zn-SOD Fe-SOD Mn-SOD Olive |
url | http://link.springer.com/article/10.1186/s12870-018-1328-z |
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