Identification of SUMO targets by a novel proteomic approach in plants
Post-translational modifications (PTMs) chemically and physically alter the properties of proteins, including their folding, subcellular localization, stability, activity, and consequently their function. In spite of their relevance, studies on PTMs in plants are still limited. Small Ubiquitin-like Modifier (SUMO) modification regulates several biological processes by affecting protein-protein interactions, or changing the subcellular localizations of the target proteins. Here, we describe a novel proteomic approach to identify SUMO targets that combines 2-D liquid chromatography, immunodetection, and mass spectrometry (MS) analyses. We have applied this approach to identify nuclear SUMO targets in response to heat shock. Using a bacterial SUMOylation system, we validated that some of the targets identified here are, in fact, labeled with SUMO1. Interestingly, we found that GIGANTEA (GI), a photoperiodic-pathway protein, is modified with SUMO in response to heat shock both in vitro and in vivo. © 2013 Institute of Botany, Chinese Academy of Sciences.
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| Language: | English |
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Wiley
2013
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| Subjects: | Mass spectrometry, Plants, Post-translational modification, Proteomics, SUMO, |
| Online Access: | http://hdl.handle.net/20.500.12792/2495 http://hdl.handle.net/10261/291906 |
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dig-inia-es-10261-2919062023-02-20T07:23:32Z Identification of SUMO targets by a novel proteomic approach in plants López-Torrejón, G. Guerra, D. Catalá, R. Salinas, J. del Pozo, J. C. Mass spectrometry Plants Post-translational modification Proteomics SUMO Post-translational modifications (PTMs) chemically and physically alter the properties of proteins, including their folding, subcellular localization, stability, activity, and consequently their function. In spite of their relevance, studies on PTMs in plants are still limited. Small Ubiquitin-like Modifier (SUMO) modification regulates several biological processes by affecting protein-protein interactions, or changing the subcellular localizations of the target proteins. Here, we describe a novel proteomic approach to identify SUMO targets that combines 2-D liquid chromatography, immunodetection, and mass spectrometry (MS) analyses. We have applied this approach to identify nuclear SUMO targets in response to heat shock. Using a bacterial SUMOylation system, we validated that some of the targets identified here are, in fact, labeled with SUMO1. Interestingly, we found that GIGANTEA (GI), a photoperiodic-pathway protein, is modified with SUMO in response to heat shock both in vitro and in vivo. © 2013 Institute of Botany, Chinese Academy of Sciences. 2023-02-20T07:23:32Z 2023-02-20T07:23:32Z 2013 artículo Journal of Integrative Plant Biology 55(1): 96-107 (2013) 1672-9072 http://hdl.handle.net/20.500.12792/2495 http://hdl.handle.net/10261/291906 10.1111/jipb.12012 1744-7909 en none Wiley |
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Mass spectrometry Plants Post-translational modification Proteomics SUMO Mass spectrometry Plants Post-translational modification Proteomics SUMO |
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Mass spectrometry Plants Post-translational modification Proteomics SUMO Mass spectrometry Plants Post-translational modification Proteomics SUMO López-Torrejón, G. Guerra, D. Catalá, R. Salinas, J. del Pozo, J. C. Identification of SUMO targets by a novel proteomic approach in plants |
| description |
Post-translational modifications (PTMs) chemically and physically alter the properties of proteins, including their folding, subcellular localization, stability, activity, and consequently their function. In spite of their relevance, studies on PTMs in plants are still limited. Small Ubiquitin-like Modifier (SUMO) modification regulates several biological processes by affecting protein-protein interactions, or changing the subcellular localizations of the target proteins. Here, we describe a novel proteomic approach to identify SUMO targets that combines 2-D liquid chromatography, immunodetection, and mass spectrometry (MS) analyses. We have applied this approach to identify nuclear SUMO targets in response to heat shock. Using a bacterial SUMOylation system, we validated that some of the targets identified here are, in fact, labeled with SUMO1. Interestingly, we found that GIGANTEA (GI), a photoperiodic-pathway protein, is modified with SUMO in response to heat shock both in vitro and in vivo. © 2013 Institute of Botany, Chinese Academy of Sciences. |
| format |
artículo |
| topic_facet |
Mass spectrometry Plants Post-translational modification Proteomics SUMO |
| author |
López-Torrejón, G. Guerra, D. Catalá, R. Salinas, J. del Pozo, J. C. |
| author_facet |
López-Torrejón, G. Guerra, D. Catalá, R. Salinas, J. del Pozo, J. C. |
| author_sort |
López-Torrejón, G. |
| title |
Identification of SUMO targets by a novel proteomic approach in plants |
| title_short |
Identification of SUMO targets by a novel proteomic approach in plants |
| title_full |
Identification of SUMO targets by a novel proteomic approach in plants |
| title_fullStr |
Identification of SUMO targets by a novel proteomic approach in plants |
| title_full_unstemmed |
Identification of SUMO targets by a novel proteomic approach in plants |
| title_sort |
identification of sumo targets by a novel proteomic approach in plants |
| publisher |
Wiley |
| publishDate |
2013 |
| url |
http://hdl.handle.net/20.500.12792/2495 http://hdl.handle.net/10261/291906 |
| work_keys_str_mv |
AT lopeztorrejong identificationofsumotargetsbyanovelproteomicapproachinplants AT guerrad identificationofsumotargetsbyanovelproteomicapproachinplants AT catalar identificationofsumotargetsbyanovelproteomicapproachinplants AT salinasj identificationofsumotargetsbyanovelproteomicapproachinplants AT delpozojc identificationofsumotargetsbyanovelproteomicapproachinplants |
| _version_ |
1767603271534379008 |