Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/124457
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DC Field | Value | Language |
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dc.contributor.author | Stratilova, B. | - |
dc.contributor.author | Rehulka, P. | - |
dc.contributor.author | Garajova, S. | - |
dc.contributor.author | Rehulkova, H. | - |
dc.contributor.author | Stratilova, E. | - |
dc.contributor.author | Hrmova, M. | - |
dc.contributor.author | Kozmon, S. | - |
dc.date.issued | 2020 | - |
dc.identifier.citation | Phytochemistry: the international journal of plant chemistry, plant biochemistry and molecular biology, 2020; 175:112368-1-112368-9 | - |
dc.identifier.issn | 0031-9422 | - |
dc.identifier.issn | 1873-3700 | - |
dc.identifier.uri | http://hdl.handle.net/2440/124457 | - |
dc.description.abstract | The native dimeric Petroselinum crispum (Mill.) Fuss protein Pet c 1.0201 and a monomeric xyloglucan endotransglycosylase enzyme (Garajova et al., 2008) isolated from the root cells co-purify and share similar molecular masses and acidic isoelectric points. In this work, we determined the complete primary structure of the parsley Pet c 1.0201 protein, based on tryptic and chymotryptic peptides followed by the manual micro-gradient chromatographic separation coupled with offline MALDI-TOF/TOF mass spectrometry. The bioinformatics approach enabled us to include the parsley protein into the PR-10 family, as it exhibited the highest protein sequence identity with the Apium graveolens Api g 1.0201 allergen and the major Daucus carota allergen Dau c 1.0201. Hence, we designated the Petroselinum crispum protein as Pet c 1.0201 and deposited it in the UniProt Knowledgebase under the accession C0HKF5. 3D protein homology modelling and molecular dynamics simulations of the Pet c 1.0201 dimer confirmed the typical structure of the Bet v 1 family allergens, and the potential of the Pet c 1.0201 protein to dimerize in water. However, the behavioural properties of Pet c 1.0201 and the celery allergen Api g 1.0101 differed in the presence of salts due to transiently and stably formed dimeric forms of Pet c 1.0201 and Api g 1.0101, respectively. | - |
dc.description.statementofresponsibility | Barbora Stratilová, Pavel Řehulka, Soňa Garajová, Helena Řehulková, Eva Stratilová, Maria Hrmova, Stanislav Kozmon | - |
dc.language.iso | en | - |
dc.publisher | Elsevier | - |
dc.rights | © 2020 Elsevier Ltd. All rights reserved. | - |
dc.source.uri | http://dx.doi.org/10.1016/j.phytochem.2020.112368 | - |
dc.subject | Petroselinum crispum; apiaceae; parsley; mass spectrometry; 3D structural modelling; molecular dynamics simulations; PR-10 proteins | - |
dc.title | Structural characterization of the Pet c 1.0201 PR-10 protein isolated from roots of Petroselinum crispum (Mill.) Fuss | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1016/j.phytochem.2020.112368 | - |
dc.relation.grant | http://purl.org/au-research/grants/arc/DP120100900 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Hrmova, M. [0000-0002-3545-0605] | - |
Appears in Collections: | Agriculture, Food and Wine publications Aurora harvest 8 |
Files in This Item:
File | Description | Size | Format | |
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hdl_124457.pdf | Accepted version | 1.7 MB | Adobe PDF | View/Open |
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