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Type: Journal article
Title: Structural characterization of the Pet c 1.0201 PR-10 protein isolated from roots of Petroselinum crispum (Mill.) Fuss
Author: Stratilova, B.
Rehulka, P.
Garajova, S.
Rehulkova, H.
Stratilova, E.
Hrmova, M.
Kozmon, S.
Citation: Phytochemistry: the international journal of plant chemistry, plant biochemistry and molecular biology, 2020; 175:112368-1-112368-9
Publisher: Elsevier
Issue Date: 2020
ISSN: 0031-9422
Statement of
Barbora Stratilová, Pavel Řehulka, Soňa Garajová, Helena Řehulková, Eva Stratilová, Maria Hrmova, Stanislav Kozmon
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.
Keywords: Petroselinum crispum; apiaceae; parsley; mass spectrometry; 3D structural modelling; molecular dynamics simulations; PR-10 proteins
Rights: © 2020 Elsevier Ltd. All rights reserved.
DOI: 10.1016/j.phytochem.2020.112368
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Appears in Collections:Agriculture, Food and Wine publications
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