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231225s2019 xx |||||o 00| ||eng c |
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|a 10.1016/j.jplph.2018.12.002
|2 doi
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|a pubmed25n0973.xml
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|a (DE-627)NLM29201774X
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|a (NLM)30572279
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|a (PII)S0176-1617(18)30362-6
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Besbes, Fatma
|e verfasserin
|4 aut
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|a Phosphorylation-dependent ribonuclease activity of Fra a 1 proteins
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|c 2019
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 12.02.2019
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2018 Elsevier GmbH. All rights reserved.
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|a Abiotic and biotic stress situations cause the upregulation of the transcription of a number of plant defence genes. They code for so-called pathogenesis-related (PR) proteins such as PR proteins of class-10 (PR-10), whose biological functions are still unclear. PR10 proteins are members of the Bet v 1 (major birch pollen allergen) superfamily including related proteins from the cultivated strawberry Fragaria × ananassa (Fra a 1 proteins). Here, we analyzed the expression of 21 Fra a 1 genes in different tissues of the strawberry plant by quantitative real-time PCR. Thirteen members were mainly expressed in roots, three in stems, two in red fruits and leaves, and one in flowers. Five genes (Fra a 1.04-1.08) were selected based on their expression profiles, heterologously expressed in Escherichia coli, and their recombinant proteins functionally characterized. Ribonuclease activity, demonstrated by in-solution and in-gel RNA degradation assays, indicated complete hydrolysis of RNA only by Fra a 1.06. Moreover, phosphorylation assays showed that except for Fra a 1.06, the remaining four recombinant proteins were phosphorylated. Consequently, we investigated whether the phosphorylation status of the proteins affects their ribonuclease activity. Using an in-solution as well as an in-gel RNase activity assay, results demonstrated that the four recombinant proteins, dephosphorylated with phosphatases, exhibited ribonucleolytic activity against total RNA. Thus, the PR10 related proteins characterized in this study harbour a phosphorylation-dependent RNase activity. The results shed new light on the assumed function of PR10 proteins in plant defence
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|a Journal Article
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|a Fragaria × ananassa
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|a Heterologous expression
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|a PR-10
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|a Phosphorylation
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|a RNase activity
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|a qPCR
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|a Antigens, Plant
|2 NLM
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|a Fra a 1 allergen, Fragaria ananassa
|2 NLM
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|a Recombinant Proteins
|2 NLM
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| 650 |
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|a Ribonucleases
|2 NLM
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| 650 |
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|a EC 3.1.-
|2 NLM
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| 700 |
1 |
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|a Franz-Oberdorf, Katrin
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Schwab, Wilfried
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 233(2019) vom: 01. Feb., Seite 1-11
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnns
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| 773 |
1 |
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|g volume:233
|g year:2019
|g day:01
|g month:02
|g pages:1-11
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| 856 |
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|u http://dx.doi.org/10.1016/j.jplph.2018.12.002
|3 Volltext
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|d 233
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|b 01
|c 02
|h 1-11
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