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231225s2022 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/erab409
|2 doi
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|a pubmed24n1100.xml
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|a (DE-627)NLM330295837
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|a (NLM)34487166
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a O'Gallagher, Bryden
|e verfasserin
|4 aut
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|a Arabidopsis PAP17 is a dual-localized purple acid phosphatase up-regulated during phosphate deprivation, senescence, and oxidative stress
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|c 2022
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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 27.01.2022
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|a Date Revised 27.01.2022
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|a published: Print
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|a Citation Status MEDLINE
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|a © The Author(s) 2021. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.
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|a A 35 kDa monomeric purple acid phosphatase (APase) was purified from cell wall extracts of Pi starved (-Pi) Arabidopsis thaliana suspension cells and identified as AtPAP17 (At3g17790) by mass spectrometry and N-terminal microsequencing. AtPAP17 was de novo synthesized and dual-localized to the secretome and/or intracellular fraction of -Pi or salt-stressed plants, or senescing leaves. Transiently expressed AtPAP17-green fluorescent protein localized to lytic vacuoles of the Arabidopsis suspension cells. No significant biochemical or phenotypical changes associated with AtPAP17 loss of function were observed in an atpap17 mutant during Pi deprivation, leaf senescence, or salinity stress. Nevertheless, AtPAP17 is hypothesized to contribute to Pi metabolism owing to its marked up-regulation during Pi starvation and leaf senescence, broad APase substrate selectivity and pH activity profile, and rapid repression and turnover following Pi resupply to -Pi plants. While AtPAP17 also catalyzed the peroxidation of luminol, which was optimal at pH 9.2, it exhibited a low Vmax and affinity for hydrogen peroxide relative to horseradish peroxidase. These results, coupled with absence of a phenotype in the salt-stressed or -Pi atpap17 mutant, do not support proposals that the peroxidase activity of AtPAP17 contributes to the detoxification of reactive oxygen species during stresses that trigger AtPAP17 up-regulation
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a Hydrogen peroxide metabolism
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|a peroxidase
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|a phosphate metabolism
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|a phosphate starvation response
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|a purple acid phosphatase
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|a reactive oxygen species
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|a salinity stress
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|a senescence
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|a Arabidopsis Proteins
|2 NLM
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|a Glycoproteins
|2 NLM
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|a Phosphates
|2 NLM
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|a purple acid phosphatase
|2 NLM
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|a EC 3.1.3.-
|2 NLM
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|a Acid Phosphatase
|2 NLM
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| 650 |
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|a EC 3.1.3.2
|2 NLM
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| 700 |
1 |
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|a Ghahremani, Mina
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Stigter, Kyla
|e verfasserin
|4 aut
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| 700 |
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|a Walker, Emma J L
|e verfasserin
|4 aut
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|a Pyc, Michal
|e verfasserin
|4 aut
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| 700 |
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|a Liu, Ang-Yu
|e verfasserin
|4 aut
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| 700 |
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|a MacIntosh, Gustavo C
|e verfasserin
|4 aut
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|a Mullen, Robert T
|e verfasserin
|4 aut
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|a Plaxton, William C
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 73(2022), 1 vom: 05. Jan., Seite 382-399
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
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|g volume:73
|g year:2022
|g number:1
|g day:05
|g month:01
|g pages:382-399
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|u http://dx.doi.org/10.1093/jxb/erab409
|3 Volltext
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