Expression and functional characterization of sugar beet phosphoethanolamine/phosphocholine phosphatase under salt stress

Copyright © 2019 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 142(2019) vom: 01. Sept., Seite 211-216
1. Verfasser: Sahashi, Kosuke (VerfasserIn)
Weitere Verfasser: Yamada-Kato, Nana, Maeda, Takumi, Kito, Kunihide, Cha-Um, Suriyan, Rai, Vandna, Tanaka, Yoshito, Takabe, Teruhiro
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2019
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Betaine Choline Phosphocholine phosphatase Phosphoethanolamine phosphatase Salt stress Sugar beet Ethanolamines Plant Proteins Recombinant Proteins mehr... phosphorylethanolamine 78A2BX7AEU phosphocholine phosphatase EC 3.1.3.- Phosphoric Monoester Hydrolases EC 3.1.3.2 N91BDP6H0X
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100 1 |a Sahashi, Kosuke  |e verfasserin  |4 aut 
245 1 0 |a Expression and functional characterization of sugar beet phosphoethanolamine/phosphocholine phosphatase under salt stress 
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500 |a Date Completed 26.11.2019 
500 |a Date Revised 30.09.2020 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a Copyright © 2019 Elsevier Masson SAS. All rights reserved. 
520 |a Choline is a vital metabolite in plant and synthesized from phosphocholine by phosphocholine phosphatase. The Arabidopsis At1g17710 was identified as the first plant gene encoding the phosphatase for both phosphoethanolamine and phosphocholine (PECP) with much higher catalytic efficiency (>10-fold) for former. In betaine accumulating plants, choline is further required for betaine synthesis. In this report, we found three putative PECP genes in sugar beet, betaine accumulating plants. Two genes encode the proteins of 274 amino acid residues and designated as BvPECP1S and BvPECP2S. Another gene encodes the 331 amino acid protein (BvPECP2L) consisted of BvPECP2S with extra C-terminal amino acid. Enzymatic assays of BvPECP1S revealed that BvPECP1S exhibited the phosphatase activity for both phosphoethanolamine and phosphocholine with higher affinity (>1.8-fold) and catalytic efficiency (>2.64-fold) for phosphocholine. BvPECP2L exhibited low activity. RT-PCR experiments for BvPECP1S showed the increased expression in young leaf and root tip under salt-stress whereas the increased expression in all organs under phosphate deficiency. The expression level of BvPECP2L in salt stressed young leaf and root tip was induced by phosphate deficient. Physiological roles of BvPECP1S and BvPECP2L for the betaine synthesis were discussed 
650 4 |a Journal Article 
650 4 |a Betaine 
650 4 |a Choline 
650 4 |a Phosphocholine phosphatase 
650 4 |a Phosphoethanolamine phosphatase 
650 4 |a Salt stress 
650 4 |a Sugar beet 
650 7 |a Ethanolamines  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Recombinant Proteins  |2 NLM 
650 7 |a phosphorylethanolamine  |2 NLM 
650 7 |a 78A2BX7AEU  |2 NLM 
650 7 |a phosphocholine phosphatase  |2 NLM 
650 7 |a EC 3.1.3.-  |2 NLM 
650 7 |a Phosphoric Monoester Hydrolases  |2 NLM 
650 7 |a EC 3.1.3.2  |2 NLM 
650 7 |a Choline  |2 NLM 
650 7 |a N91BDP6H0X  |2 NLM 
700 1 |a Yamada-Kato, Nana  |e verfasserin  |4 aut 
700 1 |a Maeda, Takumi  |e verfasserin  |4 aut 
700 1 |a Kito, Kunihide  |e verfasserin  |4 aut 
700 1 |a Cha-Um, Suriyan  |e verfasserin  |4 aut 
700 1 |a Rai, Vandna  |e verfasserin  |4 aut 
700 1 |a Tanaka, Yoshito  |e verfasserin  |4 aut 
700 1 |a Takabe, Teruhiro  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Plant physiology and biochemistry : PPB  |d 1991  |g 142(2019) vom: 01. Sept., Seite 211-216  |w (DE-627)NLM098178261  |x 1873-2690  |7 nnns 
773 1 8 |g volume:142  |g year:2019  |g day:01  |g month:09  |g pages:211-216 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2019.07.011  |3 Volltext 
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