Biosynthetic pathways of glycinebetaine in Thalassiosira pseudonana; functional characterization of enzyme catalyzing three-step methylation of glycine

Copyright © 2018 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 127(2018) vom: 10. Juni, Seite 248-255
1. Verfasser: Kageyama, Hakuto (VerfasserIn)
Weitere Verfasser: Tanaka, Yoshito, Takabe, Teruhiro
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2018
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Betaine Betaine synthetic pathway Choline dehydrogenase GSDMT Thalassiosira pseudonana 3SCV180C9W Methyltransferases EC 2.1.1.- Choline mehr... N91BDP6H0X Glycine TE7660XO1C
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245 1 0 |a Biosynthetic pathways of glycinebetaine in Thalassiosira pseudonana; functional characterization of enzyme catalyzing three-step methylation of glycine 
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500 |a Date Completed 26.07.2018 
500 |a Date Revised 30.09.2020 
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500 |a Citation Status MEDLINE 
520 |a Copyright © 2018 Elsevier Masson SAS. All rights reserved. 
520 |a Betaine (trimethylglycine) is an important compatible solute that accumulates in response to abiotic stresses such as drought and salinity. Biosynthetic pathways of betaine have been extensively studied, but it remains to be clarified on algae. A diatom Thalassiosira pseudonana CCMP1335 is an important component of marine ecosystems. Here we show that the genome sequence of Thalassiosira suggests the presence of two biosynthetic pathways for betaine, via three step methylation of glycine and via two step oxidation of choline. The choline oxidation via choline dehydrogenase was suggested and its sequential characteristics were analyzed. A candidate gene TpORF1 for glycine methylation encodes a protein consisted of 574 amino acids with two putative tandem repeat methyltransferase domains. The TpORF1 was expressed in E. coli, and the purified protein was shown to synthesize betaine via three step methylation of glycine and designated as TpGSDMT. The proteins containing C-terminal half or N-terminal half were expressed in E. coli and exhibited the methyl transferase activities with different substrate specificity for glycine, sarcosine and dimethylglycine. Upregulation of TpGSDMT transcription and betaine levels were observed at high salinity, suggesting the importance of TpGSDMT for salt tolerance in T. pseudonana cells 
650 4 |a Journal Article 
650 4 |a Betaine 
650 4 |a Betaine synthetic pathway 
650 4 |a Choline dehydrogenase 
650 4 |a GSDMT 
650 4 |a Thalassiosira pseudonana 
650 7 |a Betaine  |2 NLM 
650 7 |a 3SCV180C9W  |2 NLM 
650 7 |a Methyltransferases  |2 NLM 
650 7 |a EC 2.1.1.-  |2 NLM 
650 7 |a Choline  |2 NLM 
650 7 |a N91BDP6H0X  |2 NLM 
650 7 |a Glycine  |2 NLM 
650 7 |a TE7660XO1C  |2 NLM 
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 127(2018) vom: 10. Juni, Seite 248-255  |w (DE-627)NLM098178261  |x 1873-2690  |7 nnns 
773 1 8 |g volume:127  |g year:2018  |g day:10  |g month:06  |g pages:248-255 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2018.03.032  |3 Volltext 
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