Isolation and characterization of a phosphatidylglycerophosphate phosphatase1, PGPP1, in Chlamydomonas reinhardtii

Copyright © 2015 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 92(2015) vom: 24. Juli, Seite 56-61
1. Verfasser: Hung, Chun-Hsien (VerfasserIn)
Weitere Verfasser: Kobayashi, Koichi, Wada, Hajime, Nakamura, Yuki
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2015
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Chlamydomonas reinhardtii Chloroplast Phosphatidylglycerol Phosphatidylglycerophosphate phosphatase Photosynthesis Phosphatidylglycerols Plant Proteins phosphatidylglycerophosphate mehr... Aspartic Acid 30KYC7MIAI Phosphoric Monoester Hydrolases EC 3.1.3.2
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245 1 0 |a Isolation and characterization of a phosphatidylglycerophosphate phosphatase1, PGPP1, in Chlamydomonas reinhardtii 
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520 |a Copyright © 2015 Elsevier Masson SAS. All rights reserved. 
520 |a Phosphatidylglycerol (PG) is the exclusive phospholipid synthesized in chloroplasts and plays important roles in photosynthesis. However, phosphatidylglycerophosphate phosphatase (PGPP), which catalyzes the final step of PG biosynthesis, is a missing piece in photosynthetic eukaryotes. Here, we isolated a previously uncharacterized haloacid dehalogenase-like phosphatase, designated CrPGPP1, as a putative PGPP in Chlamydomonas reinhardtii. CrPGPP1 complemented growth and lipid compositional defects in Δgep4, a yeast mutant of PGPP, which indicates that CrPGPP1 is a functional PGPP. Two aspartic acid residues, which are both essential for the yeast PGPP (Gep4p) activity, are also conserved in the putative catalytic motif of CrPGPP1. Site-specific mutagenesis showed that the first but not the second aspartic acid residue was required for CrPGPP1 to complement the growth defect of Δgep4 mutant, which highlights the distinct molecular features of CrPGPP1. Our results suggest that CrPGPP1 is a functional PGPP in C. reinhardtii, for the first PGPP in photosynthetic eukaryotes 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Chlamydomonas reinhardtii 
650 4 |a Chloroplast 
650 4 |a Phosphatidylglycerol 
650 4 |a Phosphatidylglycerophosphate phosphatase 
650 4 |a Photosynthesis 
650 7 |a Phosphatidylglycerols  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a phosphatidylglycerophosphate  |2 NLM 
650 7 |a Aspartic Acid  |2 NLM 
650 7 |a 30KYC7MIAI  |2 NLM 
650 7 |a Phosphoric Monoester Hydrolases  |2 NLM 
650 7 |a EC 3.1.3.2  |2 NLM 
700 1 |a Kobayashi, Koichi  |e verfasserin  |4 aut 
700 1 |a Wada, Hajime  |e verfasserin  |4 aut 
700 1 |a Nakamura, Yuki  |e verfasserin  |4 aut 
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773 1 8 |g volume:92  |g year:2015  |g day:24  |g month:07  |g pages:56-61 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2015.04.002  |3 Volltext 
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