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

被引:10
作者
Hung, Chun-Hsien [1 ]
Kobayashi, Koichi [2 ]
Wada, Hajime [2 ,3 ]
Nakamura, Yuki [1 ,4 ]
机构
[1] Acad Sinica, Inst Plant & Microbial Biol, Taipei 11529, Taiwan
[2] Univ Tokyo, Grad Sch Arts & Sci, Dept Life Sci, Tokyo 1138654, Japan
[3] Japan Sci & Technol Agcy, CREST, Saitamd, Japan
[4] Japan Sci & Technol Agcy, PRESTO, Saitama, Japan
基金
日本科学技术振兴机构;
关键词
Chlamydomonas reinhardtii; Chloroplast; Phosphatidylglycerol; Phosphatidylglycerophosphate phosphatase; Photosynthesis; CARDIOLIPIN SYNTHASE; PHOTOSYSTEM-II; ARABIDOPSIS; BIOSYNTHESIS; REQUIREMENT; CHLOROPLASTS; MITOCHONDRIA; PATHWAY; MUTANT; GENES;
D O I
10.1016/j.plaphy.2015.04.002
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
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 Delta gep4, 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 Delta gep4 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. (C) 2015 Elsevier Masson SAS. All rights reserved.
引用
收藏
页码:56 / 61
页数:6
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