Effects of phospholipase and lipase treatments on photosystem II core dimer from a thermophilic cyanobacterium

Jing Leng, Isamu Sakurai, Hajime Wada, Jian-Ren Shen

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Lipids are important components of transmembrane protein complexes. In order to study the roles of lipids in photosystem II (PSII), we treated the PSII core dimer complex from a thermophilic cyanobacterium Thermosynechococcus vulcanus with phospholipase A2 (PLA2) and lipase, and examined their effects on PSII structure and function. PLA2-treatment decreased the content of phospholipid, phosphatidylglycerol (PG) by 59%, leading to a decrease of oxygen evolution by 40%. On the other hand, although treatment with lipase specifically decreased the content of monogalactosyldiacylglycerol (MGDG) by 52%, it decreased oxygen evolution only by 16%. This indicates that PG plays a more important role in PSII than MGDG. Both PLA2- and lipase-treatments induced neither the dissociation of PSII dimer, nor any loss of polypeptides. The degradation of PG resulted in a damage to the QB-binding site as demonstrated from photoreduction activity of 2,6-dichlorophenolindophenol and chlorophyll fluorescence yields in the absence or presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea, and the dependencies of oxygen evolution on various electron acceptors before and after PLA2- or lipase-treatments. However, there were approximately three and five molecules of PG and MGDG per PSII reaction center left in the PSII dimeric complex after the PLA2- and lipase-treatments. These lipids are therefore bound to the interior of the protein matrix and resistant to the lipase treatments. The resistance of these lipids against PLA2- and lipase-treatments may be a specific feature of PSII from the thermophilic cyanobacterium, suggesting a possible correlation between binding of lipids and thermostability of PSII.

Original languageEnglish
Pages (from-to)469-478
Number of pages10
JournalPhotosynthesis Research
Volume98
Issue number1-3
DOIs
Publication statusPublished - Oct 2008

Fingerprint

Photosystem II Protein Complex
Phospholipases
Cyanobacteria
Lipase
Dimers
photosystem II
phospholipase A2
Phospholipases A2
Phosphatidylglycerols
phosphatidylglycerols
Lipids
lipids
Oxygen
Thermosynechococcus vulcanus
2,6-Dichloroindophenol
Diuron
phospholipases
transmembrane proteins
Chlorophyll
thermal stability

Keywords

  • Cyanobacteria
  • Lipids
  • Oxygen evolution
  • Phospholipase- treatment
  • Phospholipid
  • Photosystem II

ASJC Scopus subject areas

  • Plant Science
  • Cell Biology
  • Biochemistry

Cite this

Effects of phospholipase and lipase treatments on photosystem II core dimer from a thermophilic cyanobacterium. / Leng, Jing; Sakurai, Isamu; Wada, Hajime; Shen, Jian-Ren.

In: Photosynthesis Research, Vol. 98, No. 1-3, 10.2008, p. 469-478.

Research output: Contribution to journalArticle

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abstract = "Lipids are important components of transmembrane protein complexes. In order to study the roles of lipids in photosystem II (PSII), we treated the PSII core dimer complex from a thermophilic cyanobacterium Thermosynechococcus vulcanus with phospholipase A2 (PLA2) and lipase, and examined their effects on PSII structure and function. PLA2-treatment decreased the content of phospholipid, phosphatidylglycerol (PG) by 59{\%}, leading to a decrease of oxygen evolution by 40{\%}. On the other hand, although treatment with lipase specifically decreased the content of monogalactosyldiacylglycerol (MGDG) by 52{\%}, it decreased oxygen evolution only by 16{\%}. This indicates that PG plays a more important role in PSII than MGDG. Both PLA2- and lipase-treatments induced neither the dissociation of PSII dimer, nor any loss of polypeptides. The degradation of PG resulted in a damage to the QB-binding site as demonstrated from photoreduction activity of 2,6-dichlorophenolindophenol and chlorophyll fluorescence yields in the absence or presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea, and the dependencies of oxygen evolution on various electron acceptors before and after PLA2- or lipase-treatments. However, there were approximately three and five molecules of PG and MGDG per PSII reaction center left in the PSII dimeric complex after the PLA2- and lipase-treatments. These lipids are therefore bound to the interior of the protein matrix and resistant to the lipase treatments. The resistance of these lipids against PLA2- and lipase-treatments may be a specific feature of PSII from the thermophilic cyanobacterium, suggesting a possible correlation between binding of lipids and thermostability of PSII.",
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