Cross-reconstitution of various extrinsic proteins and Photosystem II complexes from Cyanobacteria, red algae and higher plants

Isao Enami, Shizue Yoshihara, Akihiro Tohri, Akinori Okumura, Hisataka Ohta, Jian-Ren Shen

Research output: Contribution to journalArticle

60 Citations (Scopus)

Abstract

Photosystem II (PSII) contains different extrinsic proteins required for oxygen evolution among different organisms. Cyanobacterial PSII contains the 33 kDa, 12 kDa proteins and cytochrome (cyt) c-550; red algal PSII contains a 20 kDa protein in addition to the three homologous cyanobacterial proteins; whereas higher plant PSII contains the 33 kDa, 23 kDa and 17 kDa proteins. In order to understand the binding and functional properties of these proteins, we performed cross-reconstitution experiments with combinations of PSII and extrinsic proteins from three different sources: Higher plant (spinach), red alga (Cyanidium caldarium) and cyanobacterium (Synechococcus vulcanus). Among all of the extrinsic proteins, the 33 kDa protein is common to all of the organisms and is totally exchangeable in binding to PSII from any of the three organisms. Oxygen evolution of higher plant and red algal PSII was restored to a more or less similar level by binding of any one of the three 33 kDa proteins, whereas oxygen evolution of cyanobacterial PSII was restored to a larger extent with its own 33 kDa protein than with the 33 kDa protein from other sources. In addition to the 33 kDa protein, the red algal 20 kDa, 12 kDa proteins and cyt c-550 were able to bind to cyanobacterial and higher plant PSII, leading to a partial restoration of oxygen evolution in both organisms. The cyanobacterial 12 kDa protein and cyt c-550 partially bound to the red algal PSII, but this binding did not restore oxygen evolution. The higher plant 23 kDa and 17 kDa proteins bound to the cyanobacterial and red algal PSII only through non-specific interactions. Thus, only the red algal extrinsic proteins are partially functional in both the cyanobacterial and higher plant PSII, which implies a possible intermediate position of the red algal PSII during its evolution from cyanobacteria to higher plants.

Original languageEnglish
Pages (from-to)1354-1364
Number of pages11
JournalPlant and Cell Physiology
Volume41
Issue number12
Publication statusPublished - 2000
Externally publishedYes

Fingerprint

Rhodophyta
Photosystem II Protein Complex
Cyanobacteria
photosystem II
Proteins
proteins
Algal Proteins
Oxygen
cytochrome c
Cytochromes c
organisms
Synechococcus vulcanus
algal proteins
Cyanidium caldarium
Synechococcus
Spinacia oleracea
binding properties

Keywords

  • Evolution
  • Extrinsic proteins
  • Oxygen evolution
  • Photosynthesis
  • Photosystem II
  • Reconstitution

ASJC Scopus subject areas

  • Plant Science
  • Physiology
  • Cell Biology

Cite this

Cross-reconstitution of various extrinsic proteins and Photosystem II complexes from Cyanobacteria, red algae and higher plants. / Enami, Isao; Yoshihara, Shizue; Tohri, Akihiro; Okumura, Akinori; Ohta, Hisataka; Shen, Jian-Ren.

In: Plant and Cell Physiology, Vol. 41, No. 12, 2000, p. 1354-1364.

Research output: Contribution to journalArticle

Enami, Isao ; Yoshihara, Shizue ; Tohri, Akihiro ; Okumura, Akinori ; Ohta, Hisataka ; Shen, Jian-Ren. / Cross-reconstitution of various extrinsic proteins and Photosystem II complexes from Cyanobacteria, red algae and higher plants. In: Plant and Cell Physiology. 2000 ; Vol. 41, No. 12. pp. 1354-1364.
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AU - Enami, Isao

AU - Yoshihara, Shizue

AU - Tohri, Akihiro

AU - Okumura, Akinori

AU - Ohta, Hisataka

AU - Shen, Jian-Ren

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AB - Photosystem II (PSII) contains different extrinsic proteins required for oxygen evolution among different organisms. Cyanobacterial PSII contains the 33 kDa, 12 kDa proteins and cytochrome (cyt) c-550; red algal PSII contains a 20 kDa protein in addition to the three homologous cyanobacterial proteins; whereas higher plant PSII contains the 33 kDa, 23 kDa and 17 kDa proteins. In order to understand the binding and functional properties of these proteins, we performed cross-reconstitution experiments with combinations of PSII and extrinsic proteins from three different sources: Higher plant (spinach), red alga (Cyanidium caldarium) and cyanobacterium (Synechococcus vulcanus). Among all of the extrinsic proteins, the 33 kDa protein is common to all of the organisms and is totally exchangeable in binding to PSII from any of the three organisms. Oxygen evolution of higher plant and red algal PSII was restored to a more or less similar level by binding of any one of the three 33 kDa proteins, whereas oxygen evolution of cyanobacterial PSII was restored to a larger extent with its own 33 kDa protein than with the 33 kDa protein from other sources. In addition to the 33 kDa protein, the red algal 20 kDa, 12 kDa proteins and cyt c-550 were able to bind to cyanobacterial and higher plant PSII, leading to a partial restoration of oxygen evolution in both organisms. The cyanobacterial 12 kDa protein and cyt c-550 partially bound to the red algal PSII, but this binding did not restore oxygen evolution. The higher plant 23 kDa and 17 kDa proteins bound to the cyanobacterial and red algal PSII only through non-specific interactions. Thus, only the red algal extrinsic proteins are partially functional in both the cyanobacterial and higher plant PSII, which implies a possible intermediate position of the red algal PSII during its evolution from cyanobacteria to higher plants.

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KW - Reconstitution

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