Comparison of binding and functional properties of two extrinsic components, Cyt c550 and a 12 kDa protein, in cyanobacterial PSII with those in red algal PSII

Isao Enami, Masako Iwai, Ai Akiyama, Takehiro Suzuki, Akinori Okumura, Takara Katoh, Osamu Tada, Hisataka Ohta, Jian-Ren Shen

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Cyt c550 and 12 kDa protein are two extrinsic proteins of photosystem II (PSII) found in cyanobacteria and some eukaryotic algae. The binding patterns of these two extrinsic proteins are different between cyanobacterial (Thermosynechococcus vulcanus) and red algal (Cyanidium caldarium) PSIIs [Shen and Inoue (1993) Biochemistry 32: 1825; Enami et al. (1998) Biochemistry 39: 2787]. In order to elucidate the possible causes responsible for these differences, we first cloned the psbV gene encoding Cyt c550 from a red alga, Cyanidium caldarium, which was compared with the homologous sequences from other organisms. Cross-reconstitution experiments were then performed with different combinations of the extrinsic proteins and the cyanobacterial or red algal PSII. (1) Both the cyanobacterial and red algal Cyt c550 bound directly to the cyanobacterial PSII, whereas none of them bound directly to the red algal PSII, indicating that direct binding of Cyt c550 to PSII principally depends on the structure of PSII intrinsic proteins but not that of Cyt c550 itself. (2) Cyt c550 was functionally exchangeable between the red algal and the cyanobacterial PSII, and the red algal 12 kDa protein functionally bound to the cyanobacterial PSII, whereas the cyanobacterial 12 kDa protein did not bind to the red algal PSII. (3) The antibody against the cyanobacterial or red algal 12 kDa protein reacted with its original one but not with the homologous protein from the other organism, whereas the antibody against the red algal Cyt c550 reacted with both cyanobacterial and red algal Cyt c550. These results imply that the structure and function of Cyt c550 have been largely conserved, whereas those of the 12 kDa protein have been changed, in the two organisms studied here.

Original languageEnglish
Pages (from-to)820-827
Number of pages8
JournalPlant and Cell Physiology
Volume44
Issue number8
DOIs
Publication statusPublished - Aug 1 2003
Externally publishedYes

Fingerprint

Photosystem II Protein Complex
binding properties
photosystem II
functional properties
Proteins
proteins
Cyanidium caldarium
algae
Thermosynechococcus vulcanus
Biochemistry
biochemistry
organisms
Rhodophyta
antibodies
Antibodies
Cyanobacteria
Sequence Homology
sequence homology

Keywords

  • 12 kDa protein
  • Cyanobacteria
  • Cyt c550
  • Extrinsic protein
  • Red algae

ASJC Scopus subject areas

  • Plant Science
  • Physiology
  • Cell Biology

Cite this

Comparison of binding and functional properties of two extrinsic components, Cyt c550 and a 12 kDa protein, in cyanobacterial PSII with those in red algal PSII. / Enami, Isao; Iwai, Masako; Akiyama, Ai; Suzuki, Takehiro; Okumura, Akinori; Katoh, Takara; Tada, Osamu; Ohta, Hisataka; Shen, Jian-Ren.

In: Plant and Cell Physiology, Vol. 44, No. 8, 01.08.2003, p. 820-827.

Research output: Contribution to journalArticle

Enami, Isao ; Iwai, Masako ; Akiyama, Ai ; Suzuki, Takehiro ; Okumura, Akinori ; Katoh, Takara ; Tada, Osamu ; Ohta, Hisataka ; Shen, Jian-Ren. / Comparison of binding and functional properties of two extrinsic components, Cyt c550 and a 12 kDa protein, in cyanobacterial PSII with those in red algal PSII. In: Plant and Cell Physiology. 2003 ; Vol. 44, No. 8. pp. 820-827.
@article{9d9825245a604197ae1ffc3964d97300,
title = "Comparison of binding and functional properties of two extrinsic components, Cyt c550 and a 12 kDa protein, in cyanobacterial PSII with those in red algal PSII",
abstract = "Cyt c550 and 12 kDa protein are two extrinsic proteins of photosystem II (PSII) found in cyanobacteria and some eukaryotic algae. The binding patterns of these two extrinsic proteins are different between cyanobacterial (Thermosynechococcus vulcanus) and red algal (Cyanidium caldarium) PSIIs [Shen and Inoue (1993) Biochemistry 32: 1825; Enami et al. (1998) Biochemistry 39: 2787]. In order to elucidate the possible causes responsible for these differences, we first cloned the psbV gene encoding Cyt c550 from a red alga, Cyanidium caldarium, which was compared with the homologous sequences from other organisms. Cross-reconstitution experiments were then performed with different combinations of the extrinsic proteins and the cyanobacterial or red algal PSII. (1) Both the cyanobacterial and red algal Cyt c550 bound directly to the cyanobacterial PSII, whereas none of them bound directly to the red algal PSII, indicating that direct binding of Cyt c550 to PSII principally depends on the structure of PSII intrinsic proteins but not that of Cyt c550 itself. (2) Cyt c550 was functionally exchangeable between the red algal and the cyanobacterial PSII, and the red algal 12 kDa protein functionally bound to the cyanobacterial PSII, whereas the cyanobacterial 12 kDa protein did not bind to the red algal PSII. (3) The antibody against the cyanobacterial or red algal 12 kDa protein reacted with its original one but not with the homologous protein from the other organism, whereas the antibody against the red algal Cyt c550 reacted with both cyanobacterial and red algal Cyt c550. These results imply that the structure and function of Cyt c550 have been largely conserved, whereas those of the 12 kDa protein have been changed, in the two organisms studied here.",
keywords = "12 kDa protein, Cyanobacteria, Cyt c550, Extrinsic protein, Red algae",
author = "Isao Enami and Masako Iwai and Ai Akiyama and Takehiro Suzuki and Akinori Okumura and Takara Katoh and Osamu Tada and Hisataka Ohta and Jian-Ren Shen",
year = "2003",
month = "8",
day = "1",
doi = "10.1093/pcp/pcg106",
language = "English",
volume = "44",
pages = "820--827",
journal = "Plant and Cell Physiology",
issn = "0032-0781",
publisher = "Oxford University Press",
number = "8",

}

TY - JOUR

T1 - Comparison of binding and functional properties of two extrinsic components, Cyt c550 and a 12 kDa protein, in cyanobacterial PSII with those in red algal PSII

AU - Enami, Isao

AU - Iwai, Masako

AU - Akiyama, Ai

AU - Suzuki, Takehiro

AU - Okumura, Akinori

AU - Katoh, Takara

AU - Tada, Osamu

AU - Ohta, Hisataka

AU - Shen, Jian-Ren

PY - 2003/8/1

Y1 - 2003/8/1

N2 - Cyt c550 and 12 kDa protein are two extrinsic proteins of photosystem II (PSII) found in cyanobacteria and some eukaryotic algae. The binding patterns of these two extrinsic proteins are different between cyanobacterial (Thermosynechococcus vulcanus) and red algal (Cyanidium caldarium) PSIIs [Shen and Inoue (1993) Biochemistry 32: 1825; Enami et al. (1998) Biochemistry 39: 2787]. In order to elucidate the possible causes responsible for these differences, we first cloned the psbV gene encoding Cyt c550 from a red alga, Cyanidium caldarium, which was compared with the homologous sequences from other organisms. Cross-reconstitution experiments were then performed with different combinations of the extrinsic proteins and the cyanobacterial or red algal PSII. (1) Both the cyanobacterial and red algal Cyt c550 bound directly to the cyanobacterial PSII, whereas none of them bound directly to the red algal PSII, indicating that direct binding of Cyt c550 to PSII principally depends on the structure of PSII intrinsic proteins but not that of Cyt c550 itself. (2) Cyt c550 was functionally exchangeable between the red algal and the cyanobacterial PSII, and the red algal 12 kDa protein functionally bound to the cyanobacterial PSII, whereas the cyanobacterial 12 kDa protein did not bind to the red algal PSII. (3) The antibody against the cyanobacterial or red algal 12 kDa protein reacted with its original one but not with the homologous protein from the other organism, whereas the antibody against the red algal Cyt c550 reacted with both cyanobacterial and red algal Cyt c550. These results imply that the structure and function of Cyt c550 have been largely conserved, whereas those of the 12 kDa protein have been changed, in the two organisms studied here.

AB - Cyt c550 and 12 kDa protein are two extrinsic proteins of photosystem II (PSII) found in cyanobacteria and some eukaryotic algae. The binding patterns of these two extrinsic proteins are different between cyanobacterial (Thermosynechococcus vulcanus) and red algal (Cyanidium caldarium) PSIIs [Shen and Inoue (1993) Biochemistry 32: 1825; Enami et al. (1998) Biochemistry 39: 2787]. In order to elucidate the possible causes responsible for these differences, we first cloned the psbV gene encoding Cyt c550 from a red alga, Cyanidium caldarium, which was compared with the homologous sequences from other organisms. Cross-reconstitution experiments were then performed with different combinations of the extrinsic proteins and the cyanobacterial or red algal PSII. (1) Both the cyanobacterial and red algal Cyt c550 bound directly to the cyanobacterial PSII, whereas none of them bound directly to the red algal PSII, indicating that direct binding of Cyt c550 to PSII principally depends on the structure of PSII intrinsic proteins but not that of Cyt c550 itself. (2) Cyt c550 was functionally exchangeable between the red algal and the cyanobacterial PSII, and the red algal 12 kDa protein functionally bound to the cyanobacterial PSII, whereas the cyanobacterial 12 kDa protein did not bind to the red algal PSII. (3) The antibody against the cyanobacterial or red algal 12 kDa protein reacted with its original one but not with the homologous protein from the other organism, whereas the antibody against the red algal Cyt c550 reacted with both cyanobacterial and red algal Cyt c550. These results imply that the structure and function of Cyt c550 have been largely conserved, whereas those of the 12 kDa protein have been changed, in the two organisms studied here.

KW - 12 kDa protein

KW - Cyanobacteria

KW - Cyt c550

KW - Extrinsic protein

KW - Red algae

UR - http://www.scopus.com/inward/record.url?scp=0041783532&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0041783532&partnerID=8YFLogxK

U2 - 10.1093/pcp/pcg106

DO - 10.1093/pcp/pcg106

M3 - Article

C2 - 12941874

AN - SCOPUS:0041783532

VL - 44

SP - 820

EP - 827

JO - Plant and Cell Physiology

JF - Plant and Cell Physiology

SN - 0032-0781

IS - 8

ER -