Possible involvement of a low redox potential component(s) downstream of photosystem I in the translational regulation of the D1 subunit of the photosystem II reaction center in isolated pea chloroplasts

Hiroshi Kuroda, Kumiko Kobashi, Hiroyuki Kaseyama, Kimiyuki Satoh

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28 Citations (Scopus)

Abstract

Accumulation of the precursor and the mature form of the D1 protein of the photosystem II reaction center in illuminated pea chloroplasts was prevented by the addition of the inhibitors atrazine, 3-(3,4-dichlorophenyl)- 1,1-dimethylurea and 3,5-dibromo-4-hydroxybenzonitrile. Under such conditions, the compensatory accumulation of two translational intermediates of the D1 protein, of 22 and 24 kDa, respectively, was induced by the addition of ATP, as also observed in darkness in the presence of ATP [Taniguchi et al. (1993) FEBS Lett. 317: 57], suggesting that the synthesis of the full-length D1 protein requires a factor that is generated by the operation of photosynthetic electron transport. The accumulation of the full- length D1 protein was induced in the light, even in the presence of atrazine, when both 2,6-dichlorophenolindophenol and ascorbate were also present and in darkness upon the addition of dithiothreitol. Moreover, reagents with a relatively low redox potential, namely, duroquinone and methylviologen, prevented the accumulation. These observations suggest that the translation of the D1 protein might be regulated at specific steps during the elongation of the polypeptide via a redox change in a component around photosystem I. Results of pre-illumination experiments indicate that the factor needed for the accumulation of D1 protein is relatively stable and retains its activity in darkness after exposure to light.

Original languageEnglish
Pages (from-to)754-761
Number of pages8
JournalPlant and Cell Physiology
Volume37
Issue number6
Publication statusPublished - Sep 1996

Fingerprint

Photosystem I Protein Complex
D1 protein
Photosystem II Protein Complex
photosystem I
Peas
redox potential
Chloroplasts
photosystem II
Oxidation-Reduction
peas
chloroplasts
Darkness
Atrazine
Proteins
atrazine
Adenosine Triphosphate
2,6-Dichloroindophenol
Diuron
Light
Dithiothreitol

Keywords

  • D1 protein
  • Photosystem I
  • Photosystem II
  • Pisum sativum
  • Redox control
  • Translation

ASJC Scopus subject areas

  • Plant Science
  • Cell Biology
  • Physiology

Cite this

@article{7e8dc342bac0425686201cb67fbb3422,
title = "Possible involvement of a low redox potential component(s) downstream of photosystem I in the translational regulation of the D1 subunit of the photosystem II reaction center in isolated pea chloroplasts",
abstract = "Accumulation of the precursor and the mature form of the D1 protein of the photosystem II reaction center in illuminated pea chloroplasts was prevented by the addition of the inhibitors atrazine, 3-(3,4-dichlorophenyl)- 1,1-dimethylurea and 3,5-dibromo-4-hydroxybenzonitrile. Under such conditions, the compensatory accumulation of two translational intermediates of the D1 protein, of 22 and 24 kDa, respectively, was induced by the addition of ATP, as also observed in darkness in the presence of ATP [Taniguchi et al. (1993) FEBS Lett. 317: 57], suggesting that the synthesis of the full-length D1 protein requires a factor that is generated by the operation of photosynthetic electron transport. The accumulation of the full- length D1 protein was induced in the light, even in the presence of atrazine, when both 2,6-dichlorophenolindophenol and ascorbate were also present and in darkness upon the addition of dithiothreitol. Moreover, reagents with a relatively low redox potential, namely, duroquinone and methylviologen, prevented the accumulation. These observations suggest that the translation of the D1 protein might be regulated at specific steps during the elongation of the polypeptide via a redox change in a component around photosystem I. Results of pre-illumination experiments indicate that the factor needed for the accumulation of D1 protein is relatively stable and retains its activity in darkness after exposure to light.",
keywords = "D1 protein, Photosystem I, Photosystem II, Pisum sativum, Redox control, Translation",
author = "Hiroshi Kuroda and Kumiko Kobashi and Hiroyuki Kaseyama and Kimiyuki Satoh",
year = "1996",
month = "9",
language = "English",
volume = "37",
pages = "754--761",
journal = "Plant and Cell Physiology",
issn = "0032-0781",
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TY - JOUR

T1 - Possible involvement of a low redox potential component(s) downstream of photosystem I in the translational regulation of the D1 subunit of the photosystem II reaction center in isolated pea chloroplasts

AU - Kuroda, Hiroshi

AU - Kobashi, Kumiko

AU - Kaseyama, Hiroyuki

AU - Satoh, Kimiyuki

PY - 1996/9

Y1 - 1996/9

N2 - Accumulation of the precursor and the mature form of the D1 protein of the photosystem II reaction center in illuminated pea chloroplasts was prevented by the addition of the inhibitors atrazine, 3-(3,4-dichlorophenyl)- 1,1-dimethylurea and 3,5-dibromo-4-hydroxybenzonitrile. Under such conditions, the compensatory accumulation of two translational intermediates of the D1 protein, of 22 and 24 kDa, respectively, was induced by the addition of ATP, as also observed in darkness in the presence of ATP [Taniguchi et al. (1993) FEBS Lett. 317: 57], suggesting that the synthesis of the full-length D1 protein requires a factor that is generated by the operation of photosynthetic electron transport. The accumulation of the full- length D1 protein was induced in the light, even in the presence of atrazine, when both 2,6-dichlorophenolindophenol and ascorbate were also present and in darkness upon the addition of dithiothreitol. Moreover, reagents with a relatively low redox potential, namely, duroquinone and methylviologen, prevented the accumulation. These observations suggest that the translation of the D1 protein might be regulated at specific steps during the elongation of the polypeptide via a redox change in a component around photosystem I. Results of pre-illumination experiments indicate that the factor needed for the accumulation of D1 protein is relatively stable and retains its activity in darkness after exposure to light.

AB - Accumulation of the precursor and the mature form of the D1 protein of the photosystem II reaction center in illuminated pea chloroplasts was prevented by the addition of the inhibitors atrazine, 3-(3,4-dichlorophenyl)- 1,1-dimethylurea and 3,5-dibromo-4-hydroxybenzonitrile. Under such conditions, the compensatory accumulation of two translational intermediates of the D1 protein, of 22 and 24 kDa, respectively, was induced by the addition of ATP, as also observed in darkness in the presence of ATP [Taniguchi et al. (1993) FEBS Lett. 317: 57], suggesting that the synthesis of the full-length D1 protein requires a factor that is generated by the operation of photosynthetic electron transport. The accumulation of the full- length D1 protein was induced in the light, even in the presence of atrazine, when both 2,6-dichlorophenolindophenol and ascorbate were also present and in darkness upon the addition of dithiothreitol. Moreover, reagents with a relatively low redox potential, namely, duroquinone and methylviologen, prevented the accumulation. These observations suggest that the translation of the D1 protein might be regulated at specific steps during the elongation of the polypeptide via a redox change in a component around photosystem I. Results of pre-illumination experiments indicate that the factor needed for the accumulation of D1 protein is relatively stable and retains its activity in darkness after exposure to light.

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