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 language | English |
|---|---|
| Pages (from-to) | 754-761 |
| Number of pages | 8 |
| Journal | Plant and Cell Physiology |
| Volume | 37 |
| Issue number | 6 |
| Publication status | Published - Sep 1996 |
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Keywords
- D1 protein
- Photosystem I
- Photosystem II
- Pisum sativum
- Redox control
- Translation
ASJC Scopus subject areas
- Plant Science
- Cell Biology
- Physiology
Cite this
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. / Kuroda, Hiroshi; Kobashi, Kumiko; Kaseyama, Hiroyuki; Satoh, Kimiyuki.
In: Plant and Cell Physiology, Vol. 37, No. 6, 09.1996, p. 754-761.Research output: Contribution to journal › Article
}
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.
KW - D1 protein
KW - Photosystem I
KW - Photosystem II
KW - Pisum sativum
KW - Redox control
KW - Translation
UR - http://www.scopus.com/inward/record.url?scp=0029808927&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0029808927&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0029808927
VL - 37
SP - 754
EP - 761
JO - Plant and Cell Physiology
JF - Plant and Cell Physiology
SN - 0032-0781
IS - 6
ER -