Involvement of the CP47 protein in stabilization and photoactivation of a functional water-oxidizing complex in the cyanobacterium synechocystis sp. PCC 6803

Hermann M. Gleiter, Elisabeth Haag, Jian Ren Shen, Julian J. Eaton-Rye, Angela G. Seeliger, Yorinao Inoue, Willem Vermaas, Gernot Renger

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Abstract

Oscillation patterns of the oxygen yield per flash induced by a train of single-turnover flashes were measured as a function of dark incubation and different pre-illumination conditions in several autotrophic mutant strains of Synechocystis sp. PCC 6803 carrying short deletions within the large, lumen-exposed hydrophilic region (loop E) of the chlorophyll a-binding photosystem II protein CP47. A physiological and biochemical characterization of these mutant strains has been presented previously [Eaton-Rye, J. J., & Vermaas, W. F. J. (1991) Plant Mol. Biol. 17, 1165-1177; Haag, E., Eaton-Rye, J. J., Renger, G., & Vermaas, W. F. J. (1993) Biochemistry 32, 4444-4454], and some functional properties were described recently [Gleiter, H. M., Haag, E., Shen, J.-R., Eaton-Rye, J. J., Inoue, Y., Vermaas, W. F. J., & Renger, G. (1994) Biochemistry 33, 12063-12071]. The present study shows that in several mutants the water-oxidizing complex (WOC) became inactivated during prolonged dark incubation, whereas the WOC of the wild-type strain remained active. The rate and extent of the inactivation in the mutants depend on the domain of loop E, where 3-8 amino acid residues were deleted. The most pronounced effects are observed in mutants Δ(A373-D380) and Δ(R384-V392). A competent WOC can be restored from the fully inactivated state by illumination with short saturating flashes. The number of flashes required for this process strongly depends on the site at which a deletion has been introduced into loop E. Again, the most prominent effects were found in mutants Δ(A373-D380) and Δ(R384-V392). Interestingly, the number of flashes required for activation was reduced by more than an order of magnitude in both mutants by the addition of 10 mM CaCl2 to the cell suspension. On the basis of a model for photoactivation proposed by Tamura and Cheniae (1987) [Biochim. Biophys. Acta 890, 179-194], a scheme is presented for the processes of dark inactivation and photoactivation in these mutants. The results presented here corroborate an important role of the large hydrophilic domain (loop E) of CP47 in a functional and stable WOC.

Original languageEnglish (US)
Pages (from-to)6847-6856
Number of pages10
JournalBiochemistry®
Volume34
Issue number20
StatePublished - 1995

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Synechocystis
Cyanobacteria
Stabilization
Biochemistry
Water
Lighting
Proteins
Suspensions
Chemical activation
Oxygen
Amino Acids
Secale

ASJC Scopus subject areas

  • Biochemistry

Cite this

Gleiter, H. M., Haag, E., Shen, J. R., Eaton-Rye, J. J., Seeliger, A. G., Inoue, Y., ... Renger, G. (1995). Involvement of the CP47 protein in stabilization and photoactivation of a functional water-oxidizing complex in the cyanobacterium synechocystis sp. PCC 6803. Biochemistry®, 34(20), 6847-6856.

Involvement of the CP47 protein in stabilization and photoactivation of a functional water-oxidizing complex in the cyanobacterium synechocystis sp. PCC 6803. / Gleiter, Hermann M.; Haag, Elisabeth; Shen, Jian Ren; Eaton-Rye, Julian J.; Seeliger, Angela G.; Inoue, Yorinao; Vermaas, Willem; Renger, Gernot.

In: Biochemistry®, Vol. 34, No. 20, 1995, p. 6847-6856.

Research output: Contribution to journalArticle

Gleiter, HM, Haag, E, Shen, JR, Eaton-Rye, JJ, Seeliger, AG, Inoue, Y, Vermaas, W & Renger, G 1995, 'Involvement of the CP47 protein in stabilization and photoactivation of a functional water-oxidizing complex in the cyanobacterium synechocystis sp. PCC 6803', Biochemistry®, vol. 34, no. 20, pp. 6847-6856.
Gleiter, Hermann M. ; Haag, Elisabeth ; Shen, Jian Ren ; Eaton-Rye, Julian J. ; Seeliger, Angela G. ; Inoue, Yorinao ; Vermaas, Willem ; Renger, Gernot. / Involvement of the CP47 protein in stabilization and photoactivation of a functional water-oxidizing complex in the cyanobacterium synechocystis sp. PCC 6803. In: Biochemistry®. 1995 ; Vol. 34, No. 20. pp. 6847-6856.
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abstract = "Oscillation patterns of the oxygen yield per flash induced by a train of single-turnover flashes were measured as a function of dark incubation and different pre-illumination conditions in several autotrophic mutant strains of Synechocystis sp. PCC 6803 carrying short deletions within the large, lumen-exposed hydrophilic region (loop E) of the chlorophyll a-binding photosystem II protein CP47. A physiological and biochemical characterization of these mutant strains has been presented previously [Eaton-Rye, J. J., & Vermaas, W. F. J. (1991) Plant Mol. Biol. 17, 1165-1177; Haag, E., Eaton-Rye, J. J., Renger, G., & Vermaas, W. F. J. (1993) Biochemistry 32, 4444-4454], and some functional properties were described recently [Gleiter, H. M., Haag, E., Shen, J.-R., Eaton-Rye, J. J., Inoue, Y., Vermaas, W. F. J., & Renger, G. (1994) Biochemistry 33, 12063-12071]. The present study shows that in several mutants the water-oxidizing complex (WOC) became inactivated during prolonged dark incubation, whereas the WOC of the wild-type strain remained active. The rate and extent of the inactivation in the mutants depend on the domain of loop E, where 3-8 amino acid residues were deleted. The most pronounced effects are observed in mutants Δ(A373-D380) and Δ(R384-V392). A competent WOC can be restored from the fully inactivated state by illumination with short saturating flashes. The number of flashes required for this process strongly depends on the site at which a deletion has been introduced into loop E. Again, the most prominent effects were found in mutants Δ(A373-D380) and Δ(R384-V392). Interestingly, the number of flashes required for activation was reduced by more than an order of magnitude in both mutants by the addition of 10 mM CaCl2 to the cell suspension. On the basis of a model for photoactivation proposed by Tamura and Cheniae (1987) [Biochim. Biophys. Acta 890, 179-194], a scheme is presented for the processes of dark inactivation and photoactivation in these mutants. The results presented here corroborate an important role of the large hydrophilic domain (loop E) of CP47 in a functional and stable WOC.",
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T1 - Involvement of the CP47 protein in stabilization and photoactivation of a functional water-oxidizing complex in the cyanobacterium synechocystis sp. PCC 6803

AU - Gleiter, Hermann M.

AU - Haag, Elisabeth

AU - Shen, Jian Ren

AU - Eaton-Rye, Julian J.

AU - Seeliger, Angela G.

AU - Inoue, Yorinao

AU - Vermaas, Willem

AU - Renger, Gernot

PY - 1995

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N2 - Oscillation patterns of the oxygen yield per flash induced by a train of single-turnover flashes were measured as a function of dark incubation and different pre-illumination conditions in several autotrophic mutant strains of Synechocystis sp. PCC 6803 carrying short deletions within the large, lumen-exposed hydrophilic region (loop E) of the chlorophyll a-binding photosystem II protein CP47. A physiological and biochemical characterization of these mutant strains has been presented previously [Eaton-Rye, J. J., & Vermaas, W. F. J. (1991) Plant Mol. Biol. 17, 1165-1177; Haag, E., Eaton-Rye, J. J., Renger, G., & Vermaas, W. F. J. (1993) Biochemistry 32, 4444-4454], and some functional properties were described recently [Gleiter, H. M., Haag, E., Shen, J.-R., Eaton-Rye, J. J., Inoue, Y., Vermaas, W. F. J., & Renger, G. (1994) Biochemistry 33, 12063-12071]. The present study shows that in several mutants the water-oxidizing complex (WOC) became inactivated during prolonged dark incubation, whereas the WOC of the wild-type strain remained active. The rate and extent of the inactivation in the mutants depend on the domain of loop E, where 3-8 amino acid residues were deleted. The most pronounced effects are observed in mutants Δ(A373-D380) and Δ(R384-V392). A competent WOC can be restored from the fully inactivated state by illumination with short saturating flashes. The number of flashes required for this process strongly depends on the site at which a deletion has been introduced into loop E. Again, the most prominent effects were found in mutants Δ(A373-D380) and Δ(R384-V392). Interestingly, the number of flashes required for activation was reduced by more than an order of magnitude in both mutants by the addition of 10 mM CaCl2 to the cell suspension. On the basis of a model for photoactivation proposed by Tamura and Cheniae (1987) [Biochim. Biophys. Acta 890, 179-194], a scheme is presented for the processes of dark inactivation and photoactivation in these mutants. The results presented here corroborate an important role of the large hydrophilic domain (loop E) of CP47 in a functional and stable WOC.

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