Functional characterization of mutant strains of the cyanobacterium synechocystis sp. pcc 6803 lacking short domains within the large, lumen-exposed loop of the chlorophyll protein cp47 in photosystem II

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

Research output: Contribution to journalArticle

57 Citations (Scopus)

Abstract

Several autotrophic mutant strains of Synechocystis sp. PCC 6803 carrying short deletions or a single-site mutation within the large, lumen-exposed loop (loop E) of the chlorophyll a-binding photosytem II core protein, CP47, are analyzed for their functional properties by measuring the flash-induced pattern of thermoluminescence, oxygen yield, and fluorescence quantum yield. A physiological and biochemical characterization of these mutant strains has been given in two previous reports [Eaton-Rye, J. J., & Vermaas, W. F. J. (1991) Plant Mol. Biol. 17, 1165-1177; Haag, E., Eaton-Rye, J. J., Renger, G., & Vermaas, S. F. J. (1993) Biochemistry 32, 4444-4454]. The results of the present study show that deletion of charged and conserved amino acids in a region roughly located between residues 370 and 390 decreases the binding affinity of the extrinsic PS II-O protein to photosystem II. Marked differences with PSII-O deletion mutants are observed with respect to Ca2+ requirement and the flash-induced pattern of oxygen evolution. Under conditions where a sufficient light activation is provided, the psbB mutants assayed in this study reveal normal S-state parameters and lifetimes. The results bear two basic implications: (i) the manganese involved in water oxidation can still be bound in a functionally normal or only slightly distorted manner, and (ii) the binding of the extrinsic PS II-O protein to photosystem II is impaired in mutants carrying a deletion in the domain between residues 370 and 390, but the presence of the PS II-O protein is still of functional relevance for the PS II complex, e.g., for maintenance of a high-affinity binding site for Ca2+ and/or involvement during the process of photoactivation.

Original languageEnglish (US)
Pages (from-to)12063-12071
Number of pages9
JournalBiochemistry
Volume33
Issue number40
StatePublished - 1994

Fingerprint

Synechocystis
Photosystem II Protein Complex
Cyanobacteria
Chlorophyll
Proteins
Oxygen
Biochemistry
Thermoluminescence
Quantum yield
Manganese
Fluorescence
Chemical activation
Binding Sites
Light
Amino Acids
Oxidation
Mutation
Water
Secale

ASJC Scopus subject areas

  • Biochemistry

Cite this

Functional characterization of mutant strains of the cyanobacterium synechocystis sp. pcc 6803 lacking short domains within the large, lumen-exposed loop of the chlorophyll protein cp47 in photosystem II. / Gleiter, Hermann M.; Haag, Elisabeth; Shen, Jian Ren; Eaton-Rye, Julian J.; Inoue, Yorinao; Vermaas, Willem; Renger, Gernot.

In: Biochemistry, Vol. 33, No. 40, 1994, p. 12063-12071.

Research output: Contribution to journalArticle

Gleiter, Hermann M. ; Haag, Elisabeth ; Shen, Jian Ren ; Eaton-Rye, Julian J. ; Inoue, Yorinao ; Vermaas, Willem ; Renger, Gernot. / Functional characterization of mutant strains of the cyanobacterium synechocystis sp. pcc 6803 lacking short domains within the large, lumen-exposed loop of the chlorophyll protein cp47 in photosystem II. In: Biochemistry. 1994 ; Vol. 33, No. 40. pp. 12063-12071.
@article{5520845af62f46928df0c326cc021018,
title = "Functional characterization of mutant strains of the cyanobacterium synechocystis sp. pcc 6803 lacking short domains within the large, lumen-exposed loop of the chlorophyll protein cp47 in photosystem II",
abstract = "Several autotrophic mutant strains of Synechocystis sp. PCC 6803 carrying short deletions or a single-site mutation within the large, lumen-exposed loop (loop E) of the chlorophyll a-binding photosytem II core protein, CP47, are analyzed for their functional properties by measuring the flash-induced pattern of thermoluminescence, oxygen yield, and fluorescence quantum yield. A physiological and biochemical characterization of these mutant strains has been given in two previous reports [Eaton-Rye, J. J., & Vermaas, W. F. J. (1991) Plant Mol. Biol. 17, 1165-1177; Haag, E., Eaton-Rye, J. J., Renger, G., & Vermaas, S. F. J. (1993) Biochemistry 32, 4444-4454]. The results of the present study show that deletion of charged and conserved amino acids in a region roughly located between residues 370 and 390 decreases the binding affinity of the extrinsic PS II-O protein to photosystem II. Marked differences with PSII-O deletion mutants are observed with respect to Ca2+ requirement and the flash-induced pattern of oxygen evolution. Under conditions where a sufficient light activation is provided, the psbB mutants assayed in this study reveal normal S-state parameters and lifetimes. The results bear two basic implications: (i) the manganese involved in water oxidation can still be bound in a functionally normal or only slightly distorted manner, and (ii) the binding of the extrinsic PS II-O protein to photosystem II is impaired in mutants carrying a deletion in the domain between residues 370 and 390, but the presence of the PS II-O protein is still of functional relevance for the PS II complex, e.g., for maintenance of a high-affinity binding site for Ca2+ and/or involvement during the process of photoactivation.",
author = "Gleiter, {Hermann M.} and Elisabeth Haag and Shen, {Jian Ren} and Eaton-Rye, {Julian J.} and Yorinao Inoue and Willem Vermaas and Gernot Renger",
year = "1994",
language = "English (US)",
volume = "33",
pages = "12063--12071",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "40",

}

TY - JOUR

T1 - Functional characterization of mutant strains of the cyanobacterium synechocystis sp. pcc 6803 lacking short domains within the large, lumen-exposed loop of the chlorophyll protein cp47 in photosystem II

AU - Gleiter, Hermann M.

AU - Haag, Elisabeth

AU - Shen, Jian Ren

AU - Eaton-Rye, Julian J.

AU - Inoue, Yorinao

AU - Vermaas, Willem

AU - Renger, Gernot

PY - 1994

Y1 - 1994

N2 - Several autotrophic mutant strains of Synechocystis sp. PCC 6803 carrying short deletions or a single-site mutation within the large, lumen-exposed loop (loop E) of the chlorophyll a-binding photosytem II core protein, CP47, are analyzed for their functional properties by measuring the flash-induced pattern of thermoluminescence, oxygen yield, and fluorescence quantum yield. A physiological and biochemical characterization of these mutant strains has been given in two previous reports [Eaton-Rye, J. J., & Vermaas, W. F. J. (1991) Plant Mol. Biol. 17, 1165-1177; Haag, E., Eaton-Rye, J. J., Renger, G., & Vermaas, S. F. J. (1993) Biochemistry 32, 4444-4454]. The results of the present study show that deletion of charged and conserved amino acids in a region roughly located between residues 370 and 390 decreases the binding affinity of the extrinsic PS II-O protein to photosystem II. Marked differences with PSII-O deletion mutants are observed with respect to Ca2+ requirement and the flash-induced pattern of oxygen evolution. Under conditions where a sufficient light activation is provided, the psbB mutants assayed in this study reveal normal S-state parameters and lifetimes. The results bear two basic implications: (i) the manganese involved in water oxidation can still be bound in a functionally normal or only slightly distorted manner, and (ii) the binding of the extrinsic PS II-O protein to photosystem II is impaired in mutants carrying a deletion in the domain between residues 370 and 390, but the presence of the PS II-O protein is still of functional relevance for the PS II complex, e.g., for maintenance of a high-affinity binding site for Ca2+ and/or involvement during the process of photoactivation.

AB - Several autotrophic mutant strains of Synechocystis sp. PCC 6803 carrying short deletions or a single-site mutation within the large, lumen-exposed loop (loop E) of the chlorophyll a-binding photosytem II core protein, CP47, are analyzed for their functional properties by measuring the flash-induced pattern of thermoluminescence, oxygen yield, and fluorescence quantum yield. A physiological and biochemical characterization of these mutant strains has been given in two previous reports [Eaton-Rye, J. J., & Vermaas, W. F. J. (1991) Plant Mol. Biol. 17, 1165-1177; Haag, E., Eaton-Rye, J. J., Renger, G., & Vermaas, S. F. J. (1993) Biochemistry 32, 4444-4454]. The results of the present study show that deletion of charged and conserved amino acids in a region roughly located between residues 370 and 390 decreases the binding affinity of the extrinsic PS II-O protein to photosystem II. Marked differences with PSII-O deletion mutants are observed with respect to Ca2+ requirement and the flash-induced pattern of oxygen evolution. Under conditions where a sufficient light activation is provided, the psbB mutants assayed in this study reveal normal S-state parameters and lifetimes. The results bear two basic implications: (i) the manganese involved in water oxidation can still be bound in a functionally normal or only slightly distorted manner, and (ii) the binding of the extrinsic PS II-O protein to photosystem II is impaired in mutants carrying a deletion in the domain between residues 370 and 390, but the presence of the PS II-O protein is still of functional relevance for the PS II complex, e.g., for maintenance of a high-affinity binding site for Ca2+ and/or involvement during the process of photoactivation.

UR - http://www.scopus.com/inward/record.url?scp=0028032823&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028032823&partnerID=8YFLogxK

M3 - Article

VL - 33

SP - 12063

EP - 12071

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 40

ER -