Site-Directed Mutations of Two Histidine Residues in the D2 Protein Inactivate and Destabilize Photosystem II in the Cyanobacterium Synechocystis 6803

Willem Vermaas, John G K Williams, Charles J. Arntzen

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Abstract

Site-directed mutations were created in the cyanobacterium Synechocystis 6803 to alter specific histidine residues of the photosystem II (PS II) D 2 protein. In one mutant (tyr-197). the his-197 residue was replaced by tyrosine, in another mutant (asn-214), his-214 was changed into asparagine. The tyr-197 mutant did notshow any low-temperature fluorescence attributable to PS II. but contained a PS II chlorophyll-protein, CP-47, in significant quantities. Another PS II chlorophyll-protein, CP-43, was absent, as was PS II-related herbicide binding. The asn-214 mutant showed a blue-shifted low-temperature fluorescence maximum around 682 nm. but did not have a significant amount of membrane-incorporated CP-43 or CP-47. Herbicide binding was also absent in this mutant. These data indicate a very important role of the his-197 and his-214 residues in the D 2 protein, and are interpreted to support the hypothesis that the D 2 protein and the M subunit from the photosynthetic reaction center of purple bacteria have analogous functions. According to this hypothesis, his-197 is involved in binding of P680. and his-214 forms ligands with QA and Fe:+. In absence of a functional D 2 protein, the PS II core com plex appears to be destabilized as evidenced by loss of chlorophyll-proteins in the mutants.

Original languageEnglish (US)
Pages (from-to)762-768
Number of pages7
JournalZeitschrift fur Naturforschung - Section C Journal of Biosciences
Volume42
Issue number7-8
DOIs
StatePublished - Aug 1 1987

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Synechocystis
Photosystem II Protein Complex
Cyanobacteria
Histidine
Mutation
Chlorophyll
Proteins
Herbicides
Fluorescence
Photosynthetic Reaction Center Complex Proteins
Proteobacteria
Temperature
Asparagine
Protein Subunits
Mutant Proteins
Tyrosine
Ligands
Membranes

Keywords

  • Cyanobacteria
  • Herbicide Binding
  • Photosynthesis
  • Photosystem II Proteins
  • Site-Directed Mutagenesis

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

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title = "Site-Directed Mutations of Two Histidine Residues in the D2 Protein Inactivate and Destabilize Photosystem II in the Cyanobacterium Synechocystis 6803",
abstract = "Site-directed mutations were created in the cyanobacterium Synechocystis 6803 to alter specific histidine residues of the photosystem II (PS II) D 2 protein. In one mutant (tyr-197). the his-197 residue was replaced by tyrosine, in another mutant (asn-214), his-214 was changed into asparagine. The tyr-197 mutant did notshow any low-temperature fluorescence attributable to PS II. but contained a PS II chlorophyll-protein, CP-47, in significant quantities. Another PS II chlorophyll-protein, CP-43, was absent, as was PS II-related herbicide binding. The asn-214 mutant showed a blue-shifted low-temperature fluorescence maximum around 682 nm. but did not have a significant amount of membrane-incorporated CP-43 or CP-47. Herbicide binding was also absent in this mutant. These data indicate a very important role of the his-197 and his-214 residues in the D 2 protein, and are interpreted to support the hypothesis that the D 2 protein and the M subunit from the photosynthetic reaction center of purple bacteria have analogous functions. According to this hypothesis, his-197 is involved in binding of P680. and his-214 forms ligands with QA and Fe:+. In absence of a functional D 2 protein, the PS II core com plex appears to be destabilized as evidenced by loss of chlorophyll-proteins in the mutants.",
keywords = "Cyanobacteria, Herbicide Binding, Photosynthesis, Photosystem II Proteins, Site-Directed Mutagenesis",
author = "Willem Vermaas and Williams, {John G K} and Arntzen, {Charles J.}",
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T1 - Site-Directed Mutations of Two Histidine Residues in the D2 Protein Inactivate and Destabilize Photosystem II in the Cyanobacterium Synechocystis 6803

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AU - Williams, John G K

AU - Arntzen, Charles J.

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N2 - Site-directed mutations were created in the cyanobacterium Synechocystis 6803 to alter specific histidine residues of the photosystem II (PS II) D 2 protein. In one mutant (tyr-197). the his-197 residue was replaced by tyrosine, in another mutant (asn-214), his-214 was changed into asparagine. The tyr-197 mutant did notshow any low-temperature fluorescence attributable to PS II. but contained a PS II chlorophyll-protein, CP-47, in significant quantities. Another PS II chlorophyll-protein, CP-43, was absent, as was PS II-related herbicide binding. The asn-214 mutant showed a blue-shifted low-temperature fluorescence maximum around 682 nm. but did not have a significant amount of membrane-incorporated CP-43 or CP-47. Herbicide binding was also absent in this mutant. These data indicate a very important role of the his-197 and his-214 residues in the D 2 protein, and are interpreted to support the hypothesis that the D 2 protein and the M subunit from the photosynthetic reaction center of purple bacteria have analogous functions. According to this hypothesis, his-197 is involved in binding of P680. and his-214 forms ligands with QA and Fe:+. In absence of a functional D 2 protein, the PS II core com plex appears to be destabilized as evidenced by loss of chlorophyll-proteins in the mutants.

AB - Site-directed mutations were created in the cyanobacterium Synechocystis 6803 to alter specific histidine residues of the photosystem II (PS II) D 2 protein. In one mutant (tyr-197). the his-197 residue was replaced by tyrosine, in another mutant (asn-214), his-214 was changed into asparagine. The tyr-197 mutant did notshow any low-temperature fluorescence attributable to PS II. but contained a PS II chlorophyll-protein, CP-47, in significant quantities. Another PS II chlorophyll-protein, CP-43, was absent, as was PS II-related herbicide binding. The asn-214 mutant showed a blue-shifted low-temperature fluorescence maximum around 682 nm. but did not have a significant amount of membrane-incorporated CP-43 or CP-47. Herbicide binding was also absent in this mutant. These data indicate a very important role of the his-197 and his-214 residues in the D 2 protein, and are interpreted to support the hypothesis that the D 2 protein and the M subunit from the photosynthetic reaction center of purple bacteria have analogous functions. According to this hypothesis, his-197 is involved in binding of P680. and his-214 forms ligands with QA and Fe:+. In absence of a functional D 2 protein, the PS II core com plex appears to be destabilized as evidenced by loss of chlorophyll-proteins in the mutants.

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