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Journal ArticleDOI

Sequencing and modification of psbB, the gene encoding the CP-47 protein of Photosystem II, in the cyanobacterium Synechocystis 6803.

Wim F. J. Vermaas, +2 more
- 01 Jul 1987 - 
- Vol. 8, Iss: 4, pp 317-326
TLDR
The psbB gene, encoding this protein, was cloned from the genome of the cyanobacterium Synechocystis 6803, and sequenced, indicating that an intact CP-47 is required for a functional Photosystem II complex, but does not necessarily indicate that this protein would house the reaction center.
Abstract
The Photosystem II protein CP-47 has been hypothesized to be involved in binding the reaction center chlorophyll. The psbB gene, encoding this protein, was cloned from the genome of the cyanobacterium Synechocystis 6803, and sequenced. The DNA sequence is 68% homologous with that of the psbB gene from spinach, whereas the predicted amino acid sequence is 76% homologous. The hydropathy patterns of Synechocystis and spinach CP-47 are almost indistinguishable, indicating the same general CP-47 folding pattern in the thylakoid membrane in the two species. There are five pairs of histidine residues in CP-47 that are spaced by 13 or 14 amino acids and that are located in hydrophobic regions of the protein; these histidine residues may be involved in chlorophyll binding. Interruption of the psbB gene by a DNA fragment carrying a gene conferring kanamycin resistance results in a loss of Photosystem II activity. This indicates that an intact CP-47 is required for a functional Photosystem II complex, but does not necessarily indicate that this protein would house the reaction center.

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Citations
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Journal ArticleDOI

Rapid Diversification of Marine Picophytoplankton with Dissimilar Light-Harvesting Structures Inferred from Sequences of Prochlorococcus and Synechococcus (Cyanobacteria)

TL;DR: Standard phylogenetic methods and newer algorithms insensitive to such biases did not recover different branching patterns within the marine picophytoplankton group, and failed to cluster Prochlorococcus with chloroplasts or other chlorophyll b-containing prokaryotes.
Journal ArticleDOI

Purification and characterization of photosystem I and photosystem II core complexes from wild-type and phycocyanin-deficient strains of the cyanobacterium Synechocystis PCC 6803.

TL;DR: Highly photoactive Photosystem I (PS I) and Photosystem II (PS II) core complexes have been isolated from the cyanobacterium Synechocystis Pasteur Culture Collection (PCC) 6803 and a phycocyanin-deficient mutant, enriched in PS II.
Journal ArticleDOI

The structure and function of CPa-1 and CPa-2 in photosystem II.

TL;DR: Comparisons of the derived amino acid sequences of these proteins suggest sites for chlorophyll binding and for interactions between these chlorophylla-proteins and other Photosystem II components.
Journal ArticleDOI

A High-Resolution Gene Map of the Chloroplast Genome of the Red Alga Porphyra purpurea.

TL;DR: The increased coding capacity of the P. purpurea chloroplast genome demonstrates the primitive nature of the red alga, and evidence for a monophyletic origin of chloroplasts is suggested by the identification of two groups of genes that are clustered inchloroplast genomes but not in cyanobacteria.
References
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Journal ArticleDOI

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Journal ArticleDOI

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Journal ArticleDOI

Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution

TL;DR: The molecular structure of the photosynthetic reaction centre from Rhodopseudomonas viridis has been elucidated using X-ray crystallographic analysis and the first description of the high-resolution structure of an integral membrane protein is presented.
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