The importance of protein–protein interactions for optimising oxygen activity in photosystem II: reconstitution with a recombinant thioredoxin—manganese stabilising protein
| Autor: | Warwick Hillier, Adele Kim Williamson, Thomas Wydrzynski, John R. Liggins |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Photosystem II
Molecular Sequence Data macromolecular substances Plant Science Biology Cyanobacteria medicine.disease_cause Biochemistry law.invention Protein–protein interaction Thioredoxins Bacterial Proteins law parasitic diseases Escherichia coli medicine Amino Acid Sequence Peptide sequence Temperature Photosystem II Protein Complex food and beverages Cell Biology General Medicine biology.organism_classification Fusion protein Recombinant Proteins Oxygen Recombinant DNA Spinach Thioredoxin Protein Binding |
| Zdroj: | Photosynthesis Research. 92:305-314 |
| ISSN: | 1573-5079 0166-8595 |
| DOI: | 10.1007/s11120-007-9165-1 |
| Popis: | In this paper we describe how photosystem II (PSII) from higher plants, which have been depleted, of the extrinsic proteins can be reconstituted with a chimeric fusion protein comprising thioredoxin from Escherichia coli and the manganese stabilising protein from Thermosynechococcus elongatus. Surprisingly, even though E. coli thioredoxin is completely unrelated to PSII, the fusion protein restores higher rates of activity upon rebinding to PSII than either the native spinach MSP, or T. elongatus MSP. PSII reconstituted with the fusion protein also has a lower requirement for calcium than PSII with the small extrinsic proteins removed, or PSII reconstituted with spinach or T. elongatus MSP. The MSP portion of the fusion protein is less thermally stable compared to isolated MSP from T. elongatus, which could be the key to its superior activation capability through greater flexibility. This work reveals the importance of protein-protein interactions in the water splitting activity of PSII and suggests that conformational configurations, which increase flexibility in MSP, are essential to its function, even when these are induced by an unrelated protein. |
| Databáze: | OpenAIRE |
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