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  • cyanobacteria  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Function and organization of Photosystem I polypeptides (1995)
    Springer
    Photosynthesis research 44 (1995), S. 23-40 
    Details
    ISSN: 1573-5079
    Keywords: chloroplasts ; cyanobacteria ; ferredoxin ; photosynthesis ; plastocyanin ; thylakoids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Photosystem I functions as a plastocyanin:ferredoxin oxidoreductase in the thylakoid membranes of chloroplasts and cyanobacteria. The PS I complex contains the photosynthetic pigments, the reaction center P700, and five electron transfer centers (A0, A1, FX, FA, and FB) that are bound to the PsaA, PsaB, and PsaC proteins. In addition, PS I complex contains at least eight other polypeptides that are accessory in their functions. Recent use of cyanobacterial molecular genetics has revealed functions of the accessory subunits of PS I. Site-directed mutagenesis is now being used to explore structure-function relations in PS I. The overall architecture of PSI complex has been revealed by X-ray crystallography, electron microscopy, and biochemical methods. The information obtained by different techniques can be used to propose a model for the organization of PS I. Spectroscopic and molecular genetic techniques have deciphered interaction of PS I proteins with the soluble electron transfer partners. This review focuses on the recent structural, biochemical and molecular genetic studies that decipher topology and functions of PS I proteins, and their interactions with soluble electron carriers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00018294
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  • 2
    Electronic Resource
    Electronic Resource
    Targeted deletion of psaJ from the cyanobacterium Synechocystis sp. PCC 6803 indicates structural interactions between the PsaJ and PsaF subunits of photosystem I (1994)
    Springer
    Plant molecular biology 26 (1994), S. 291-302 
    Details
    ISSN: 1573-5028
    Keywords: cyanobacteria ; RNA levels ; mutagenesis ; photosystem I ; protein interactions ; Synechocystis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Photosystem I catalyzes the light-driven oxidation of plastocyanin or cytochrome c 6 and the reduction of ferredoxin or flavodoxin. PsaJ is a 4.4 kDa hydrophobic subunit of photosystem I from cyanobacteria and chloroplasts. To investigate the function of PsaJ, we generated a mutant strain of the cyanobacterium Synechocystis sp. PCC 6803 in which the psaJ gene is replaced by a gene for chloramphenicol resistance. Deletion of psaJ led to a reduction in the steady state RNA level from psaF which is located upstream from psaJ. Immunoquantification using an anti-PsaF antibody revealed a significant decrease in the amount of PsaF in membranes of the mutant strain. Trimeric photosystem I complexes isolated from the mutant strain using n-dodecyl β-D-maltoside lacked PsaJ, contained ca. 80% less PsaF, but maintained wild-type levels of other photosystem I subunits. In contrast, the photosystem I purified using Triton X-100 contained less than 2% PsaF when compared to the wild type, showing the more extractable nature of PsaF in PsaJ-less photosystem I in the presence of Triton X-100. PsaE was more accessible to removal by NaI in a mutant strain lacking PsaF and PsaJ than in the wild type. The presence of PsaF in photosystem I from the PsaJ-less strain did not alter the increased susceptibility of PsaE to removal by NaI. These results indicate an interaction between PsaJ and PsaF in the organization of the complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00039540
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