Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: KEGG:D02259 (NaI)
 1,823 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Photosystem I catalyzes the light-driven oxidation of plastocyanin or cytochrome c6 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 beta-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.
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PMID:Targeted deletion of psaJ from the cyanobacterium Synechocystis sp. PCC 6803 indicates structural interactions between the PsaJ and PsaF subunits of photosystem I. 752 26

Photosystem I functions as a light-driven plastocyanin-ferredoxin oxidoreductase in the photosynthetic membranes of cyanobacteria and chloroplasts. A mutant strain of the cyanobacterium Synechocystis sp. PCC 6803 that contains a deletion of the psaF gene and a transcriptionally inactive psaJ gene has assembled photosystem I complexes that lack PsaF, a lumenal protein and PsaJ, a 4-kDa hydrophobic protein. The cells of the mutant and wild type strains have similar rates of photosynthetic electron transfer and P700+ rereduction under linear and cyclic electron transfer conditions. Analysis of flash-induced absorption transients at 700 nm demonstrate that the absence of PsaF in purified mutant photosystem I did not affect the rate of P700 rereduction by cytochrome c553. Therefore, PsaF is not essential for docking of cytochrome c553. We also studied the organization of the proteins of mutant and wild type photosystem I by comparing their accessibility to digestion by thermolysin or to removal by 1 M NaI. The PsaA-PsaB subunits were more easily degraded by thermolysin in the mutant photosystem I. Thermolysin cleavage of PsaB yielded two major fragments that were immunoreactive with an antibody raised against the C terminus of PsaB. The N termini of these PsaB peptides mapped at Ile482 and Ile498 residues, thus identifying a surface-exposed domain of the core of photosystem I. The PsaE subunit could be removed by 1 M NaI and was rapidly digested by thermolysin in the mutant but not in the wild type photosystem I. Therefore, PsaF and PsaJ subunits of photosystem I have dispensable accessory roles in the function and organization of the complex.
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PMID:Function and organization of photosystem I in a cyanobacterial mutant strain that lacks PsaF and PsaJ subunits. 810 55

The PsaD subunit of photosystem I (PSI) is a peripheral protein that provides a docking site for ferredoxin and interacts with the PsaB, PsaC, and PsaL subunits of PSI. We used site-directed mutagenesis to determine the function of a basic region in PsaD of the cyanobacterium Synechocystis sp. PCC 6803. We generated five mutant strains in which one or more charged residues were altered. Western blotting showed that replacement of lysine (Lys)-74 with glutamine or glutamic acid led to a substantial decrease in the level of PsaD in the membranes. The mutant PSI complexes showed reduced NADP+ photoreduction activity mediated by ferredoxin; the decrease in activity correlated with the reduced level of PsaD. Using protein synthesis inhibitors we showed that the degradation rates of the mutant and wild-type PsaD were similar, indicating a defect in the assembly of the mutant protein. Treatment of the mutant PSI complexes with a different concentration of NaI showed that the mutations decreased affinity between PsaD and the transmembrane components of PSI. With glutaraldehyde, the mutant and wild-type PsaD proteins could be cross-linked with PsaC, but the PsaD-PsaL cross-linked product was reduced drastically when arginine-72, Lys-74, and Lys-76 were mutated simultaneously. These studies demonstrate that the basic residues in the central region of PsaD, especially Lys-74, are crucial in the assembly of PsaD into the PSI complex.
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PMID:The PsaD subunit of photosystem I. Mutations in the basic domain reduce the level of PsaD in the membranes. 941 69