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  • chloroplasts  (2)
  • Import in organello  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 13 (1981), S. 295-306 
    ISSN: 1573-6881
    Keywords: Photosystem I ; reaction center ; chloroplasts ; cytochrome 552 ; light induced oxidation ; effect of salts
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract A photosystem I reaction center has been isolated fromChlamydomonas chloroplasts and compared with the photosystem I reaction center from higher plants. While the higher plant reaction center is active in cytochrome 552 photooxidation, theChlamydomonas preparation was not active unless salts were included in the assay medium or the pH was lowered to 5. Subunit III-depleted photosystem I reaction center from higher plants is also inactive in cytochrome 552 photooxidation in the absence of salts. As with theChlamydomonas reaction center, salts induced its activity. Subunit I of the photosystem I reaction center has tentatively been identified as the binding site of cytochrome 552.
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  • 2
    ISSN: 1573-5079
    Keywords: biogenesis ; cyanobacteria ; chloroplasts ; membrane-proteins ; Photosystem I
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The assembly of the multi-subunit membrane-protein Photosystem I (PS I) complex involves incorporation of peripheral proteins into the complex. Here we studied assembly of the PsaD subunit of the cyanobacterial and plant PS I into the thylakoid membranes. We generated partial and chimeric psaD genes from which labeled proteins were synthesized in vitro. Assembly of these proteins into the cyanobacterial or plant thylakoids was assayed. The deletion of leader sequence and N-terminal extension of spinach prePsaD did not inhibit its assembly into spinach or cyanobacterial thylakoids. Addition of these sequences to the cyanobacterial PsaD did not enable it to assemble into plant thylakoids. Moreover, these additions significantly decreased the ability of the chimeric proteins to assemble into cyanobacterial thylakoids. In contrast, when the carboxyl-terminal half of cyanobacterial PsaD was replaced by the corresponding region of the spinach PsaD, the chimeric protein could assemble into both spinach and cyanobacterial thylakoids. Therefore, information in the carboxyl-terminal region of spinach PsaD is crucial for its assembly into plant thylakoids.
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  • 3
    ISSN: 1617-4623
    Keywords: cDNA expression library ; Thylakoid membrane polypeptides ; Import in organello ; transcripts ; Spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Spinach cDNA libraries, made from polyadenylated seedling RNA, have been constructed in pBR322 and the expression vector λgt11. Recombinant plasmids or phage for 14 intrinsic and peripheral thylakoid membrane proteins and one stromal protein have been identified. They encode components containing antigenic determinants against the lysine-rich 34 kd, the 23 kd and 16 kd proteins all associated with the water-splitting apparatus of the photosystem II reaction center, the ATP synthase subunits gamma, delta and CFo-II, the Rieske Fe/S protein of the cytochrome b/f complex, subunits 2, 3, 5 and 6 of the photosystem I reaction center, plastocyanin, ferredoxin oxidoreductase, chlorophyll a/b-binding apoproteins of the lightharvesting complex associated with photosystem II, and the small subunit of the stromal enzyme ribulose bisphosphate corboxylase/oxygenase. The cDNA inserts lack complementarity to plastid DNA but hybridize to restricted nuclear DNA as well as to discrete poly A+-mRNA species. The precursor products obtained after translation of hybrid selected RNA fractions in a wheat germ assay are imported and processed by isolated unbroken spinach chloroplasts. The imported components comigrate with the respective authentic proteins.
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