Proton gradient-driven import of the 16 kDa oxygen-evolving complex protein as the full precursor protein by isolated thylakoids.
The biogenesis of the lumenal 16 kDa protein of the photosynthetic oxygen-evolving complex was analysed using an assay for the import of proteins by isolated thylakoids. The precursor protein is imported with high efficiency in the light in both the presence and absence of stromal extract. Import is almost completely blocked in the dark or if the uncoupler nigericin is present in the light. The data indicate that transport across the thylakoid membrane is driven by a proton motive force in which the proton gradient is the dominant component, and that the full precursor protein can be transported across the thylakoid membrane without prior cleavage by the stromal processing peptidase.
Klösgen
R B
RB
Botanisches Institut der Ludwig-Maximilians-Universität, München, FRG.
Brock
I W
IW
Herrmann
R G
RG
Robinson
C
C
D001693:Biological Transport, Active; D002736:Chloroplasts / Q000187:drug effects / Q000378:metabolism*; D008027:Light; D008666:Metalloendopeptidases / Q000378:metabolism; D009550:Nigericin / Q000494:pharmacology; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism*; D010940:Plant Proteins; D010944:Plants / Q000378:metabolism; D011498:Protein Precursors / Q000378:metabolism*
D045322:Photosynthetic Reaction Center Complex Proteins; D010940:Plant Proteins; D011498:Protein Precursors; D008666:Metalloendopeptidases; C071986:stromal processing peptidase; D009550:Nigericin