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. 1990 Sep;87(17):6748–6752. doi: 10.1073/pnas.87.17.6748

Metal-ion-center assembly of ferredoxin and plastocyanin in isolated chloroplasts.

H M Li 1, S M Theg 1, C M Bauerle 1, K Keegstra 1
PMCID: PMC54614  PMID: 11607098

Abstract

Most chloroplastic proteins are cytosolically synthesized and posttranslationally transported to their proper locations. Two examples of this group of proteins are ferredoxin and plastocyanin, both of which are metal-containing components of the photosynthetic electron-transport chain. The import process for these two proteins includes the insertion of the metal ions to produce the holo forms of the proteins. We show here that in vitro translated precursor proteins of ferredoxin and plastocyanin are synthesized as apo forms and are assembled into their respective holo forms after being imported into isolated chloroplasts. We also provide evidence that only mature-sized proteins are competent to be assembled into holo forms.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Choi S. Y., Churchich J. E. Biosynthesis of 4-aminobutyrate aminotransferase. Eur J Biochem. 1986 Dec 1;161(2):289–294. doi: 10.1111/j.1432-1033.1986.tb10445.x. [DOI] [PubMed] [Google Scholar]
  2. Chua N. H., Schmidt G. W. Post-translational transport into intact chloroplasts of a precursor to the small subunit of ribulose-1,5-bisphosphate carboxylase. Proc Natl Acad Sci U S A. 1978 Dec;75(12):6110–6114. doi: 10.1073/pnas.75.12.6110. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cline K. Import of proteins into chloroplasts. Membrane integration of a thylakoid precursor protein reconstituted in chloroplast lysates. J Biol Chem. 1986 Nov 5;261(31):14804–14810. [PubMed] [Google Scholar]
  4. Cline K., Werner-Washburne M., Lubben T. H., Keegstra K. Precursors to two nuclear-encoded chloroplast proteins bind to the outer envelope membrane before being imported into chloroplasts. J Biol Chem. 1985 Mar 25;260(6):3691–3696. [PubMed] [Google Scholar]
  5. Della-Cioppa G., Bauer S. C., Klein B. K., Shah D. M., Fraley R. T., Kishore G. M. Translocation of the precursor of 5-enolpyruvylshikimate-3-phosphate synthase into chloroplasts of higher plants in vitro. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6873–6877. doi: 10.1073/pnas.83.18.6873. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fernandez M. D., Lamppa G. K. Acyl carrier protein (ACP) import into chloroplasts does not require the phosphopantetheine: evidence for a chloroplast holo-ACP synthase. Plant Cell. 1990 Mar;2(3):195–206. doi: 10.1105/tpc.2.3.195. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Garrett T. P., Clingeleffer D. J., Guss J. M., Rogers S. J., Freeman H. C. The crystal structure of poplar apoplastocyanin at 1.8-A resolution. The geometry of the copper-binding site is created by the polypeptide. J Biol Chem. 1984 Mar 10;259(5):2822–2825. doi: 10.2210/pdb2pcy/pdb. [DOI] [PubMed] [Google Scholar]
  8. Korb H., Neupert W. Biogenesis of cytochrome c in Neurospora crassa. Synthesis of apocytochrome c, transfer to mitochondria and conversion to Holocytochrome c. Eur J Biochem. 1978 Nov 15;91(2):609–620. doi: 10.1111/j.1432-1033.1978.tb12714.x. [DOI] [PubMed] [Google Scholar]
  9. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  10. Pagani S., Bonomi F., Cerletti P. Enzymic synthesis of the iron-sulfur cluster of spinach ferredoxin. Eur J Biochem. 1984 Jul 16;142(2):361–366. doi: 10.1111/j.1432-1033.1984.tb08295.x. [DOI] [PubMed] [Google Scholar]
  11. Pfaller R., Freitag H., Harmey M. A., Benz R., Neupert W. A water-soluble form of porin from the mitochondrial outer membrane of Neurospora crassa. Properties and relationship to the biosynthetic precursor form. J Biol Chem. 1985 Jul 5;260(13):8188–8193. [PubMed] [Google Scholar]
  12. Randall L. L., Hardy S. J. Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli. Cell. 1986 Sep 12;46(6):921–928. doi: 10.1016/0092-8674(86)90074-7. [DOI] [PubMed] [Google Scholar]
  13. Randall L. L., Hardy S. J. Unity in function in the absence of consensus in sequence: role of leader peptides in export. Science. 1989 Mar 3;243(4895):1156–1159. doi: 10.1126/science.2646712. [DOI] [PubMed] [Google Scholar]
  14. Schmidt G. W., Bartlett S. G., Grossman A. R., Cashmore A. R., Chua N. H. Biosynthetic pathways of two polypeptide subunits of the light-harvesting chlorophyll a/b protein complex. J Cell Biol. 1981 Nov;91(2 Pt 1):468–478. doi: 10.1083/jcb.91.2.468. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Sharma C. P., Gehring H. The precursor of mitochondrial aspartate aminotransferase is translocated into mitochondria as apoprotein. J Biol Chem. 1986 Aug 25;261(24):11146–11149. [PubMed] [Google Scholar]
  16. Smeekens S., Bauerle C., Hageman J., Keegstra K., Weisbeek P. The role of the transit peptide in the routing of precursors toward different chloroplast compartments. Cell. 1986 Aug 1;46(3):365–375. doi: 10.1016/0092-8674(86)90657-4. [DOI] [PubMed] [Google Scholar]
  17. Smeekens S., van Binsbergen J., Weisbeek P. The plant ferredoxin precursor: nucleotide sequence of a full length cDNA clone. Nucleic Acids Res. 1985 May 10;13(9):3179–3194. doi: 10.1093/nar/13.9.3179. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Takahashi Y., Mitsui A., Hase T., Matsubara H. Formation of the iron-sulfur cluster of ferredoxin in isolated chloroplasts. Proc Natl Acad Sci U S A. 1986 Apr;83(8):2434–2437. doi: 10.1073/pnas.83.8.2434. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Vorst O., Oosterhoff-Teertstra R., Vankan P., Smeekens S., Weisbeek P. Plastocyanin of Arabidopsis thaliana; isolation and characterization of the gene and chloroplast import of the precursor protein. Gene. 1988 May 15;65(1):59–69. doi: 10.1016/0378-1119(88)90417-9. [DOI] [PubMed] [Google Scholar]
  20. Zimmermann R., Neupert W. Transport of proteins into mitochondria. Posttranslational transfer of ADP/ATP carrier into mitochondria in vitro. Eur J Biochem. 1980 Aug;109(1):217–229. doi: 10.1111/j.1432-1033.1980.tb04787.x. [DOI] [PubMed] [Google Scholar]

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