7
Views
6
CrossRef citations to date
0
Altmetric
Original Article

The specificity of glycolipid-preferredoxin interaction: requirements for membrane binding

, , , , &
Pages 255-261 | Received 03 Jan 1995, Published online: 09 Jul 2009

References

  • Cremers A. F. M., Voorhout W. F., Van Der Krift T. P., Leunissen-Bijvelt J. J. M., Verkleij A. J. Visualization of contact sites between outer and inner envelope membranes in isolated chloroplasts. Biochimica et Biophysica Acta 1988; 933: 334–340
  • Von Heijne G., Steppuhn J., Herrmann R. G. Domain structure of mitochondrial and chloroplast targeting peptides. European Journal of Biochemistry 1989; 180: 535–545
  • Reiss B., Wasman C. C., Bohnert H. J. Regions in the transit peptide of SSU essential for transport into chloroplasts. Molecular and General Genetics 1987; 209: 116–121
  • Smeekens S., Geerts D., Bauerle C., Weisbeek P. J. Essential function in chloroplast recognition of the ferredoxin transit peptide processing region. Molecular and General Genetics 1989; 216: 178–182
  • Pilon M., De Kruijff B., Weisbeek P. J. New insights into the import mechanism of the ferredoxin precursor into chloroplast. Journal of Biological Chemistry 1992; 267: 2548–2556
  • Van Den Broek G., Tinko M. L., Kausch A. P., Cashmore A. R., Van Montagne M., Herrera-Estrella J. Targeting of a foreign protein to chloroplasts by fusion of the transit peptide from the small subunit of ribulose-1,5-bisphosphate carboxylase. Nature 1985; 313: 358–363
  • Pilon M., Wienk H., Sips W., De Swaaf M., Talboom I., Van'T Hof R., De Korte-Kool G., Demel R. A., Weisbeek P. J., De Kruijff B. Functional dolmains of the ferredoxin transit sequence involved in chloroplast import. Journal of Biological Chemistry 1995; 270: 3882–3893
  • Olsen L. J., Theg S. M., Selman B. R., Keegstra K. ATP is required for the binding of precursor proteins to chloroplasts. Journal of Biological Chemistry 1989; 264: 6724–6729
  • Theg S. M., Bauerle C., Olsen L. J., Selman B. R., Keegstra K. Internal ATP is the only energy requirement for the translocation of the precursor proteins across chloroplast membranes. Journal of Biological Chemistry 1989; 264: 6730–6736
  • Pain D., Blobel G. Protein import into chloroplasts requires a chloroplast ATPase. Proceedings of the National Academy of Sciences, USA 1987; 84: 3288–3292
  • Robinson C., Ellis R. J. Transport of proteins into chloroplasts. European Journal of Biochemistry 1984; 142: 337–342
  • De Boer A. D., Weisbeek P. J. Chloroplast protein topogenesis: import, sorting and assembly. Biochimica et Biophysica Acta 1991; 1071: 221–253
  • 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. Journal of Biological Chemistry 1985; 260: 3691–3696
  • Perry S. E., Keegstra K. Membrane proteins that interact with chloroplast precursor proteins. The Plant Cell 1994; 6: 93–105
  • Douce R., Block M. A., Dome A. J., Joyard J. The plastid envelope membranes. Subcellular Biochemistry 1984; 10: 1–84
  • Flügge U. I. On the translocation of proteins across the chloroplast envelope. Journal of Bioenergetics and Biomembranes 1990; 22: 769–787
  • Kerber B., Soll J. Transfer of a chloroplast-bound precursor protein into the translocation apparatus is impaired after phospholipase C treatment. FEBS Letters 1992; 306: 71–74
  • Van'T Hof R., De Kruijff B. Transit sequence-dependent binding of the chloroplast precursor protein ferredoxin to lipid vesicles and its implications for membrane stability. FEB Letters 1995; 361: 35–40
  • Van'T Hof R., Van Klompenburg W., Pilon M., Kozubek A., De Korte-Kool G., Demel R. A., Weisbeek P. J., De Kruijff B. The transit sequence mediates the specific interaction of the precursor of ferredoxin with chloroplast envelope membrane lipids. Journal of Biological Chemistry 1992; 268: 4037–4042
  • Keegstra K. Transport and routing of proteins into chloroplasts. Cell 1989; 56: 247–253
  • Horniak L., Pilon M., Van'T Hof R., De Kruijff B. The secondary structure of the ferredoxin transit sequence is modulated by its interaction with negatively charged lipids. FEBS Letters 1993; 334: 241–246
  • De Kruijff B. Polymorphic regulation of membrane lipid composition. Nature 1987; 329: 587–588
  • Killian J. A., Jong De, Ph A. M., Bijvelt J., Verkleij A. J., De Kruijff B. Induction of non-bilayer lipid structures by functional signal peptides. EMBO Journal 1990; 9: 815–819
  • Arnon D. I. The discovery of ferredoxin: the photosynthetic path. Trends in Biochemical Sciences 1988; 13: 30–33
  • Knaff D. B., Hirasawa M. Ferredoxin-dependent chloroplast enzymes. Biochimica et Biophysica Acta 1991; 1056: 93–125
  • Hasleff B. G., Cammack R., Whatley F. R. Quantitative studies on ferredoxin in greening bean leaves. Biochemical Journal 1973; 136: 697–703
  • Huisman J. G., Moorman A. F. M., Verkleij F. N. In vitro synthesis of chloroplast ferredoxin as a high molecular weight precursor in a cell-free protein synthesizing system from wheat germs. Biochemical and Biophysical Research Communications 1978; 82: 1121–1131
  • Pilon M., Rietveld A. G., Weisbeek P. J., De Kruijff B. Secondary structure and folding of a functional chloroplast precursor protein. Journal of Biological Chemistry 1992; 267: 19907–19913
  • Demel R. A., Jackson R. L. Lipoprotein lipase hydrolysis of trioleoylglycerol in a phospholipid interface. Journal of Biological Chemistry 1985; 260: 9589–9592
  • Asgharian B., Cadenhead D. A., Mannock D. A., Lewis R. N. A. H., McElhaney R. N. A comparative molecular film study of 1,2-di-O-palmitoyl-3-O-(α- and β-M-glucopyranosyl)-sn-glycerols. Biochemistry 1989; 28: 7102–7106
  • Hinz H. J., Six L., Ruess K. P., Liefländer M. Head group distributions to bilayer stability: monolayer and calorimetric studies on synthetic, stereochemically uniform glucolipids. Biochemistry 1985; 24: 806–813
  • Chupin V., Van'T Hof R., De Kruijff B. The transit sequence of a chloroplast precursor protein reorients the lipids in monogalactosyl diglyceride-containing lipids. FEBS Letters 1994; 350: 104–108
  • Pilon M., De Boer A.-D, Knols S. L., Koppelman M. H. G. M., Van Der Graaf R. M., De Kruijff B., Weisbeek P. J. Expression in Escherichia coli and purification of a translocation-competent precursor of the chloroplast protein ferredoxin. Journal of Biological Chemistry 1990; 265: 3358–3361
  • Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 1976; 72: 248–254
  • Van'T Hof R., De Kruijff B. ATP-Dependent import of a transit peptide into chloroplasts. Journal of Biological Chemistry 1994, (submitted)
  • Mannock D. A., Lewis R. N. A. H., McElhaney R. N. An improved procedure for the preparation of 1, 2-di-O-acyl-3-O-(β-D-glucopyranosyl)-sn-glycerol. Chemistry and Physics of Lipids 1987; 43: 113–127
  • Mannock D. A., Lewis R. N. A. H., McElhaney R. N. The chemical synthesis and physical characterization of 1,2-di-O-acyl-3-O(α-D-glucopyranosyl)-sn-glycerol, an important class of membrane glycolipids. Chemistry and Physics of Lipids 1990; 55: 309–321
  • Glew R. U., Gopolan V., Hubbell C. A., Devraj R. V., Lawson R. A., Diven W. F., Mannock D. A. 2,3-Di-O-tetradecyl-1-O-(β-D-glucopyranosyl)-sn-glycerol is a substrate for human glucocererbrosidase. Biochemical Journal 1991; 274: 557–563
  • Trouard T. P., Mannock D. A., Lindblom G., Rilfors L., Akiyama M., McElhaney R. N. Thermolytic phase properties of 1,2-di-O-tetradecyl-3-O-(3-O-methyl-β-D-glucopyranosyl)-sn-glycerol. Biophysical Journal 1994; 26: 1090–1100
  • Demel R. A., Jordi W., Lambrechts H., Van Damme H., Hovius R., De Kruijff B. Differential interactions of apo- and holocytochrome c with acidic membrane lipids in model systems and the implications for their import into mitochondria. Journal of Biological Chemistry 1989; 264: 3988–3997

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.