Current Genetics

, Volume 8, Issue 2, pp 147–154 | Cite as

Isolation, characterization, phosphorylation and site of synthesis of Spinacia chloroplast ribosomal proteins

  • Mark Posno
  • Marjolein van Noort
  • Roger Débise
  • Gert S. P. Groot


We have characterized the ribosomal proteins from Spinacia chloroplasts using two-dimensional gel electrophoresis. The 30S and 50S subunits contain 23–25 and 36 ribosomal proteins, respectively. In contrast to prokaryotic ribosomes, chloroplast ribosomes contain at least one (and possibly two) phosphorylated ribosomal proteins. Isolated chloroplasts synthesize in the presence of (35S) labeled methionine and cysteine at least seven 30S and thirteen 50S ribosomal proteins which are assembled into (pre)ribosomes. This suggests that about one third of the chloroplast ribosomal proteins is encoded by the chloroplast DNA itself. The identity of several labeled proteins in the two-dimensional gel electrophoretic patterns which did not comigrate with stained chloroplast ribosomal proteins is discussed.

Key words

Chloroplast Ribosomal proteins Spinacia oleracea Phosphorylation Protein synthesis 



Coomassie Brilliant Blue








ethylene diamine tetraacetate


ethylene glycol-bis (β-amino ethyl ether) N,N′-tetraacetic acid




light harvesting chlorophyll a/b protein


phenyl methyl sulfonyl fluoride


ribulose-1,5-bisphosphate carboxylase




Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Alfonzo R, Nelson N, Racker E (1980) Plant Physiol 65:730–734CrossRefGoogle Scholar
  2. Barritault D, Expert-Bezancon A, Guérin MF, Hayes D (1976) Eur J Biochem 63:131–135CrossRefGoogle Scholar
  3. Bartsch M, Kimura M, Subramanian AR (1982) Proc Natl Acad Sci USA 79:6871–6875CrossRefGoogle Scholar
  4. Bedbrook JR, Kolodner R, Bogorad L (1977) Cell 11:739–749CrossRefGoogle Scholar
  5. Bennett J (1979) Eur J Biochem 99:131–137CrossRefGoogle Scholar
  6. Bennett J (1983) Biochem J 212:1–13CrossRefGoogle Scholar
  7. Bohnert HJ, Gordon KHJ (1980) Mol Gen Genet 179:539–545CrossRefGoogle Scholar
  8. Boyton JE, Gilham NW, Lambowitz AM (1980) In: Chambliss G, Craven GR, Davies J, Davies K, Kahan L, Nomura M (eds) Ribosomes. Structure, Function and Genetics. University Park Press, Baltimore, pp 903–950Google Scholar
  9. Calagan JL, Pirtle RM, Pirtle IL, Kashdon MA, Ureman HJ, Dudock BS (1980) J Biol Chem 255:9981–9984PubMedGoogle Scholar
  10. Capel MS, Bourque DP (1982) J Biol Chem 257:7746–7757PubMedGoogle Scholar
  11. Davidson JN, Hansen MR, Bogorad L (1974) Mol Gen Genet 132:119–129PubMedGoogle Scholar
  12. Edwards K, Kössel H (1981) Nucleic Acids Res 9:2853–2869CrossRefGoogle Scholar
  13. Ellis RJ, Hartley MR (1982) In: Edelman M, Hallick RB, Chua NH (eds) Methods in Chloroplast Molecular Biology. Elsevier/North Holland, Amsterdam, pp 169–188Google Scholar
  14. Eneas-Filho J, Hartley MR, Macho R (1981) Mol Gen Genet 184:484–488CrossRefGoogle Scholar
  15. Freyssinet G (1978) Exp Cell Res 115:207–219CrossRefGoogle Scholar
  16. Gordon J (1971) Biochem Biophys Res Comm 44:579–586CrossRefGoogle Scholar
  17. Graves MC, Spremulli LL (1983) Arch Biochem Biophys 222:192–199CrossRefGoogle Scholar
  18. Grivell LA, Walg HL (1972) Biochem Biophys Res Comm 49:1452–1458CrossRefGoogle Scholar
  19. Groot GSP, Mason TL, van Hartey-Loosbroek N (1979) Mol Gen Genet 174:339–342CrossRefGoogle Scholar
  20. Hardy SJS, Kurland GG, Voynow P, Mora G (1969) Biochem 8:2897–2905CrossRefGoogle Scholar
  21. Hartley MR, Head C (1979) Eur J Biochem 96:301–309CrossRefGoogle Scholar
  22. Keus RJA, Roovers DJ, van Heerikhuizen H, Groot GSP (1983) Curr Genet 7:7–12CrossRefGoogle Scholar
  23. Laemmli UK (1970) Nature 227:680–685CrossRefGoogle Scholar
  24. Lambowitz AM, Chua NH, Luck DJ (1976) Mol Biol 107:223–253CrossRefGoogle Scholar
  25. Laskey RA, Mills AD (1975) Eur J Biochem 56:335–341CrossRefGoogle Scholar
  26. Lin ZF, Lucero HA, Racker E (1982) J Biol Chem 257:12153–12156PubMedGoogle Scholar
  27. Lucero HA, Lin ZF, Racker E (1982) J Biol Chem 257:12157–12160PubMedGoogle Scholar
  28. Mache R, Dorne AM, Batlle RM (1980) Mol Gen Genet 177:333–338CrossRefGoogle Scholar
  29. Mets L, Bogorad L (1974) Anal Biochem 57:200–210CrossRefGoogle Scholar
  30. Orozco EM Jr, Hallick RB (1982) J Biol Chem 257:3265–3275PubMedGoogle Scholar
  31. Owens GC, Ohad I (1982) J Cell Biol 93:712–718CrossRefGoogle Scholar
  32. Schmidt GW, Mishkind ML (1983) Proc Natl Acad Sci USA 80:2632–2636CrossRefGoogle Scholar
  33. Soll J, Buchanan BB (1983) J Biol Chem 258:6686–6689PubMedGoogle Scholar
  34. Subramanian AR, Steinmetz A, Bogorad L (1983) Nucleic Acids Res 11:5277–5287CrossRefGoogle Scholar
  35. Sugita M, Sugiura M (1983) Nucleic Acids Res 11:1913–1918CrossRefGoogle Scholar
  36. Sugiura M, Kusuda J (1979) Mol Gen Genet 172:137–141CrossRefGoogle Scholar
  37. Süss KH (1981) Biochem Biophys Res Comm 102:724–729CrossRefGoogle Scholar
  38. Takaiwa F, Kusuda M, Sugiura M (1982) Nucleic Acids Res 10:2237–2260Google Scholar
  39. Tiboni O, Ciferri O (1982) FEBS Lett 146:197–200CrossRefGoogle Scholar
  40. Tiboni O, DiPasquale G, Ciferri O (1976) Plant Sci Lett 6:419–429CrossRefGoogle Scholar
  41. Vaessen RTMJ, Kreike J, Groot GSP (1980) FEBS Lett 124:193–196CrossRefGoogle Scholar
  42. Watson JC, Surzycki SJ (1983) Curr Genet 7:201–210CrossRefGoogle Scholar
  43. Whitfeld PR, Herrmann RG, Bottomley W (1978) Nucleic Acids Res 5:1741–1751CrossRefGoogle Scholar
  44. Yamamoto T, Burke J, Autz G, Jagendorf AT (1981) Plant Physiol 67:940–949CrossRefGoogle Scholar
  45. Zinker S, Warner JR (1976) J Biol Chem 251:1799–1807PubMedGoogle Scholar

Copyright information

© Springer-Verlag 1984

Authors and Affiliations

  • Mark Posno
    • 1
  • Marjolein van Noort
    • 1
  • Roger Débise
    • 1
  • Gert S. P. Groot
    • 1
  1. 1.Biochemical LaboratoryFree UniversityAmsterdamThe Netherlands

Personalised recommendations