Phosphorylation of thylakoid proteins during chloroplast biogenesis in greening etiolated and light-grown wheat leaves

Patrick S. Covello, Andrew N. Webber, Stephen J. Danko, John P. Markwell, Neil R. Baker

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


Phosphorylation of polypeptides in isolated thylakoids was examined during chloroplast biogenesis in greening etiolated wheat leaves and 4 day-old wheat leaves grown under a diurnal light regime. At early stages of plastid development standard thylakoid preparations were heavily contaminated with nuclear proteins, which distorted the polypeptide phosphorylation profiles. Removal of contamination from membranes by sucrose density centrifugation demonstrated that the major membrane phosphoprotein in etioplasts was at 35 kDa. During etioplast greening a number of phosphoproteins appeared, of which the 25-27 kDa apoproteins of the light-harvesting chlorophyll a/b protein complex associated with photosystem II (LHCII) became the most dominant. At the early stages of thylakoid development found at the base of the 4-day-old light grown leaf the LHCII apoproteins were evident as phosphoproteins; however the major phosphoprotein was polypeptide at ca. 9kDA. Phosphorylation of both the LHCII apoproteins and the 9 kDa polypeptide in these thylakoids was not light-dependent. In the older thylakoids isolated from the leaf tip the LHCII apoproteins were the major phosphoproteins and their phosphorylation had become light-regulated; however phosphorylation of the 9 kDa polypeptide remained insensitive to light.

Original languageEnglish (US)
Pages (from-to)243-254
Number of pages12
JournalPhotosynthesis research
Issue number3
StatePublished - Jan 1 1987
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Plant Science
  • Cell Biology


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