Cyanobacterial thylakoid membrane proteins are reversibly phosphorylated under plastoquinone-reducing conditions in vitro

Michael A. Harrison, Nicholas Tsinoremas, John F. Allen

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

Reversible, light-dependent protein phosphorylation was observed in isolated thylakoid membranes of the cyanobacterium Synechococcus 6301. A polypeptide of 15 kDA in particular was phosphorylated under plastoquinone-reducing conditions and was not phosphorylated under plastoquinone-oxidising conditions. Phosphorylation and dephosphorylation reactions involving this and several other membrane polypeptides showed sensitivity to inhibitors of protein kinases and phosphatases. Changes in phosphorylation state correlated with changes in low temperature fluorescence emission characteristic or changes in excitation energy distribution between the photosystems. The 15 kDa phosphopolypeptide is likely to be involved directly in light state adaptations in cyanobacteria.

Original languageEnglish
Pages (from-to)295-299
Number of pages5
JournalFEBS Letters
Volume282
Issue number2
DOIs
StatePublished - May 6 1991
Externally publishedYes

Fingerprint

Thylakoid Membrane Proteins
Plastoquinone
Phosphorylation
Cyanobacteria
Ocular Adaptation
Synechococcus
Membranes
Peptides
Thylakoids
Excitation energy
Phosphoprotein Phosphatases
Fluorescence
Light
Temperature
In Vitro Techniques
Proteins

Keywords

  • Cyanobacterium
  • Phosphatase
  • Photosynthesis, Protein phosphorylation
  • Protein kinase
  • State transition

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Cyanobacterial thylakoid membrane proteins are reversibly phosphorylated under plastoquinone-reducing conditions in vitro. / Harrison, Michael A.; Tsinoremas, Nicholas; Allen, John F.

In: FEBS Letters, Vol. 282, No. 2, 06.05.1991, p. 295-299.

Research output: Contribution to journalArticle

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