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Updated: May 5, 2026

Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves
Published on: March 9, 2014
Fluorescence studies on interaction between phospho-LHC II and subchloroplast Photosystem 1 preparations
S M Kochubey1, V V Shevchenko, O I Volovik
1Institute of Plant Physiology and Genetics, Ukrainian Academy of Sciences, 252022, Kiev, Ukraine.
Abstract:
Chloroplast proteins were phosphorylated under two test conditions: 'white light' irradiance alone and 'white light' irradiance with the addition of glucose and glucose oxidase, used to produce an anaerobic medium. The interaction of phospho-LHC II with Photosystem 1 (PS 1) was studied for two types of PS I preparation. Changes in the chlorophyll a/b ratio and the ratio of 650 and 680 nm band intensities (E650/E680) in fluorescence excitation spectra were used in calculating the phospho-LHC II portion which became associated with PS 1. It is shown that the associated portion of phospho-LHC II varies for each of the PS 1 preparations and phosphorylation procedures. Possible conclusions as regards the transfer of various sets of LHC II subpopulations under different phosphorylation procedures and the differences of interaction with PS 1 are discussed.
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