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Volume 193, number 2 FEES 3160 December 1985 Correlation of membrane protein phosphorylation with
 

Summary: Volume 193, number 2 FEES 3160 December 1985
Correlation of membrane protein phosphorylation with
excitation energy distribution in the cyanobacterium
Synechococcus 6301
John F. Alien*, Christine E. Sanders and Nigel G. Holmes
Department of Plant Sciences, University of Leeds, Leeds LS2 9JT, England
Received 30 September 1985
Synechococcus cells grown on [32P]orthophosphateexhibit light-dependentphosphorylationof polypeptides
at 18.5kDa (solublefraction) and 15kDa (membranefraction).The 15kDa polypeptide is also phosphory-
lated in the light in isolated Synechococcus thylakoids incubated with [y-^P]ATP. 77 K fluorescence emis-
sion spectra of both cells and thylakoids showincreasedphotosystem I emission and decreased photosystem
I1 emission under conditions required for protein phosphorylation. We propose that membrane protein
phosphorylation regulates distribution of absorbed excitation energy between the two photosystems in
Synechococcus and other phycobilisome-containing organisms, and that lateral heterogeneity in thylakoid
organizationis not a necessary condition for protein phosphorylation-dependent adaptations to changing
wavelength of light.
Photosynthesis Cyanobacteria Light harvesting State 1-state 2 transition Protein phosphorylation
Excitation transfer
1. INTRODUCTION
In green plants light harvesting is accomplished

  

Source: Allen, John F. - School of Biological and Chemical Sciences, Queen Mary, University of London

 

Collections: Renewable Energy; Biology and Medicine