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Correlation of membrane protein phosphorylation with excitation energy distribution in the cyanobacterium Synechococcus 6301
Author(s) -
Allen John F.,
Sanders Christine E.,
Holmes Nigel G.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80167-8
Subject(s) - synechococcus , thylakoid , phycobilisome , phosphorylation , photosystem , photosystem ii , biophysics , cyanobacteria , photosystem i , biology , protein phosphorylation , biochemistry , photosynthesis , chemistry , chloroplast , bacteria , protein kinase a , genetics , gene
Synechococcus cells grown on [ 32 P]orthophosphate exhibit light‐dependent phosphorylation of polypeptides at 18.5 kDa (soluble fraction) and 15 kDa (membrane fraction). The 15 kDa polypeptide is also phosphorylated in the light in isolated Synechococcus thylakoids incubated with [γ‐ 32 P]ATF. 77 K fluorescence emission spectra of both cells and thylakoids show increased photosystem I emission and decreased photosystem II 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 organization is not a necessary condition for protein phosphorylation‐dependent adaptations to changing wavelength of light.