Spermine is a potent modulator of proton transport through LHCII.

J Plant Physiol

Department of Biology, University of Crete, Voutes University Campus, GR-70013 Heraklion, Crete, Greece. Electronic address:

Published: April 2015

The effect of spermine on proton transport across large unilamellar liposomes containing incorporated complexes of the PSII antenna has been studied with the application of a pH-sensitive dye entrapped inside the vesicles. Both monomeric LHCbs and trimeric LHCII increased the permeability of proteoliposomes to protons when in a partly aggregated state within the lipid membrane. We have previously shown that a spermine-induced conformational change in LHCII results in its aggregation and ultimately in the enhancement of excitation energy as heat (qE). In this paper, spermine-induced aggregation of LHCII was found to facilitate proton transport across the proteoliposomes, indicating that a second protective mechanism (other than qE) might exist and might be regulated in vivo by polyamines when photosynthesis is saturated in excess light.

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http://dx.doi.org/10.1016/j.jplph.2015.01.010DOI Listing

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