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Published on November 14, 2008; 10.1104/pp.108.129957


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Received September 16, 2008
Accepted November 11, 2008

The zeaxanthin-independent and zeaxanthin-dependent qE components of non-photochemical quenching involve common conformational changes within the Photosystem II antenna in Arabidopsis thaliana

Matthew P. Johnson *, Maria L. Perez-Bueno , Ahmad Zia , Peter Horton , and Alexander V. Ruban

School of Biological and Chemical Sciences, Queen Mary, University of London, Mile End, Bancroft Road, London, E1 4NS, United Kingdom; Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, United Kingdom

* Corresponding author; email: m.johnson{at}qmul.ac.uk.

The light harvesting antenna of higher plant photosystem II (LHCII) has the intrinsic capacity to dissipate excess light energy as heat in a process termed nonphotochemical quenching (NPQ). Recent studies suggest that zeaxanthin and lutein both contribute to the rapidly relaxing component of NPQ, qE, possibly acting respectively in the minor monomeric antenna complexes and the major trimeric LHCII. To distinguish whether zeaxanthin and lutein act independently as quenchers at separate sites, or alternatively whether zeaxanthin fulfils an allosteric role regulating lutein-mediated quenching, the kinetics of qE and the qE-related conformational changes ({Delta}A535) were compared in Arabidopsis thaliana mutant/ antisense plants with altered contents of minor antenna (kolhcb6, aslhcb4), trimeric LHCII (aslhcb2), lutein (lut2, lut2npq1, lut2npq2) and zeaxanthin (npq1, npq2). The kinetics of the two components of NPQ induction arising from zeaxanthin-independent and zeaxanthin-dependent qE were both sensitive to changes in the protein composition of the PSII antenna. The replacement of lutein by zeaxanthin or violaxanthin in the internal Lhcb protein binding sites affected the kinetics and relative amplitude of each component, as well as the absolute chlorophyll fluorescence lifetime. Both components of qE were characterized by a conformational change leading to nearly identical absorption changes in the Soret region that indicated the involvement of the LHCII lutein 1 domain. Based on these observations we suggest that both components of qE arise from a common quenching mechanism based upon a conformational change within the PSII antenna, optimized by Lhcb subunit-subunit interactions and tuned by the synergistic effects of external and internally bound xanthophylls.




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