The zeaxanthin epoxidase is degraded along with the D1 protein during photoinhibition of photosystem II.

The xanthophyll zeaxanthin is synthesized in chloroplasts upon high light exposure of plants and serves central photoprotective functions. The reconversion of zeaxanthin to violaxanthin is catalyzed by the zeaxanthin epoxidase (ZEP). ZEP shows highest activity after short and moderate high light periods, but becomes gradually down-regulated in response to increasing high light stress along with down-regulation of photosystem II (PSII) activity. ZEP activity and ZEP protein levels were studied in response to high light stress in four plant species: Arabidopsis thaliana, Pisum sativum, Nicotiana benthamiana and Spinacia oleracea. In all species, ZEP protein was degraded during photoinhibition of PSII in parallel with the D1 protein of PSII. In the presence of streptomycin, an inhibitor of chloroplast protein synthesis, photoinhibition of PSII and ZEP activity as well as degradation of D1 and ZEP protein was strongly increased, indicating a close correlation of ZEP regulation with PSII photoinhibition and repair. The concomitant high light-induced inactivation/degradation of ZEP and D1 prevents the reconversion of zeaxanthin during photoinhibition and repair of PSII. This regulation of ZEP activity supports a coordinated degradation of D1 and ZEP during photoinhibition/repair of PSII and an essential photoprotective function of zeaxanthin during the PSII repair cycle.