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PLANT PHYSIOLOGY , Vol 110, Issue 2 697-703, Copyright © 1996 by American Society of Plant Biologists

BIOCHEMISTRY AND ENZYMOLOGY

Violaxanthin De-Epoxidase (Purification of a 43-Kilodalton Lumenal Protein from Lettuce by Lipid-Affinity Precipitation with Monogalactosyldiacylglyceride)

D. C. Rockholm and H. Y. Yamamoto
College of Tropical Agriculture and Human Resources, Department of Plant Molecular Physiology, University of Hawaii at Manoa, 3190 Maile Way, Honolulu, Hawaii 96822

Violaxanthin de-epoxidase catalyzes the de-epoxidation of violaxanthin to antheraxanthin and zeaxanthin in the xanthophyll cycle. Its activity is optimal at approximately pH 5.2 and requires ascorbate. In conjunction with the transthylakoid pH gradient, the formation of antheraxanthin and zeaxanthin reduces the photo-chemical efficiency of photosystem II by increasing the nonradiative (heat) dissipation of energy in the antennae. Previously, violax-anthin de-epoxidase had been partially purified. Here we report its purification from lettuce (Lactuca sativa var Romaine) to one major polypeptide fraction, detectable by two-dimensional isoelectic focusing/sodium dodecyl sulfate-polyacrylamide gel electrophoresis, using anion-exchange chromatography on Mono Q and a novellipid-affinity precipitation step with monogalactosyldiacylglyceride. The association of violaxanthin de-epoxidase and monogalactosyldiacyglyceride at pH 5.2 is apparently specific, since little enzyme was precipitated by eight other lipids tested. Violaxanthin de-epoxidase has an isoelectric point of 5.4 and an apparent molecular mass of 43 kD. Partial amino acid sequences of the N terminus and tryptic fragments are reported. The peptide sequences are unique in the GenBank data base and suggest that violaxanthin de-epoxidase is nuclear encoded, similar to other chloroplast proteins localized in the lumen.


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