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Light-independent and light-dependent protochlorophyllide-reducing activities and two distinct NADPH-protochlorophyllide oxidoreductase polypeptides in mountain pine (Pinus mugo)

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Abstract

Lower plants and gymnosperms synthesize chlorophyll and develop photosynthetically competent chloroplasts even when grown in the dark. In cell-free extracts of pine (Pinus mugo, Turra, ssp. mugo) seedlings, light-independent and light-dependent protochlorophyllide-reducing activities are present. Two distinct NADPH-protochlorophyllide-oxidoreductase (POR) polypeptides can be detected immunologically with an antiserum raised against the POR of barley. The subcellular localization and amounts of the two POR polypeptides are differentially affected by light: one of them is predominantly present in prolamellar bodies of etiochloroplasts and its abundance rapidly declines once the pine seedlings are exposed to light; the other is found in thylakoid membranes and its amount does not change during illumination of dark-grown seedlings. Two types of cDNA sequences are identified that encode two distinct POR polypeptides in pine. The relevance of these POR polypeptides for the two chlorophyll biosynthetic pathways active in gymnosperms is discussed.

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Abbreviations

Chlide:

chlorophyllide

HPLC:

high-performance liquid chromatography

PAGE:

polyacrylamide gel electrophoresis

Pchlide:

protochlorophyllide

PLB:

prolamellar body

POR:

protochlorophyllide oxidoreductase

SDS:

sodium dodecyl sulfate

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We are grateful to Drs. D. Dörnemann and H. Senger (Botanical Institute of the Philipps-Universität, Marburg, FRG) for their kind help in pigment analysis and to Dr. B. van Cleve (ETH Zürich) for her help during the preparation of ultrathin sections. We also like to thank Dr. Greg Armstrong for reading the manuscript, Dr. D. Rubli for art work (both Institut für Pflanzenwissenschaften, ETH Zürich) C. Marquard and M. Motzkus for technical assistance and U. Aguilar for typing the manuscript. This work was supported by the Swiss National Foundation.

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Forreiter, C., Apel, K. Light-independent and light-dependent protochlorophyllide-reducing activities and two distinct NADPH-protochlorophyllide oxidoreductase polypeptides in mountain pine (Pinus mugo). Planta 190, 536–545 (1993). https://doi.org/10.1007/BF00224793

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  • DOI: https://doi.org/10.1007/BF00224793

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