Carotenoid and chlorophyll biosynthesis in isolated plastids from mustard seedling cotyledons (Sinapis alba L.) during etioplast-chloroplast conversion

Etioplasts and etiochloroplasts, isolated from seedlings of white mustard (Sinapis alba L.) grown in continuous far-red light, and chloroplasts isolated from cotyledons and primary leaves of white-light-grown seedlings exhibit high prenyl-lipid-forming activities. Only the etioplasts and etiochlorop...

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Bibliographic Details
Published in:Planta 1987, Vol.170 (1), p.121-129
Main Authors: Luetke-Brinkhaus, F. (Freiburg Univ. (Germany, F.R.). Inst. fuer Biologie 2), Kleinig, H
Format: Article
Language:English
Subjects:
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
Biological and medical sciences
BIOSINTESIS
BIOSYNTHESE
BIOSYNTHESIS
BRASSICA ALBA
CAROTENOIDE
CAROTENOIDES
CAROTENOIDS
Chlorophyll
CHLOROPHYLLE
CHLOROPHYLLS
Chloroplasts
CLOROFILAS
COTILEDONES
COTYLEDON
COTYLEDONS
Diphosphates
Enzymaktivitaet
Enzymes
ENZYMIC ACTIVITY
Etioplasts
Fundamental and applied biological sciences. Psychology
Karotinoid
Kotyledone
Lipids
Metabolism
Pigmentsynthese
Plant physiology and development
PLASTE
Plastidentwicklung
PLASTIDIOS
PLASTIDS
Saemling
Seedlings
Sinapis
Storage and secretion, pigments, phytochrome
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Summary:Etioplasts and etiochloroplasts, isolated from seedlings of white mustard (Sinapis alba L.) grown in continuous far-red light, and chloroplasts isolated from cotyledons and primary leaves of white-light-grown seedlings exhibit high prenyl-lipid-forming activities. Only the etioplasts and etiochloroplasts, and to a much lesser extent chloroplasts from cotyledons are capable of forming carotenes from isopentenyl diphosphate as substrate, whereas in chloroplasts from primary leaves no such activities could be detected. By subfractionation experiments, it could be demonstrated that the phytoene-synthase complex in etioplasts and etiochloroplasts is present in a soluble form in the stroma, whereas the subsequent enzymes, i.e. the dehydrogenase, cis-trans isomerase and cyclase are bound to both membrane fractions, the prolamellar bodies/prothylakoids and the envelopes. In good agreement with previous results using isolated chromoplasts and chloroplasts, it is concluded that the phytoene-synthase complex may change its topology from a peripheral membrane protein in non-green plastids to a tightly membrane-associated protein in chloroplasts. This change is apparently paralleled by altered functional properties which render the complex undetectable in isolated chloroplasts. Further experiments concerning the reduction of chlorophyll a containing a geranylgeranyl side chain to chlorophyll a indicate that the light-induced etioplast-chloroplast conversion is accompanied by a certain reorganization of the polyprenoid-forming enzymatic equipment.
ISSN:0032-0935
1432-2048
DOI:10.1007/BF00392388