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Activity of the Fe-Branch of Tetrapyrrole Biosynthesis in the Chlorophyll-Deficient Plastome Mutant of Sunflower
Authors:Lezhneva  L. A.  Rassadina  V. V.  Yaronskaya  E. B.  Radyuk  M. S.  Taran  S. F.  Averina  N. G.
Affiliation:(1) Institute of Photobiology, National Academy of Sciences of Belarus, ul. Akademicheskaya 27, Minsk, 220072, Belarus;(2) Rostov State University, Rostov-on-Don
Abstract:The biosynthesis of heme, a plant tetrapyrrole, was studied in the leaves of a chlorophyll-deficient plastome mutant of the sunflower (Helianthus annuus L, line 2-24, albina form). In the light, the content of 5-aminolevulinic acid (ALA) in white mutant leaves was, on the average, ten times less than in that of the wild-type form (line 3629). Chlorophyll content in mutant leaves comprised only 0.3% of that of control plants. The activities of Fe-chelatase and ALA dehydratase in the heme synthesis were either comparable to or even higher than those in the wild-type leaves. A normal respiration rate in white mutant leaves, the equal content of phytochrome apoproteins in plants of both types, and the lack of noticeable morphogenetic differences realized through the phytochrome system can indicate that mutant and wild-type leaves are similar in their levels of phytochrome and the cytochromes of mitochondrial respiration. Nevertheless, in the mutant, the content of heme noncovalently bound by apoproteins amounted to only one third of its content in the wild-type plants. It seems that a dramatic decrease in the capability of white leaves for chlorophyll biosynthesis and for the formation of the photosynthetic apparatus is responsible for a low demand for chloroplast cytochromes, which is the major cause of a reduced heme content in the mutant.
Keywords:Helianthus annuus  plastome sunflower mutant (albina type)  5-aminolevulinic acid  5-aminolevulinate dehydratase  Fe-chelatase  hemin  chlorophyll
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