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Amino acid sequences of heterotrophic and photosynthetic ferredoxins from the tomato plant (Lycopersicon esculentum Mill.)
Authors:Kaeko Kamide  Harumi Sakai  Koh Aoki  Yukika Sanada  Keishiro Wada  Laura S. Green  Boihon C. Yee  Bob B. Buchanan
Affiliation:(1) Department of Biology, Faculty of Science, Kanazawa University, Kakuma, 920-11 Kanazawa, Japan;(2) Department of Plant Biology, University of California, 111 Koshland Hall, 94720 Berkeley, California, USA;(3) Present address: Central Research Institute, Green Cross Co., Ltd., Shoudai, 500 Hirakata, Japan;(4) Present address: Toyobo Co, Ltd., Pharmaceuticals Production Technology Center, Katata, 520-20 Ohtsu, Shiga, Japan;(5) Present address: Department of Biochemistry, University of Missouri, 65211 Columbia, MO, USA
Abstract:Several forms (isoproteins) of ferredoxin in roots, leaves, and green and red pericarps in tomato plants (Lycopersicon esculentum Mill.) were earlier identified on the basis of N-terminal amino acid sequence and chromatographic behavior (Green et al. 1991). In the present study, a large scale preparation made possible determination of the full length amino acid sequence of the two ferredoxins from leaves. The ferredoxins characteristic of fruit and root were sequenced from the amino terminus to the 30th residue or beyond. The leaf ferredoxins were confirmed to be expressed in pericarp of both green and red fruit. The ferredoxins characteristic of fruit and root appeared to be restricted to those tissue. The results extend earlier findings in demonstrating that ferredoxin occurs in the major organs of the tomato plant where it appears to function irrespective of photosynthetic competence.Abbreviations CBB Coomassie brilliant blue R-250 - Cm Carboxymethylated - Fd Ferredoxin - FNR ferredoxin-NADP+ oxidoreductase - FPLC Fast protein liquid chromatography - HPLC High performance liquid chromatography - rt root
Keywords:ferredoxin  chloroplast  chromoplast  amyloplast  fruit  pericarp  root
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