The carboxyl terminus of isocitrate lyase is not essential for import into glyoxysomes in an in vitro system.
作者： R. Behari , A. Baker
DOI: 10.1016/S0021-9258(18)53177-X
关键词: Amino acid 、 Biology 、 IDH1 、 Gene 、 Biochemistry 、 Glyoxysome 、 Peroxisome 、 RNA 、 Isocitrate lyase 、 Complementary DNA
摘要: Abstract A procedure has been established for the isolation of intact and import-competent glyoxysomes from cotyledons sunflower (Helianthus annuus) seedlings. Radiolabeled isocitrate lyase (a glyoxysomal matrix protein) was produced by in vitro transcription castor bean cDNA translation RNA a wheat germ lysate. The heterologous imported into isolated protease-protected. Dihydrofolate reductase, cytoplasmic protein, neither bound to nor glyoxysomes. Import not observed when glyoxysome fraction replaced mitochondrial fraction. import temperature- ATP-dependent. Progressive carboxyl-terminal truncations gene were transcribed translated yield polypeptides with same amino terminus but lacking varying amounts carboxyl terminus. All these characteristics as full-length suggesting that targeting information must be present within first 168 acids, and, unlike some other peroxisomal proteins, is dispensable import.
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