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The carboxy‐terminal end of glycolate oxidase directs a foreign protein into tobacco leaf peroxisomes.
Author(s) -
Volokita M
Publication year - 1991
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.1991.t01-4-00999.x
Subject(s) - peroxisome , terminal (telecommunication) , tobacco leaf , biochemistry , chemistry , biology , gene , computer science , engineering , telecommunications , agricultural engineering
Summary The carboxy‐terminal residues of several peroxisomal proteins were shown to act as a peroxisomal targetting signal. This study was conducted to test whether the C‐terminus of glycolate oxidase, a key enzyme in the glycolate metabolism pathway, is functioning as a targetting signal that directs proteins into plant leaf peroxisomes. A chimeric gene coding for a fusion protein composed of the C‐terminal‐ truncated beta‐glucuronidase, a synthetic linker of four amino acids and the last six C‐terminal amino acids of glycolate oxidase, was constructed. Transformation of tobacco plants with the chimeric gene resulted in expression of beta‐glucuronidase enzymic activity. About 50% of the transgenic beta‐glucuronidase activity was localized to the peroxisomes. The results indicate that the six C‐terminal amino acid residues of glycolate oxidase act as a targetting signal that is recognized by leaf peroxisomes.