Transport of peroxisomal proteins synthesized as large precursors in plants |
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Authors: | Akira Kato Makoto Hayashi Maki Kondo Mikio Nishimura |
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Institution: | (1) Department of Cell Biology, National Institute for Basic Biology, 444-8585 Okazaki, Japan |
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Abstract: | Plant peroxisomes contain at least four proteins, namely, citrate synthase, malate dehydrogenase, long-chain acyl-CoA oxidase,
and 3-ketoacyl-CoA thiolase, which are synthesized as large precursors with an N-terminal cleavable presequence. Each presequence
has a conserved domain (RI/L./Q]-X5-HL) that is homologous to peroxisomal targeting signal 2 from mammals and yeasts. In addition, a cysteine residue is found
at the C-terminal ends of the presequences, whose function has not yet been described. The authors analyzed the function of
the presequences and the conserved amino acids using transgenic Arabidopsis plants, which accumulate β-glucuronidase carrying the presequence of the peroxisomal proteins from plants. Immunological
and immunocytochemical studies on the transgenic plants showed that a conserved sequence in the extrapeptides is essential
for targeting to peroxisomes, and a cysteine residue at the cleavage site is involved in the processing of the presequence.
These results suggest that the presequences of the peroxisomal proteins function as targeting signals, and are necessary for
the recognition of the processing. |
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Keywords: | Peroxisome glyoxysome peroxisomal targeting signal 2 (PTS2) citrate synthase malate dehydrogenase pumpkin transgenic Arabidopsis |
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