Pumpkin hydroxypyruvate reductases with and without a putative C-terminal signal for targeting to microbodies may be produced by alternative splicing |
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Authors: | Makoto Hayashi Ryuji Tsugeki Maki Kondo Hitoshi Mori Mikio Nishimura |
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Institution: | (1) Department of Cell Biology, National Institute for Basic Biology, 444 Okazaki, Japan;(2) Present address: Carnegie Institution of Washington, Department of Embryology, 115 West University Parkway, 21210 Baltimore, MD, USA;(3) Present address: Graduate Course of Biochemical Regulation, School of Agricultural Science, Nagoya University, Chikusa, 464-01 Nagoya, Japan |
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Abstract: | Two full-length cDNAs encoding hydroxypyruvate reductase were isolated from a cDNA library constructed with poly(A)+ RNA from pumpkin green cotyledons. One of the cDNAs, designated HPR1, encodes a polypeptide of 386 amino acids, while the other cDNA, HPR2 encodes a polypeptide of 381 amino acids. Although the nucleotide and deduced amino acid sequences of these cDNAs are almost identical, the deduced HPR1 protein contains Ser-Lys-Leu at its carboxy-terminal end, which is known as a microbody-targeting signal, while the deduced HPR2 protein does not. Analysis of genomic DNA strongly suggests that HPR1 and HPR2 are produced by alternative splicing. |
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Keywords: | alternative splicing hydroxypyruvate reductase microbody leaf peroxisome photorespiration protein targeting |
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