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Pumpkin hydroxypyruvate reductases with and without a putative C-terminal signal for targeting to microbodies may be produced by alternative splicing
Authors:Makoto Hayashi  Ryuji Tsugeki  Maki Kondo  Hitoshi Mori  Mikio Nishimura
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
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.
Keywords:alternative splicing  hydroxypyruvate reductase  microbody  leaf peroxisome  photorespiration  protein targeting
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