Olczak Mariusz, Olczak Teresa
Institute of Biochemistry and Molecular Biology, Wroclaw University, Tamka 2, Wroclaw, Poland.
FEBS Lett. 2002 May 22;519(1-3):159-63. doi: 10.1016/s0014-5793(02)02740-0.
A cDNA encoding previously purified and characterized diphosphonucleotide phosphatase/phosphodiesterase (PPD1) from yellow lupin (Lupinus luteus L.) was identified. The ppd1 gene encodes a protein containing a cleavable signal sequence. A functional expression of PPD1 in Saccharomyces cerevisiae confirmed the proper gene identification. A gene homologous to ppd1, encoding a putative membrane protein (PPD2), as well as fragments of two other genes encoding PPD3 and PPD4 proteins were also isolated. Amino acids composing the putative active center of PPD1 and PPD2 are similar to those present in known purple acid phosphatases, which suggests that the reported genes might encode a novel group of specific metallophosphatases. RT-PCR revealed that the corresponding PPD1 mRNA accumulates in stems and leaves, and PPD2 mRNA in stems, leaves and seedlings.
鉴定出一个编码来自黄羽扇豆（Lupinus luteus L.）的先前纯化和表征的二磷酸核苷酸磷酸酶/磷酸二酯酶（PPD1）的cDNA。ppd1基因编码一种含有可切割信号序列的蛋白质。PPD1在酿酒酵母中的功能表达证实了基因鉴定的正确性。还分离出了与ppd1同源的一个编码假定膜蛋白（PPD2）的基因，以及另外两个分别编码PPD3和PPD4蛋白的基因片段。构成PPD1和PPD2假定活性中心的氨基酸与已知紫色酸性磷酸酶中的氨基酸相似，这表明所报道的基因可能编码一组新型的特异性金属磷酸酶。逆转录聚合酶链反应（RT-PCR）显示，相应的PPD1 mRNA在茎和叶中积累，而PPD2 mRNA在茎、叶和幼苗中积累。
