Lewis M L, Miki K, Ueda T
Department of Bioscience, Program in Molecular Biology and Biotechnology, Salem-Teikyo University, 223 W. Main Street, Salem, WV 26426-0500, USA.
Gene. 2000 Apr 4;246(1-2):81-91. doi: 10.1016/s0378-1119(00)00045-7.
A cDNA corresponding to 1-Cys peroxiredoxin, an evolutionarily conserved thiol-specific antioxidant enzyme, was isolated from buckwheat (Fagopyrum esculentum Moench), a dicotyledonous plant species belonging to the Polygonaceae family. The cDNA, which we have designated as FePer1, contains a major open reading frame capable of encoding a polypeptide of 219 residues with a predicted molecular mass of 24.3kDa. The deduced primary structure of FePer1 polypeptide shows a high level (about 70%) of sequence homology to other recently identified plant 1-Cys peroxiredoxins. FePer1 also exhibits a significant level of sequence similarity to non-plant 1-Cys peroxiredoxins, sharing 52 and 42% identities with mammalian and fungal 1-Cys peroxiredoxins, respectively. As for all 1-Cys peroxiredoxins identified from various organisms, the amino acid sequence proposed to constitute the active site of the enzyme is highly conserved in FePer1 polypeptide. The gene corresponding to FePer1 cDNA is a single-copy gene in the buckwheat genome. Its expression is regulated in a seed-specific and temporal manner during seed development. FePer1 gene is induced transiently for a short period immediately after seed imbibition.
从属于蓼科的双子叶植物荞麦(苦荞麦)中分离出了与1-半胱氨酸过氧化物酶(一种进化上保守的硫醇特异性抗氧化酶)相对应的cDNA。我们将该cDNA命名为FePer1,它包含一个主要的开放阅读框,能够编码一个由219个残基组成的多肽,预测分子量为24.3kDa。FePer1多肽推导的一级结构与其他最近鉴定的植物1-半胱氨酸过氧化物酶具有高度的序列同源性(约70%)。FePer1与非植物1-半胱氨酸过氧化物酶也表现出显著的序列相似性,分别与哺乳动物和真菌的1-半胱氨酸过氧化物酶有52%和42%的同源性。对于从各种生物体中鉴定出的所有1-半胱氨酸过氧化物酶来说,在FePer1多肽中构成该酶活性位点的氨基酸序列是高度保守的。与FePer1 cDNA相对应的基因在荞麦基因组中是单拷贝基因。其表达在种子发育过程中以种子特异性和时间性的方式受到调控。FePer1基因在种子吸胀后立即被短暂诱导。