A nod factor binding lectin with apyrase activity from legume roots

A nod factor binding lectin with apyrase activity from legume roots
复制标题

DOI:
10.1073/pnas.96.10.5856
复制
发表时间:
1999-05-11
影响因子:
11.1
通讯作者:
Murphy, JB
Murphy, JB
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Etzler, ME;Kalsi, G;Murphy, JB

文献摘要

被引文献

相似文献

从豆科植物Dolichos biflorus的根中分离出的一种凝集素,与根瘤菌产生的结瘤因子结合,并具有推导的氨基酸序列,与迄今报道的任何凝集素没有显著的同源性。这种凝集素也是一种酶,催化二磷酸和三磷酸核苷的磷酸酸氢键的水解;在碳水化合物配体的存在下,酶的活性增加,这种凝集素核苷酸磷酸水解酶(LNP)具有磷水解酶apyrase类别的底物特异性,其序列包含这类酶的四个基序特征,LNP存在于根毛表面,用LNP的抗血清处理根,抑制根毛变形和在根瘤菌暴露下形成根瘤的能力。这些特性表明,该蛋白可能在根瘤菌-豆类共生和/或相关的植物内源碳水化合物识别事件中发挥作用。
A lectin isolated from the roots of the legume, Dolichos biflorus, binds to Nod factors produced by rhizobial strains that nodulate this plant and has a deduced amino acid sequence with no significant homology to any lectin reported to date. This lectin also is an enzyme that catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside di- and triphosphates; the enzyme activity is increased in the presence of carbohydrate ligands, This lectin-nucleotide phosphohydrolase (LNP) has a substrate specificity characteristic of the apyrase category of phosphohydrolases, and its sequence contains four motifs characteristic of this category of enzymes, LNP is present on the surface of the root hairs, and treatment of roots with antiserum to LNP inhibits their ability to undergo root hair deformation and to form nodules on exposure to rhizobia. These properties suggest that this protein may play a role in the rhizobium-legume symbiosis and/or in a related carbohydrate recognition event endogenous to the plant.