Chlamydomonas reinhardtii has a small family of purple acid phosphatase homologue genes that are differentially expressed in response to phytate
Chlamydomonas reinhardtii has a small family of purple acid phosphatase homologue genes that are differentially expressed in response to phytate
复制标题
DOI：
10.1007/s13213-013-0688-8
复制
发表时间：
2014-06-01
影响因子：
3
通讯作者：
Aurora Herrera-Valencia, Virginia
中科院分区：
文献类型：
--
作者：
Arturo Rivera-Solis, Rodrigo;Peraza-Echeverria, Santy;Aurora Herrera-Valencia, Virginia
紫酸性磷酸酶（PAPs）是一种金属磷酸酯酶，参与磷的获取和再循环。来自微生物和植物的PAP植酸酶负责植酸的去磷酸化。植酸盐是植物种子中磷的主要储存形式，也是土壤中有机磷的主要形式。虽然在莱茵衣藻中已经研究了一些磷酸酶，但迄今为止还没有鉴定出PAPs的基因编码。本研究在莱茵假体中鉴定了6个PAP同源基因（CrPAP1 ~ CrPAP6）。在所有6个crpap中都发现了包含PAP酶特征的7个保守残基的金属磷酸酯酶结构域。由来自微藻、植物和动物的PAP同源序列组成的系统发育树显示出9个主要分支，其中4个分支中存在crpap。CrPAP2、CrPAP3、CrPAP4和CrPAP6在所有培养基中均有组成性表达，而CrPAP1和CrPAP5在不含磷酸盐的培养基中通过添加植酸盐诱导表达。我们的研究结果为进一步分析CrPAP基因家族的功能以及评估它们在莱茵梭菌中作为植酸酶的潜力提供了一个起点。
Purple acid phosphatases (PAPs) are metallophosphoesterase enzymes involved in the acquisition and recycling of phosphorus. PAP phytases from microorganisms and plants are responsible for the dephosphorylation of phytate. Phytate is the main storage form of phosphorus in plant seeds and constitutes the major form of organic phosphorus present in soil. Although some phosphatases have been studied in Chlamydomonas reinhardtii, no gene coding for PAPs have so far been characterized. In this study, six PAP homologue genes were identified and characterized in silico in C. reinhardtii (CrPAP1 to CrPAP6). A metallophosphoesterase domain including the seven conserved residues characteristic of PAP enzymes was found in all six CrPAPs. The phylogenetic tree comprising PAP homologue sequences from microalgae, plants, and animals showed nine major clades and CrPAPs resolved in four of them. A constitutive expression was found for CrPAP2, CrPAP3, CrPAP4, and CrPAP6 in all media tested, while CrPAP1 and CrPAP5 were induced by the addition of phytate in a medium without phosphate salts. Our results provide a starting point for further functional analysis of the CrPAP gene family, and the evaluation of their potential as phytases in C. reinhardtii.