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首页> 外文期刊>Plant Cell Reports >AtCML8, a calmodulin-like protein, differentially activating CaM-dependent enzymes in Arabidopsis thaliana
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AtCML8, a calmodulin-like protein, differentially activating CaM-dependent enzymes in Arabidopsis thaliana

机译：AtCML8，一种钙调蛋白样蛋白，在拟南芥中差异激活CaM依赖性酶

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摘要

Plants express many calmodulins (CaMs) and calmodulin-like (CML) proteins that sense and transduce different Ca2+ signals. Previously, we reported divergent soybean (Glycine max) CaM isoforms (GmCaM4/5) with differential abilities to activate CaM-dependent enzymes. To elucidate biological functions of divergent CaM proteins, we isolated a cDNA encoding a CML protein, AtCML8, from Arabidopsis. AtCML8 shows highest identity with GmCaM4 at the protein sequence level. Expression of AtCML8 was high in roots, leaves, and flowers but low in stems. In addition, the expression of AtCML8 was induced by exposure to salicylic acid or NaCl. AtCML8 showed typical characteristics of CaM such as Ca2+-dependent electrophoretic mobility shift and Ca2+ binding ability. In immunoblot analyses, AtCML8 was recognized only by antiserum against GmCaM4 but not by GmCaM1 antibodies. Interestingly, AtCML8 was able to activate phosphodiesterase (PDE) but did not activate NAD kinase. These results suggest that AtCML8 acts as a CML protein in Arabidopsis with characteristics similar to soybean divergent GmCaM4 at the biochemical levels.
机译：植物表达许多钙调蛋白（CaMs）和钙调蛋白样（CML）蛋白，它们可以感应并转导不同的Ca 2 + 信号。以前，我们报道了不同的​​大豆（Glycine max）CaM亚型（GmCaM4 / 5），具有不同的激活CaM依赖酶的能力。为了阐明不同CaM蛋白的生物学功能，我们从拟南芥中分离了编码CML蛋白AtCML8的cDNA。 AtCML8在蛋白质序列水平上与GmCaM4的同一性最高。 AtCML8的表达在根，叶和花中高，但在茎中低。另外，通过暴露于水杨酸或NaCl诱导AtCML8的表达。 AtCML8具有CaM的典型特征，如Ca 2 + 依赖的电泳迁移率变化和Ca 2 + 结合能力。在免疫印迹分析中，AtCML8仅被抗GmCaM4的抗血清识别，而未被GmCaM1抗体识别。有趣的是，AtCML8能够激活磷酸二酯酶（PDE），但不能激活NAD激酶。这些结果表明，AtCML8在拟南芥中起CML蛋白的作用，其生化水平与大豆发散的GmCaM4相似。

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