Phosphate-starvation response in plant cells: de novo synthesis and degradation of acid phosphatases.
Phosphate-starvation response in plant cells: de novo synthesis and degradation of acid phosphatases.
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植物细胞中的磷酸盐饥饿反应：酸性磷酸酶的从头合成和降解。
DOI：
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发表时间：
1991
影响因子：
11.1
通讯作者：
D. Lefebvre
中科院分区：
文献类型：
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作者：
S. Duff;W. Plaxton;D. Lefebvre
磷酸酶活性的诱导是植物细胞对缺磷反应的重要组成部分。黑菜悬浮细胞含有两种主要的诱导酸性磷酸酶(APase)同工酶：液泡型磷酸烯醇式丙酮酸(PEP)同工酶和细胞壁非特异性APase。纯化的PEP-APase多克隆抗体可与两种同工酶发生交叉反应。此外，抗(PEP-APase)IgG检测到来自广泛高等植物的蛋白质，这表明主要的植物APase同工酶已经偏离了共同的祖先形式。免疫印迹定量结果表明，在由等电点充足向低等电点转变的悬浮细胞中，总抗原性APase蛋白含量与总酶活性密切相关。这一点也在完整的植物根部表现出来。因此，该酶的活性受控于APase的合成和降解。两种主要APase同工酶的数量在PI剥夺后同时发生增加，这表明参与了共同的调控机制。
Induction of phosphatase activity is an important component of the plant cell response to phosphate deficiency. Suspension cell cultures of Brassica nigra contain two major inducible acid phosphatase (APase) isozymes; vacuolar phosphoenolpyruvate (PEP) APase and cell wall nonspecific APase. Polyclonal antibodies raised against purified PEP-APase crossreacted specifically with both isozymes. Furthermore, anti-(PEP-APase) IgG detected proteins from a wide range of higher plants, suggesting that the major plant APase isozymes have diverged from a common ancestral form. Quantification on immunoblots indicated that in B. nigra suspension cells experiencing transition from Pi sufficiency to deficiency or vice versa, the amount of total antigenic APase protein correlated closely with total enzyme activity. This was also shown in intact plant roots. Therefore, the activity was governed by the synthesis and degradation of APases. Increases in the amounts of both major APase isozymes occurred simultaneously following Pi deprivation of B. nigra suspension cells, suggesting the involvement of a common regulatory mechanism.