Structure, function and regulation of the plant vacuolar H+-translocating ATPase

被引:174
作者
Ratajczak, R [1 ]
机构
[1] Tech Univ Darmstadt, Inst Bot, D-64287 Darmstadt, Germany
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2000年 / 1465卷 / 1-2期
关键词
ATP hydrolysis; gene expression; holoenzyme structure; proton transport; subunit composition; V-ATPase;
D O I
10.1016/S0005-2736(00)00129-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The plant V-ATPase is a primary-active proton pump present at various components of the endomembrane system. It is assembled by different protein subunits which are located in two major domains, the membrane-integral V-o-domain and the membrane peripheral V-1-domain. At the plant vacuole the V-ATPase is responsible for energization of transport of ions and metabolites, and thus the V-ATPase is important as a 'house-keeping' and as a stress response enzyme. It has been shown that transcript and protein amount of the V-ATPase are regulated depending on metabolic conditions indicating that the expression of V-ATPase subunit is highly regulated. Moreover, there is increasing evidence that modulation of the holoenzyme structure might influence V-ATpase activity, (C) 2000 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:17 / 36
页数:20
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