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

Authors
Citation
R. Ratajczak, Structure, function and regulation of the plant vacuolar H+-translocating ATPase, BBA-BIOMEMB, 1465(1-2), 2000, pp. 17-36
Citations number
185
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
ISSN journal
00052736 → ACNP
Volume
1465
Issue
1-2
Year of publication
2000
Pages
17 - 36
Database
ISI
SICI code
0005-2736(20000501)1465:1-2<17:SFAROT>2.0.ZU;2-8
Abstract
The plant V-ATPase is a primary-active proton pump present at various compo nents of the endomembrane system. It is assembled by different protein subu nits which are located in two major domains, the membrane-integral V-o-doma in and the membrane peripheral V-1-domain. At the plant vacuole the V-ATPas e 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 respon se enzyme. It has been shown that transcript and protein amount of the V-AT Pase are regulated depending on metabolic conditions indicating that the ex pression of V-ATPase subunit is highly regulated. Moreover, there is increa sing evidence that modulation of the holoenzyme structure might influence V -ATpase activity, (C) 2000 Elsevier Science B.V. All rights reserved.