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Title: AVP2, a sequence-divergent, K{sup +}-insensitive H{sup +}-translocating inorganic pyrophosphatase from arabidopsis

Abstract

Plant vacuolar H{sup +}-translocating inorganic pyrophosphatase have been considered to constitute a family of functionally and structurally monotonous intrinsic membrane proteins. Typified by AVPI from Arabidopsis, all characterized plant V-PPases share greater than 84% sequence identity and catalyze K{sup +}-stimulated H{sup +} translocation. Here the authors describe the molecular and biochemical characterization of AVP2, a sequence-divergent K{sup +}-insensitive, Ca{sup 2+}-hypersensitive V-PPase active in both inorganic pyrophosphate hydrolysis and H{sup +} translocation. The differences between AVP2 and AVP1 provide the first indication that plant V-PPase sequences from the same organism fall into two distinct categories. Phylogenetic analyses of these and other V-PPase sequences extend this principle by showing that AVP2, rather than being an isoform of AMP1, is but one representative of a novel category of AVP2-like (type 2) V-PPases that coexist with AVP1-like (type 1) V-PPases not only in plants, but also in apicomplexan protists such as the malarial parasite Plasmodium falciparum.

Authors:
; ;
Publication Date:
Research Org.:
Univ. of Pennsylvania, Philadelphia, PA (US)
OSTI Identifier:
20062530
Resource Type:
Journal Article
Journal Name:
Plant Physiology (Bethesda)
Additional Journal Information:
Journal Volume: 123; Journal Issue: 1; Other Information: PBD: May 2000; Journal ID: ISSN 0032-0889
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; PLANT CELLS; TRANSLOCATION; ARABIDOPSIS; PHOSPHATASES; HYDROGEN IONS 1 PLUS; POTASSIUM COMPOUNDS; MOLECULAR STRUCTURE

Citation Formats

Drozdowicz, Y.M., Kissinger, J.C., and Rea, P.A. AVP2, a sequence-divergent, K{sup +}-insensitive H{sup +}-translocating inorganic pyrophosphatase from arabidopsis. United States: N. p., 2000. Web. doi:10.1104/pp.123.1.353.
Drozdowicz, Y.M., Kissinger, J.C., & Rea, P.A. AVP2, a sequence-divergent, K{sup +}-insensitive H{sup +}-translocating inorganic pyrophosphatase from arabidopsis. United States. doi:10.1104/pp.123.1.353.
Drozdowicz, Y.M., Kissinger, J.C., and Rea, P.A. Mon . "AVP2, a sequence-divergent, K{sup +}-insensitive H{sup +}-translocating inorganic pyrophosphatase from arabidopsis". United States. doi:10.1104/pp.123.1.353.
@article{osti_20062530,
title = {AVP2, a sequence-divergent, K{sup +}-insensitive H{sup +}-translocating inorganic pyrophosphatase from arabidopsis},
author = {Drozdowicz, Y.M. and Kissinger, J.C. and Rea, P.A.},
abstractNote = {Plant vacuolar H{sup +}-translocating inorganic pyrophosphatase have been considered to constitute a family of functionally and structurally monotonous intrinsic membrane proteins. Typified by AVPI from Arabidopsis, all characterized plant V-PPases share greater than 84% sequence identity and catalyze K{sup +}-stimulated H{sup +} translocation. Here the authors describe the molecular and biochemical characterization of AVP2, a sequence-divergent K{sup +}-insensitive, Ca{sup 2+}-hypersensitive V-PPase active in both inorganic pyrophosphate hydrolysis and H{sup +} translocation. The differences between AVP2 and AVP1 provide the first indication that plant V-PPase sequences from the same organism fall into two distinct categories. Phylogenetic analyses of these and other V-PPase sequences extend this principle by showing that AVP2, rather than being an isoform of AMP1, is but one representative of a novel category of AVP2-like (type 2) V-PPases that coexist with AVP1-like (type 1) V-PPases not only in plants, but also in apicomplexan protists such as the malarial parasite Plasmodium falciparum.},
doi = {10.1104/pp.123.1.353},
journal = {Plant Physiology (Bethesda)},
issn = {0032-0889},
number = 1,
volume = 123,
place = {United States},
year = {2000},
month = {5}
}