A thermostable vacuolar-type membrane pyrophosphatase from the archaeon Pyrobaculum aerophilum:: implications for the origins of pyrophosphate-energized pumps

被引：59

作者：

Drozdowicz, YM

Lu, YP

Patel, V

Fitz-Gibbon, S

Miller, JH

Rea, PA ^{[1
]}

机构：

[1] Univ Penn, Dept Biol, Inst Plant Sci, Philadelphia, PA 19104 USA

[2] Univ Calif Los Angeles, Dept Microbiol & Mol Genet, Los Angeles, CA 90095 USA

来源：

FEBS LETTERS | 1999年 / 460卷 / 03期

基金：

美国国家科学基金会;

关键词：

archaeon; inorganic pyrophosphatase; proton pump; pyrophosphate; vacuolar-type H+-pyrophosphatase; Pyrobaculum aerophilum;

D O I：

10.1016/S0014-5793(99)01404-0

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：

Vacuolar-type H+-translocating pyrophosphatases (V-PPases) hale been considered to be restricted to plants, a few species of phototrophic proteobacteria and protists. Here, we describe PVP, a thermostable, sequence-divergent V-PPase from the facultatively aerobic hyperthermophilic archaeon Pyrobaculum nel aerophilum. PVP shares only 38% sequence identity with both the prototypical V-PPase from Arabidopsis thaliana and the H+-PPi synthase from Rhodospirillum rubrum, yet possesses most of the structural features characteristic of V-PPases, Heterologous expression of PVP in Saccharomyces cerevisiae yields a M-r 64 000 membrane polypeptide that specifically catalyzes Mg2+-dependent PPi hydrolysis. The existence of PVP implies that PPi-energized H+-translocation is phylogenetically more deeply rooted than previously: thought, (C) 1999 Federation of European Biochemical Societies.

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收藏

页码：505 / 512

页数：8

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