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

58Citations
Citations of this article
20Readers
Mendeley users who have this article in their library.

Abstract

Vacuolar-type H+-translocating pyrophosphatases (V-PPases) have 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 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.

Cite

CITATION STYLE

APA

Drozdowicz, Y. M., Lu, Y. P., Patel, V., Fitz-Gibbon, S., Miller, J. H., & Rea, P. A. (1999). A thermostable vacuolar-type membrane pyrophosphatase from the archaeon Pyrobaculum aerophilum: Implications for the origins of pyrophosphate- energized pumps. FEBS Letters, 460(3), 505–512. https://doi.org/10.1016/S0014-5793(99)01404-0

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free