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

@article{Drozdowicz1999ATV,
  title={A thermostable vacuolar‐type membrane pyrophosphatase from the archaeon Pyrobaculum aerophilum: implications for the origins of pyrophosphate‐energized pumps},
  author={Yolanda M. Drozdowicz and Yu-Ping Lu and Vijay Muljihhai Patel and Sorel T. Fitz-Gibbon and Jeffrey H. Miller and Philip A. Rea},
  journal={FEBS Letters},
  year={1999},
  volume={460}
}

Identification and analysis of proton-translocating pyrophosphatases in the methanogenic archaeon Methanosarcina mazei

The pyrophosphatases of M. mazei Go1 represent the first examples of this enzyme class in methanogenic archaea and may be part of their energy-conserving system.

Presence of a plant-like proton-translocating pyrophosphatase in a scuticociliate parasite and its role as a possible drug target

The molecular cloning and functional characterization of a gene encoding an H+-pyrophosphatase in the protozoan scuticociliate parasite Philasterides dicentrarchi, which infects turbot is described for the first time.

Vacuolar type H+ pumping pyrophosphatases of parasitic protozoa.

Functional roles of arginine residues in mung bean vacuolar H+-pyrophosphatase.

Cloning and functional expression of a gene encoding a vacuolar-type proton-translocating pyrophosphatase from Trypanosoma cruzi.

Phylogenetic analysis of the available V-H(+)-PPase sequences indicates that TcPPase is nearer to the vascular plant cluster and the branch containing Chara, a precursor to land plants, than to any of the other pyrophosphatase sequences included in the analysis.

Differential Regulation of Soluble and Membrane-Bound Inorganic Pyrophosphatases in the Photosynthetic Bacterium Rhodospirillum rubrum Provides Insights into Pyrophosphate-Based Stress Bioenergetics

Results demonstrate a tight transcriptional regulation of the H(+)-PPase gene, which appears to be induced in response to a variety of environmental conditions, all of which constrain cell energetics.

Pyrophosphate-Fueled Na+ and H+ Transport in Prokaryotes

The determination of the three-dimensional structures of H+- and Na+-pyrophosphatases has been another recent breakthrough in the studies of these cation pumps.

AVP 2 , a Sequence-Divergent , K 1-Insensitive H 1-Translocating Inorganic Pyrophosphatase from Arabidopsis 1

The molecular and biochemical characterization of AVP2 is described, a sequence-divergent K-insensitive, Ca-hypersensitive V-PPase active in both inorganic pyrophosphate hydrolysis and H translocation that provides the first indication that plant V- PPases from the same organism fall into two distinct categories.
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References

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Pyrobaculum aerophilum sp. nov., a novel nitrate-reducing hyperthermophilic archaeum

A novel rod-shaped hyperthermophilic archaeum has been isolated from a boiling marine water hole at Maronti Beach, Ischia, Italy. It grew optimally at 100 degrees C and pH 7.0 by aerobic respiration

A vacuolar H+-pyrophosphatase in Acetabularia acetabulum: molecular cloning and comparison with higher plants and a bacterium

The primary structure of the H+-PPase from total RNA using reverse-transcription and PCR tech- was compared with the enzymes in higher plants and in the niques andignments of the primary structure to that of similar photosynthetic bacterium, R. rubrum were revealed.

Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport.

Heterologous expression of the cDNA (AVP) encoding the substrate-binding subunit of the vacuolar H(+)-pyrophosphatase from the vascular plant Arabidopsis thaliana in the yeast Saccharomyces cerevisiae results in the production of vacu polarly localized functional enzyme active in PPi-dependent H+ translocation.

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Acidic Residues Necessary for Pyrophosphate-energized Pumping and Inhibition of the Vacuolar H+-pyrophosphatase byN,N′-Dicyclohexylcarbodiimide*

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A hypothesis is formulated in which a physiological role for the mebrane-bound proton-translocating pyrophosphatase (H+-PPase) in some phototrophic bacteria is put forward, and granules containing pyroph phosphate (PPi) are proposed to be the source of hydrolyzable free PPi.